TY  - JOUR
AU  - Korićanac, Goran
AU  - Milosavljević, Tijana
AU  - Stojiljković, Mojca D.
AU  - Žakula, Zorica
AU  - Tepavčević, Snežana
AU  - Ribarac-Stepić, Nevena B.
AU  - Isenović, Esma R.
PY  - 2009
UR  - https://vinar.vin.bg.ac.rs/handle/123456789/3648
AB  - It is well known that variation in the concentration of estrogens affects insulin action. In this study we examine the impact of estradiol (E2) on insulin signaling in the rat heart. Ovariectomized female rats were treated with E2 6 h prior to analysis of basal protein and mRNA content of insulin signaling molecules, and additionally with insulin 30 min before the experiment to delineate E2 effects on phosphorylations and molecular associations relevant for insulin signaling. The results show that E2 decreased insulin receptor (IR) tyrosine phosphorylation, while it did not alter IR protein and mRNA content. E2 administration did not chance IR substrate 1 (IRS-1) protein content and tyrosine phosphorylation, while decreased mRNA content and increased its association with the p85 subunit of phosphatidylinositol 3-kinase (PI3K). E2 decreased protein and mRNA content of IR substrate 2 (IRS-2), while did not change IRS-2 tyrosine phosphorylation and IRS-2 association with p85. The increase of IRS-1/p85 is accompanied by increase of p85 protein and mRNA levels, and by stimulation of protein kinase B (Akt) Ser(473) phosphorylation. In contrast, Akt protein and mRNA content were not changed. In summary, although in some aspects cardiac insulin signaling is obviously improved by E2 treatment (increase of p85 mRNA and protein levels, enhancement of IRS-1/p85 association and Ser(473) Akt phosphorylation), the observed decrease of IR tyrosine phosphorylation, IRS-2 protein content, and IRSs mRNA contents, suggest very complex interplay of beneficial and suppressive effects of E2, both genomic and non-genomic, in regulation of heart insulin signaling. Copyright (C) 2009 John Wiley and Sons, Ltd.
T2  - Cell Biochemistry and Function
T1  - Impact of estradiol on insulin signaling in the rat heart
VL  - 27
IS  - 2
SP  - 102
EP  - 110
DO  - 10.1002/cbf.1542
ER  - 

@article{
author = "Korićanac, Goran and Milosavljević, Tijana and Stojiljković, Mojca D. and Žakula, Zorica and Tepavčević, Snežana and Ribarac-Stepić, Nevena B. and Isenović, Esma R.",
year = "2009",
abstract = "It is well known that variation in the concentration of estrogens affects insulin action. In this study we examine the impact of estradiol (E2) on insulin signaling in the rat heart. Ovariectomized female rats were treated with E2 6 h prior to analysis of basal protein and mRNA content of insulin signaling molecules, and additionally with insulin 30 min before the experiment to delineate E2 effects on phosphorylations and molecular associations relevant for insulin signaling. The results show that E2 decreased insulin receptor (IR) tyrosine phosphorylation, while it did not alter IR protein and mRNA content. E2 administration did not chance IR substrate 1 (IRS-1) protein content and tyrosine phosphorylation, while decreased mRNA content and increased its association with the p85 subunit of phosphatidylinositol 3-kinase (PI3K). E2 decreased protein and mRNA content of IR substrate 2 (IRS-2), while did not change IRS-2 tyrosine phosphorylation and IRS-2 association with p85. The increase of IRS-1/p85 is accompanied by increase of p85 protein and mRNA levels, and by stimulation of protein kinase B (Akt) Ser(473) phosphorylation. In contrast, Akt protein and mRNA content were not changed. In summary, although in some aspects cardiac insulin signaling is obviously improved by E2 treatment (increase of p85 mRNA and protein levels, enhancement of IRS-1/p85 association and Ser(473) Akt phosphorylation), the observed decrease of IR tyrosine phosphorylation, IRS-2 protein content, and IRSs mRNA contents, suggest very complex interplay of beneficial and suppressive effects of E2, both genomic and non-genomic, in regulation of heart insulin signaling. Copyright (C) 2009 John Wiley and Sons, Ltd.",
journal = "Cell Biochemistry and Function",
title = "Impact of estradiol on insulin signaling in the rat heart",
volume = "27",
number = "2",
pages = "102-110",
doi = "10.1002/cbf.1542"
}

Korićanac, G., Milosavljević, T., Stojiljković, M. D., Žakula, Z., Tepavčević, S., Ribarac-Stepić, N. B.,& Isenović, E. R.. (2009). Impact of estradiol on insulin signaling in the rat heart. in Cell Biochemistry and Function, 27(2), 102-110.
https://doi.org/10.1002/cbf.1542

Korićanac G, Milosavljević T, Stojiljković MD, Žakula Z, Tepavčević S, Ribarac-Stepić NB, Isenović ER. Impact of estradiol on insulin signaling in the rat heart. in Cell Biochemistry and Function. 2009;27(2):102-110.
doi:10.1002/cbf.1542 .

Korićanac, Goran, Milosavljević, Tijana, Stojiljković, Mojca D., Žakula, Zorica, Tepavčević, Snežana, Ribarac-Stepić, Nevena B., Isenović, Esma R., "Impact of estradiol on insulin signaling in the rat heart" in Cell Biochemistry and Function, 27, no. 2 (2009):102-110,
https://doi.org/10.1002/cbf.1542 . .

TY  - JOUR
AU  - Korićanac, Goran
AU  - Stojiljković, Mojca D.
AU  - Radivojša, Snežana
AU  - Žakula, Zorica
AU  - Ribarac-Stepić, Nevena B.
AU  - Isenović, Esma R.
PY  - 2008
UR  - https://vinar.vin.bg.ac.rs/handle/123456789/3365
AB  - The aim of this study was to examine the effects of dexamethasone (Dex) on functional properties of the rat insulin receptor (IR). Male Mill Hill hooded rats, 3, 6, 12, 18 and 21 months old, were injected with Dex (4 mg/kg) and rat liver and erythrocytes were used for experiments 18 h after Dex administration. Treatment with Dex lowered the specific binding (SB) of insulin ( INS) in the liver of 3- and 18-month-old rats and concentration of INS binding sites (N-1, N-2) and the dissociation constant of low-affinity binding sites (Kd(2)) in the liver of 6- and 18-month-old rats. In addition, Dex treatment lowered the liver IR protein level in all analyzed groups, except 21-month-old rats where it remained unchanged, but raised the IR mRNA level in 18-month-old rats. In erythrocytes, treatment with Dex decreased SB and Kd2 ( in animals 3 and 6 months old) and N1 ( in ones 3 and 18 months old). Following Dex treatment, the INS plasma level increased ( in rats 3, 18 and 21 months old), while glucose (Glu) concentration increased in 3 and 12 months old, but decreased in 6- and 21-month-old rats. In summary, Dex exerts the strongest effect on the erythrocyte IR of 3- and 6- month-old rats and the hepatic IR of 18-month-old rats. IR in both tissues is almost insensitive to Dex in 12- and 21-month-old rats. The pattern of age-related changes of IR induced by Dex does not correlate with changes of plasma Glu and INS.
T2  - Acta Biologica Hungarica
T1  - Effects of dexamethasone on insulin receptor in aging
VL  - 59
IS  - 1
SP  - 17
EP  - 29
DO  - 10.1556/ABiol.59.2008.1.2
ER  - 

@article{
author = "Korićanac, Goran and Stojiljković, Mojca D. and Radivojša, Snežana and Žakula, Zorica and Ribarac-Stepić, Nevena B. and Isenović, Esma R.",
year = "2008",
abstract = "The aim of this study was to examine the effects of dexamethasone (Dex) on functional properties of the rat insulin receptor (IR). Male Mill Hill hooded rats, 3, 6, 12, 18 and 21 months old, were injected with Dex (4 mg/kg) and rat liver and erythrocytes were used for experiments 18 h after Dex administration. Treatment with Dex lowered the specific binding (SB) of insulin ( INS) in the liver of 3- and 18-month-old rats and concentration of INS binding sites (N-1, N-2) and the dissociation constant of low-affinity binding sites (Kd(2)) in the liver of 6- and 18-month-old rats. In addition, Dex treatment lowered the liver IR protein level in all analyzed groups, except 21-month-old rats where it remained unchanged, but raised the IR mRNA level in 18-month-old rats. In erythrocytes, treatment with Dex decreased SB and Kd2 ( in animals 3 and 6 months old) and N1 ( in ones 3 and 18 months old). Following Dex treatment, the INS plasma level increased ( in rats 3, 18 and 21 months old), while glucose (Glu) concentration increased in 3 and 12 months old, but decreased in 6- and 21-month-old rats. In summary, Dex exerts the strongest effect on the erythrocyte IR of 3- and 6- month-old rats and the hepatic IR of 18-month-old rats. IR in both tissues is almost insensitive to Dex in 12- and 21-month-old rats. The pattern of age-related changes of IR induced by Dex does not correlate with changes of plasma Glu and INS.",
journal = "Acta Biologica Hungarica",
title = "Effects of dexamethasone on insulin receptor in aging",
volume = "59",
number = "1",
pages = "17-29",
doi = "10.1556/ABiol.59.2008.1.2"
}

Korićanac, G., Stojiljković, M. D., Radivojša, S., Žakula, Z., Ribarac-Stepić, N. B.,& Isenović, E. R.. (2008). Effects of dexamethasone on insulin receptor in aging. in Acta Biologica Hungarica, 59(1), 17-29.
https://doi.org/10.1556/ABiol.59.2008.1.2

Korićanac G, Stojiljković MD, Radivojša S, Žakula Z, Ribarac-Stepić NB, Isenović ER. Effects of dexamethasone on insulin receptor in aging. in Acta Biologica Hungarica. 2008;59(1):17-29.
doi:10.1556/ABiol.59.2008.1.2 .

Korićanac, Goran, Stojiljković, Mojca D., Radivojša, Snežana, Žakula, Zorica, Ribarac-Stepić, Nevena B., Isenović, Esma R., "Effects of dexamethasone on insulin receptor in aging" in Acta Biologica Hungarica, 59, no. 1 (2008):17-29,
https://doi.org/10.1556/ABiol.59.2008.1.2 . .

TY  - JOUR
AU  - Korićanac, Goran
AU  - Milosavljević, Tijana
AU  - Stojiljković, Mojca D.
AU  - Žakula, Zorica
AU  - Ribarac-Stepić, Nevena B.
AU  - Isenović, Esma R.
PY  - 2008
UR  - https://vinar.vin.bg.ac.rs/handle/123456789/3378
AB  - We used rat hepatic and uterine tissues to examine the impact of estradiol (E2) on insulin (INS) signaling. Ovariectotnized (OVX) female Wistar rats were treated with E2 (20 mu g/kg b.wt., i.p.) and used for the experiment 6 h after E2 administration. To highlight E2 effects on tyrosine phosphorylation of INS receptor (IR) and INS receptor substrates (IRSs) and IRSs association with p85 subunit of phosphatidylinositol 3-kinase (PI3-K) in the context of INS signaling, E2-treated OVX rats were also injected with INS (20 IU, i.p.), 30 min before the experiment. Treatment with E2 did not change the levels of plasma INS and glucose (Glu). However, it significantly decreased the free fatty acid (FFA) level and increased uterine weight. Furthermore, the results show that E2 had no effect on the content of hepatic IR protein, but significantly increased IR protein content in the uterus and decreased IR tyrosine phosphorylation in both the liver and uterus. Compared to the control, hepatic IRS-1 and IRS-2 were significantly decreased and increased, respectively, after E2 treatment. Protein content of both molecules, IRS-1 and IRS-2, was increased in uterine tissue after E2 administration. Protein content of the p85 subunit of PI3-K and that of protein kinase B (Akt) were increased in the uterus, with no changes in the liver. The results suggest that E2 treatment induces tissue-specific changes in INS signaling. The consequences of E2 treatment on INS signaling molecules are more apparent in the uterus, but their physiological relevance for INS action is probably greater in the liver. (c) 2007 Elsevier Ltd. All rights reserved.
T2  - Journal of Steroid Biochemistry and Molecular Biology
T1  - Insulin signaling in the liver and uterus of ovariectomized rats treated with estradiol
VL  - 108
IS  - 1-2
SP  - 109
EP  - 116
DO  - 10.1016/j.jsbmb.2007.06.001
ER  - 

@article{
author = "Korićanac, Goran and Milosavljević, Tijana and Stojiljković, Mojca D. and Žakula, Zorica and Ribarac-Stepić, Nevena B. and Isenović, Esma R.",
year = "2008",
abstract = "We used rat hepatic and uterine tissues to examine the impact of estradiol (E2) on insulin (INS) signaling. Ovariectotnized (OVX) female Wistar rats were treated with E2 (20 mu g/kg b.wt., i.p.) and used for the experiment 6 h after E2 administration. To highlight E2 effects on tyrosine phosphorylation of INS receptor (IR) and INS receptor substrates (IRSs) and IRSs association with p85 subunit of phosphatidylinositol 3-kinase (PI3-K) in the context of INS signaling, E2-treated OVX rats were also injected with INS (20 IU, i.p.), 30 min before the experiment. Treatment with E2 did not change the levels of plasma INS and glucose (Glu). However, it significantly decreased the free fatty acid (FFA) level and increased uterine weight. Furthermore, the results show that E2 had no effect on the content of hepatic IR protein, but significantly increased IR protein content in the uterus and decreased IR tyrosine phosphorylation in both the liver and uterus. Compared to the control, hepatic IRS-1 and IRS-2 were significantly decreased and increased, respectively, after E2 treatment. Protein content of both molecules, IRS-1 and IRS-2, was increased in uterine tissue after E2 administration. Protein content of the p85 subunit of PI3-K and that of protein kinase B (Akt) were increased in the uterus, with no changes in the liver. The results suggest that E2 treatment induces tissue-specific changes in INS signaling. The consequences of E2 treatment on INS signaling molecules are more apparent in the uterus, but their physiological relevance for INS action is probably greater in the liver. (c) 2007 Elsevier Ltd. All rights reserved.",
journal = "Journal of Steroid Biochemistry and Molecular Biology",
title = "Insulin signaling in the liver and uterus of ovariectomized rats treated with estradiol",
volume = "108",
number = "1-2",
pages = "109-116",
doi = "10.1016/j.jsbmb.2007.06.001"
}

Korićanac, G., Milosavljević, T., Stojiljković, M. D., Žakula, Z., Ribarac-Stepić, N. B.,& Isenović, E. R.. (2008). Insulin signaling in the liver and uterus of ovariectomized rats treated with estradiol. in Journal of Steroid Biochemistry and Molecular Biology, 108(1-2), 109-116.
https://doi.org/10.1016/j.jsbmb.2007.06.001

Korićanac G, Milosavljević T, Stojiljković MD, Žakula Z, Ribarac-Stepić NB, Isenović ER. Insulin signaling in the liver and uterus of ovariectomized rats treated with estradiol. in Journal of Steroid Biochemistry and Molecular Biology. 2008;108(1-2):109-116.
doi:10.1016/j.jsbmb.2007.06.001 .

Korićanac, Goran, Milosavljević, Tijana, Stojiljković, Mojca D., Žakula, Zorica, Ribarac-Stepić, Nevena B., Isenović, Esma R., "Insulin signaling in the liver and uterus of ovariectomized rats treated with estradiol" in Journal of Steroid Biochemistry and Molecular Biology, 108, no. 1-2 (2008):109-116,
https://doi.org/10.1016/j.jsbmb.2007.06.001 . .

TY  - JOUR
AU  - Isenović, Esma R.
AU  - Žakula, Zorica
AU  - Korićanac, Goran
AU  - Ribarac-Stepić, Nevena B.
PY  - 2008
UR  - https://vinar.vin.bg.ac.rs/handle/123456789/3422
AB  - This investigation addresses the interaction of insulin (INS) and glucocorticoid (GC) signaling in the hepatic regulation of tryptophan oxygenase (TO) enzyme activity in the rat. Male Wistar rats (200-250 g b.w) received an injection of the different doses of INS (10, 25, 50, 70 and 100 pg/200 g b.w., i.p.) and were used for experiments 3 h and 18 h after INS administration. This study shows that maximum of TO activity was found at dose of 50 mu g of INS with peak increases observed at 3 h and 18 h after injection of INS, while INS had no effect on TO activity in adrenalectomized rats. The analysis of INS effects on glucocorticoid receptor-complex (GC/GR complex) stability shows that complexes from INS-treated rats are less stable than those from control animals. In addition, INS-stimulated stability of glucocorticoid receptor (GR) protein was significantly increased from the controls. Furthermore, the results show that GC/GR complexes from INS-treated rats could be activated and accumulated at higher rate in cell nuclei of control animals. These data support the involvement of INS in modulation of GC signaling pathway which mediates, in part, the activity of TO.
T2  - Physiological Research
T1  - Comparative analysis of tryptophan oxygenase activity and glucocorticoid receptor under the influence of insulin
VL  - 57
IS  - 1
SP  - 101
EP  - 107
UR  - https://hdl.handle.net/21.15107/rcub_vinar_3422
ER  - 

@article{
author = "Isenović, Esma R. and Žakula, Zorica and Korićanac, Goran and Ribarac-Stepić, Nevena B.",
year = "2008",
abstract = "This investigation addresses the interaction of insulin (INS) and glucocorticoid (GC) signaling in the hepatic regulation of tryptophan oxygenase (TO) enzyme activity in the rat. Male Wistar rats (200-250 g b.w) received an injection of the different doses of INS (10, 25, 50, 70 and 100 pg/200 g b.w., i.p.) and were used for experiments 3 h and 18 h after INS administration. This study shows that maximum of TO activity was found at dose of 50 mu g of INS with peak increases observed at 3 h and 18 h after injection of INS, while INS had no effect on TO activity in adrenalectomized rats. The analysis of INS effects on glucocorticoid receptor-complex (GC/GR complex) stability shows that complexes from INS-treated rats are less stable than those from control animals. In addition, INS-stimulated stability of glucocorticoid receptor (GR) protein was significantly increased from the controls. Furthermore, the results show that GC/GR complexes from INS-treated rats could be activated and accumulated at higher rate in cell nuclei of control animals. These data support the involvement of INS in modulation of GC signaling pathway which mediates, in part, the activity of TO.",
journal = "Physiological Research",
title = "Comparative analysis of tryptophan oxygenase activity and glucocorticoid receptor under the influence of insulin",
volume = "57",
number = "1",
pages = "101-107",
url = "https://hdl.handle.net/21.15107/rcub_vinar_3422"
}

Isenović, E. R., Žakula, Z., Korićanac, G.,& Ribarac-Stepić, N. B.. (2008). Comparative analysis of tryptophan oxygenase activity and glucocorticoid receptor under the influence of insulin. in Physiological Research, 57(1), 101-107.
https://hdl.handle.net/21.15107/rcub_vinar_3422

Isenović ER, Žakula Z, Korićanac G, Ribarac-Stepić NB. Comparative analysis of tryptophan oxygenase activity and glucocorticoid receptor under the influence of insulin. in Physiological Research. 2008;57(1):101-107.
https://hdl.handle.net/21.15107/rcub_vinar_3422 .

Isenović, Esma R., Žakula, Zorica, Korićanac, Goran, Ribarac-Stepić, Nevena B., "Comparative analysis of tryptophan oxygenase activity and glucocorticoid receptor under the influence of insulin" in Physiological Research, 57, no. 1 (2008):101-107,
https://hdl.handle.net/21.15107/rcub_vinar_3422 .

TY  - JOUR
AU  - Žakula, Zorica
AU  - Isenović, Esma R.
AU  - Stojiljković, Mojca D.
AU  - Tepavčević, Snežana
AU  - Ribarac-Stepić, Nevena B.
PY  - 2007
UR  - https://vinar.vin.bg.ac.rs/handle/123456789/3412
AB  - The aim of this study was to examine the effects of estradiol (E2) on activity of RNA polymerase I and RNA polymerase II in uterine nuclei of ovariectomized (OVX) female rats. The obtained results show that estrogen-receptor (E-R) complexes in 30 min induced an increase of polymerase II activity. A second increase of polymerase II activity was observed after 3 h-incubation of nuclei with the E-R complex formed in the cytosol fraction. However, activity of polymerase I was increased 2 h after the start of incubation, with highest activity detected at 3 h in nuclei incubated with E-R complexes. On the contrary, no stimulatory effect on either polymerase I or polymerase II activity was observed in nuclei incubated with E2 alone. These results indicate that E2 stimulates the cytosolic estrogen receptor (ER), which in turn causes uterotrophic responses in OVX rats. In addition, they suggest that in order to provoke uterotrophic responses E-R complexes formed in the cytosol need to be retained in the nucleus for a longer period of time.
T2  - Archives of Biological Sciences
T1  - Estrogen-induced modification of uterine RNA polymerase activity depends on localization of the estrogen receptor
VL  - 59
IS  - 2
SP  - 105
EP  - 112
DO  - 10.2298/ABS0702105Z
ER  - 

@article{
author = "Žakula, Zorica and Isenović, Esma R. and Stojiljković, Mojca D. and Tepavčević, Snežana and Ribarac-Stepić, Nevena B.",
year = "2007",
abstract = "The aim of this study was to examine the effects of estradiol (E2) on activity of RNA polymerase I and RNA polymerase II in uterine nuclei of ovariectomized (OVX) female rats. The obtained results show that estrogen-receptor (E-R) complexes in 30 min induced an increase of polymerase II activity. A second increase of polymerase II activity was observed after 3 h-incubation of nuclei with the E-R complex formed in the cytosol fraction. However, activity of polymerase I was increased 2 h after the start of incubation, with highest activity detected at 3 h in nuclei incubated with E-R complexes. On the contrary, no stimulatory effect on either polymerase I or polymerase II activity was observed in nuclei incubated with E2 alone. These results indicate that E2 stimulates the cytosolic estrogen receptor (ER), which in turn causes uterotrophic responses in OVX rats. In addition, they suggest that in order to provoke uterotrophic responses E-R complexes formed in the cytosol need to be retained in the nucleus for a longer period of time.",
journal = "Archives of Biological Sciences",
title = "Estrogen-induced modification of uterine RNA polymerase activity depends on localization of the estrogen receptor",
volume = "59",
number = "2",
pages = "105-112",
doi = "10.2298/ABS0702105Z"
}

Žakula, Z., Isenović, E. R., Stojiljković, M. D., Tepavčević, S.,& Ribarac-Stepić, N. B.. (2007). Estrogen-induced modification of uterine RNA polymerase activity depends on localization of the estrogen receptor. in Archives of Biological Sciences, 59(2), 105-112.
https://doi.org/10.2298/ABS0702105Z

Žakula Z, Isenović ER, Stojiljković MD, Tepavčević S, Ribarac-Stepić NB. Estrogen-induced modification of uterine RNA polymerase activity depends on localization of the estrogen receptor. in Archives of Biological Sciences. 2007;59(2):105-112.
doi:10.2298/ABS0702105Z .

Žakula, Zorica, Isenović, Esma R., Stojiljković, Mojca D., Tepavčević, Snežana, Ribarac-Stepić, Nevena B., "Estrogen-induced modification of uterine RNA polymerase activity depends on localization of the estrogen receptor" in Archives of Biological Sciences, 59, no. 2 (2007):105-112,
https://doi.org/10.2298/ABS0702105Z . .

TY  - JOUR
AU  - Jovanovic-Santa, S
AU  - Petrović, Julijana
AU  - Sakac, M
AU  - Žakula, Zorica
AU  - Isenović, Esma R.
AU  - Ribarac-Stepić, Nevena B.
PY  - 2006
UR  - https://vinar.vin.bg.ac.rs/handle/123456789/3007
AB  - Since many of newly synthesised D-secoestratriene derivatives showed antiestrogenic effect, with almost a total loss of estrogenic activity, we studied the effects of some of these compounds on estrogen receptors (ER), the translocation of the estrogen-ER complexes formed in presence of competing substances into the nucleus, as well as the binding of these complexes to DNA. The results of uterotrophic effects of analysed derivatives are in agreement with the influence of these compounds on activity and binding parameters of estrogen receptors. Namely, compounds that show relatively high antiestrogenic activity predominantly increase K-d and inhibit translocation to nuclei of radioactive complexes formed in their presence. On the other hand, compounds that do not significantly change binding parameters of estrogen receptors do not show antiestrogenic effect in in vivo experiments.
T2  - Collection of Czechoslovak Chemical Communications
T1  - The influence of 17-oxo- and 17-hydroxy-16,17-secoestratriene derivatives on estrogen receptor
VL  - 71
IS  - 4
SP  - 532
EP  - 542
DO  - 10.1135/cccc20060532
ER  - 

@article{
author = "Jovanovic-Santa, S and Petrović, Julijana and Sakac, M and Žakula, Zorica and Isenović, Esma R. and Ribarac-Stepić, Nevena B.",
year = "2006",
abstract = "Since many of newly synthesised D-secoestratriene derivatives showed antiestrogenic effect, with almost a total loss of estrogenic activity, we studied the effects of some of these compounds on estrogen receptors (ER), the translocation of the estrogen-ER complexes formed in presence of competing substances into the nucleus, as well as the binding of these complexes to DNA. The results of uterotrophic effects of analysed derivatives are in agreement with the influence of these compounds on activity and binding parameters of estrogen receptors. Namely, compounds that show relatively high antiestrogenic activity predominantly increase K-d and inhibit translocation to nuclei of radioactive complexes formed in their presence. On the other hand, compounds that do not significantly change binding parameters of estrogen receptors do not show antiestrogenic effect in in vivo experiments.",
journal = "Collection of Czechoslovak Chemical Communications",
title = "The influence of 17-oxo- and 17-hydroxy-16,17-secoestratriene derivatives on estrogen receptor",
volume = "71",
number = "4",
pages = "532-542",
doi = "10.1135/cccc20060532"
}

Jovanovic-Santa, S., Petrović, J., Sakac, M., Žakula, Z., Isenović, E. R.,& Ribarac-Stepić, N. B.. (2006). The influence of 17-oxo- and 17-hydroxy-16,17-secoestratriene derivatives on estrogen receptor. in Collection of Czechoslovak Chemical Communications, 71(4), 532-542.
https://doi.org/10.1135/cccc20060532

Jovanovic-Santa S, Petrović J, Sakac M, Žakula Z, Isenović ER, Ribarac-Stepić NB. The influence of 17-oxo- and 17-hydroxy-16,17-secoestratriene derivatives on estrogen receptor. in Collection of Czechoslovak Chemical Communications. 2006;71(4):532-542.
doi:10.1135/cccc20060532 .

Jovanovic-Santa, S, Petrović, Julijana, Sakac, M, Žakula, Zorica, Isenović, Esma R., Ribarac-Stepić, Nevena B., "The influence of 17-oxo- and 17-hydroxy-16,17-secoestratriene derivatives on estrogen receptor" in Collection of Czechoslovak Chemical Communications, 71, no. 4 (2006):532-542,
https://doi.org/10.1135/cccc20060532 . .

TY  - JOUR
AU  - Isenović, Esma R.
AU  - Žakula, Zorica
AU  - Korićanac, Goran
AU  - Ribarac-Stepić, Nevena B.
PY  - 2006
UR  - https://vinar.vin.bg.ac.rs/handle/123456789/2982
AB  - This investigation used cytosol fraction of rat liver to examine the effects of insulin ( INS) on functional properties of glucocorticoid receptor ( GR). Male Wistar rats ( 220 - 250 g b.wt.) were injected with INS ( 50 mu g/200 g b.wt, i.p.) and 18 h after INS administration used for experiments. INS-stimulated dissociation of G-R complexes was significantly increased by 133% compared to control level. However, INS treatment significantly stimulated stability of GR protein by 138% above control value. Furthermore, results show that INS stimulated activation of formed cytosol [ H-3] TA-R complexes by 143% in respect to control. [ H-3] TA-R complexes from INS treated animals could be activated and accumulated at higher rate in cell nuclei of control animals. The physiological relevance of the data was confirmed by INS-related stimulation of Tryptophan oxigenase ( TO) activity. It was observed that INS stimulated TO activity while INS injected to adrenalectomized rats, exhibited less effects compared to control. The results indicate that a glucocorticoid hormone ( CORT) enhances INS induced stimulation of TO activity, as evidenced by enhanced enzyme activity. Presented data suggest: that INS treatment leads to modifications of the GR protein and the nuclear components and that INS activates the rat liver CORT signaling pathway which mediates, in part, the activity of TO.
T2  - Acta Biologica Hungarica
T1  - Insulin modulates rat liver glucocorticoid receptor
VL  - 57
IS  - 1
SP  - 37
EP  - 48
DO  - 10.1556/ABiol.57.2006.1.4
ER  - 

@article{
author = "Isenović, Esma R. and Žakula, Zorica and Korićanac, Goran and Ribarac-Stepić, Nevena B.",
year = "2006",
abstract = "This investigation used cytosol fraction of rat liver to examine the effects of insulin ( INS) on functional properties of glucocorticoid receptor ( GR). Male Wistar rats ( 220 - 250 g b.wt.) were injected with INS ( 50 mu g/200 g b.wt, i.p.) and 18 h after INS administration used for experiments. INS-stimulated dissociation of G-R complexes was significantly increased by 133% compared to control level. However, INS treatment significantly stimulated stability of GR protein by 138% above control value. Furthermore, results show that INS stimulated activation of formed cytosol [ H-3] TA-R complexes by 143% in respect to control. [ H-3] TA-R complexes from INS treated animals could be activated and accumulated at higher rate in cell nuclei of control animals. The physiological relevance of the data was confirmed by INS-related stimulation of Tryptophan oxigenase ( TO) activity. It was observed that INS stimulated TO activity while INS injected to adrenalectomized rats, exhibited less effects compared to control. The results indicate that a glucocorticoid hormone ( CORT) enhances INS induced stimulation of TO activity, as evidenced by enhanced enzyme activity. Presented data suggest: that INS treatment leads to modifications of the GR protein and the nuclear components and that INS activates the rat liver CORT signaling pathway which mediates, in part, the activity of TO.",
journal = "Acta Biologica Hungarica",
title = "Insulin modulates rat liver glucocorticoid receptor",
volume = "57",
number = "1",
pages = "37-48",
doi = "10.1556/ABiol.57.2006.1.4"
}

Isenović, E. R., Žakula, Z., Korićanac, G.,& Ribarac-Stepić, N. B.. (2006). Insulin modulates rat liver glucocorticoid receptor. in Acta Biologica Hungarica, 57(1), 37-48.
https://doi.org/10.1556/ABiol.57.2006.1.4

Isenović ER, Žakula Z, Korićanac G, Ribarac-Stepić NB. Insulin modulates rat liver glucocorticoid receptor. in Acta Biologica Hungarica. 2006;57(1):37-48.
doi:10.1556/ABiol.57.2006.1.4 .

Isenović, Esma R., Žakula, Zorica, Korićanac, Goran, Ribarac-Stepić, Nevena B., "Insulin modulates rat liver glucocorticoid receptor" in Acta Biologica Hungarica, 57, no. 1 (2006):37-48,
https://doi.org/10.1556/ABiol.57.2006.1.4 . .

TY  - JOUR
AU  - Korićanac, Goran
AU  - Isenović, Esma R.
AU  - Stojanovic-Susulic, V
AU  - Miskovic, D
AU  - Žakula, Zorica
AU  - Ribarac-Stepić, Nevena B.
PY  - 2006
UR  - https://vinar.vin.bg.ac.rs/handle/123456789/3023
AB  - The effects of glucocorticoid excess on regulation of insulin receptors were investigated in dexamethasone-treated rats. Glucocorticoid excess was produced by administration of dexamethasone (0.5 mg/100 g b.w.) 30 min, 4, 12, 18, 24, 42 or 70 h before experiments. This treatment caused time-dependent changes of glucose and insulin concentration in blood, as well as in amounts of specific insulin binding and insulin receptors of liver cells and erythrocytes. The time intervals in which dexamethasone produced the increase in insulin concentration were accompanied with decrease in insulin binding to receptors in membranes of liver cells, while significant changes in insulin binding to receptors of erythrocytes were not observed under the same experimental conditions. The effect is maximal 18 and 42 h after dexamethasone treatment that increase insulin blood level by about 85% and 60%, respectively. Receptor analysis revealed that changes in specific binding of insulin could be due to significant changes in amount of binding sites on cell surface rather than to mild alteration in receptor affinity. These findings suggest that besides the changes in insulin level, the alterations in insulin receptor number and affinity may play a major role in the states of altered insulin sensitivity which accompany glucocorticoid excess.
T2  - General Physiology and Biophysics
T1  - Time dependent effects of dexamethasone on serum insulin level and insulin receptors in rat liver and erythrocytes
VL  - 25
IS  - 1
SP  - 11
EP  - 24
UR  - https://hdl.handle.net/21.15107/rcub_vinar_3023
ER  - 

@article{
author = "Korićanac, Goran and Isenović, Esma R. and Stojanovic-Susulic, V and Miskovic, D and Žakula, Zorica and Ribarac-Stepić, Nevena B.",
year = "2006",
abstract = "The effects of glucocorticoid excess on regulation of insulin receptors were investigated in dexamethasone-treated rats. Glucocorticoid excess was produced by administration of dexamethasone (0.5 mg/100 g b.w.) 30 min, 4, 12, 18, 24, 42 or 70 h before experiments. This treatment caused time-dependent changes of glucose and insulin concentration in blood, as well as in amounts of specific insulin binding and insulin receptors of liver cells and erythrocytes. The time intervals in which dexamethasone produced the increase in insulin concentration were accompanied with decrease in insulin binding to receptors in membranes of liver cells, while significant changes in insulin binding to receptors of erythrocytes were not observed under the same experimental conditions. The effect is maximal 18 and 42 h after dexamethasone treatment that increase insulin blood level by about 85% and 60%, respectively. Receptor analysis revealed that changes in specific binding of insulin could be due to significant changes in amount of binding sites on cell surface rather than to mild alteration in receptor affinity. These findings suggest that besides the changes in insulin level, the alterations in insulin receptor number and affinity may play a major role in the states of altered insulin sensitivity which accompany glucocorticoid excess.",
journal = "General Physiology and Biophysics",
title = "Time dependent effects of dexamethasone on serum insulin level and insulin receptors in rat liver and erythrocytes",
volume = "25",
number = "1",
pages = "11-24",
url = "https://hdl.handle.net/21.15107/rcub_vinar_3023"
}

Korićanac, G., Isenović, E. R., Stojanovic-Susulic, V., Miskovic, D., Žakula, Z.,& Ribarac-Stepić, N. B.. (2006). Time dependent effects of dexamethasone on serum insulin level and insulin receptors in rat liver and erythrocytes. in General Physiology and Biophysics, 25(1), 11-24.
https://hdl.handle.net/21.15107/rcub_vinar_3023

Korićanac G, Isenović ER, Stojanovic-Susulic V, Miskovic D, Žakula Z, Ribarac-Stepić NB. Time dependent effects of dexamethasone on serum insulin level and insulin receptors in rat liver and erythrocytes. in General Physiology and Biophysics. 2006;25(1):11-24.
https://hdl.handle.net/21.15107/rcub_vinar_3023 .

Korićanac, Goran, Isenović, Esma R., Stojanovic-Susulic, V, Miskovic, D, Žakula, Zorica, Ribarac-Stepić, Nevena B., "Time dependent effects of dexamethasone on serum insulin level and insulin receptors in rat liver and erythrocytes" in General Physiology and Biophysics, 25, no. 1 (2006):11-24,
https://hdl.handle.net/21.15107/rcub_vinar_3023 .

TY  - CONF
AU  - Korićanac, Goran
AU  - Vulović, Mojca D.
AU  - Milosavljevic, T
AU  - Žakula, Zorica
AU  - Ribarac-Stepić, Nevena B.
PY  - 2005
UR  - https://vinar.vin.bg.ac.rs/handle/123456789/6564
C3  - FEBS Journal
T1  - The effect of 17 beta-estradiol on the content of insulin signaling molecules in liver and uterus of ovariectomized rats
VL  - 272
SP  - 221
EP  - 222
UR  - https://hdl.handle.net/21.15107/rcub_vinar_6564
ER  - 

@conference{
author = "Korićanac, Goran and Vulović, Mojca D. and Milosavljevic, T and Žakula, Zorica and Ribarac-Stepić, Nevena B.",
year = "2005",
journal = "FEBS Journal",
title = "The effect of 17 beta-estradiol on the content of insulin signaling molecules in liver and uterus of ovariectomized rats",
volume = "272",
pages = "221-222",
url = "https://hdl.handle.net/21.15107/rcub_vinar_6564"
}

Korićanac, G., Vulović, M. D., Milosavljevic, T., Žakula, Z.,& Ribarac-Stepić, N. B.. (2005). The effect of 17 beta-estradiol on the content of insulin signaling molecules in liver and uterus of ovariectomized rats. in FEBS Journal, 272, 221-222.
https://hdl.handle.net/21.15107/rcub_vinar_6564

Korićanac G, Vulović MD, Milosavljevic T, Žakula Z, Ribarac-Stepić NB. The effect of 17 beta-estradiol on the content of insulin signaling molecules in liver and uterus of ovariectomized rats. in FEBS Journal. 2005;272:221-222.
https://hdl.handle.net/21.15107/rcub_vinar_6564 .

Korićanac, Goran, Vulović, Mojca D., Milosavljevic, T, Žakula, Zorica, Ribarac-Stepić, Nevena B., "The effect of 17 beta-estradiol on the content of insulin signaling molecules in liver and uterus of ovariectomized rats" in FEBS Journal, 272 (2005):221-222,
https://hdl.handle.net/21.15107/rcub_vinar_6564 .

TY  - JOUR
AU  - Ribarac-Stepić, Nevena B.
AU  - Đurica, Snežana N.
AU  - Žakula, Zorica
AU  - Korićanac, Goran
AU  - Milošević, Dragoslav P.
PY  - 2005
UR  - http://www.doiserbia.nb.rs/Article.aspx?ID=0370-817905061R
UR  - https://vinar.vin.bg.ac.rs/handle/123456789/7805
AB  - Glucocorticoid hormones are involved in regulation of cell processes and coordinate physiological response to diverse signals. These hormones, through interaction with specific intracellular receptors, coordinate components of physiological repertoires by activating the expression of gene networks. Thus hormone-receptor complexes may function as key constituent in regulation of specific cell functions as well as in provoking differentiation in already determined cells. Analysis of steroid receptors are important for understanding of molecular details of transcriptional control as well as providing the insight as to how an individual transcriptional factor such as glucocorticoid receptor, contributes to cell identity and function. The purpose of this review is to establish the general molecular mechanism of glucocorticoid action and mechanism associated hormone-receptor complexes with the control of differential patterns (i.e. "positive" and "negative") of gene expression. One of the examples of two signal pathways regulating opposite gene expression are NF-kB and GR-mediated signal pathways. These pathways have important and opposite roles in the immune function. NF-kB is transcription factor which induces the expression of many genes that participate in immune and inflamatory response, while GR is transcription factor that serves as antiinflammatory agent and immune suppressor. Their interactions within the cell, although not yet completely understood, appear to be an important, possibly even the primary mechanism of immune homeostasis. It has not been established that glucocorticoid sensitivity can be caused by mechanisms other than changes of GR number and properties, although recent studies have indicated that receptor isoforms and transcriptional factors may modulate glucocorticoid responsiveness by interacting with receptor protein or directly at the site of DNA binding. The aim of this review is also to describe the role of glucocorticoid receptors in mechanism of glucocorticoid action on cell functions, including immune responses, as well as to present emerging issues on clinical aspects of molecular mechanisms of glucocorticoid action.
T2  - Srpski arhiv za celokupno lekarstvo
T1  - Molecular basis of glucocorticoid action
T1  - Молекулска основа деловања гликокортикоида
VL  - 133
IS  - Suppl. 1
SP  - 61
EP  - 66
DO  - 10.2298/SARH05S1061R
ER  - 

@article{
author = "Ribarac-Stepić, Nevena B. and Đurica, Snežana N. and Žakula, Zorica and Korićanac, Goran and Milošević, Dragoslav P.",
year = "2005",
abstract = "Glucocorticoid hormones are involved in regulation of cell processes and coordinate physiological response to diverse signals. These hormones, through interaction with specific intracellular receptors, coordinate components of physiological repertoires by activating the expression of gene networks. Thus hormone-receptor complexes may function as key constituent in regulation of specific cell functions as well as in provoking differentiation in already determined cells. Analysis of steroid receptors are important for understanding of molecular details of transcriptional control as well as providing the insight as to how an individual transcriptional factor such as glucocorticoid receptor, contributes to cell identity and function. The purpose of this review is to establish the general molecular mechanism of glucocorticoid action and mechanism associated hormone-receptor complexes with the control of differential patterns (i.e. "positive" and "negative") of gene expression. One of the examples of two signal pathways regulating opposite gene expression are NF-kB and GR-mediated signal pathways. These pathways have important and opposite roles in the immune function. NF-kB is transcription factor which induces the expression of many genes that participate in immune and inflamatory response, while GR is transcription factor that serves as antiinflammatory agent and immune suppressor. Their interactions within the cell, although not yet completely understood, appear to be an important, possibly even the primary mechanism of immune homeostasis. It has not been established that glucocorticoid sensitivity can be caused by mechanisms other than changes of GR number and properties, although recent studies have indicated that receptor isoforms and transcriptional factors may modulate glucocorticoid responsiveness by interacting with receptor protein or directly at the site of DNA binding. The aim of this review is also to describe the role of glucocorticoid receptors in mechanism of glucocorticoid action on cell functions, including immune responses, as well as to present emerging issues on clinical aspects of molecular mechanisms of glucocorticoid action.",
journal = "Srpski arhiv za celokupno lekarstvo",
title = "Molecular basis of glucocorticoid action, Молекулска основа деловања гликокортикоида",
volume = "133",
number = "Suppl. 1",
pages = "61-66",
doi = "10.2298/SARH05S1061R"
}

Ribarac-Stepić, N. B., Đurica, S. N., Žakula, Z., Korićanac, G.,& Milošević, D. P.. (2005). Molecular basis of glucocorticoid action. in Srpski arhiv za celokupno lekarstvo, 133(Suppl. 1), 61-66.
https://doi.org/10.2298/SARH05S1061R

Ribarac-Stepić NB, Đurica SN, Žakula Z, Korićanac G, Milošević DP. Molecular basis of glucocorticoid action. in Srpski arhiv za celokupno lekarstvo. 2005;133(Suppl. 1):61-66.
doi:10.2298/SARH05S1061R .

Ribarac-Stepić, Nevena B., Đurica, Snežana N., Žakula, Zorica, Korićanac, Goran, Milošević, Dragoslav P., "Molecular basis of glucocorticoid action" in Srpski arhiv za celokupno lekarstvo, 133, no. Suppl. 1 (2005):61-66,
https://doi.org/10.2298/SARH05S1061R . .

TY  - JOUR
AU  - Ribarac-Stepić, Nevena B.
AU  - Đurica, Snežana N.
AU  - Žakula, Zorica
AU  - Korićanac, Goran
AU  - Milošević, Dragoslav P.
PY  - 2005
UR  - http://www.doiserbia.nb.rs/Article.aspx?ID=0370-817905061R
UR  - https://vinar.vin.bg.ac.rs/handle/123456789/7825
AB  - Glucocorticoid hormones are involved in regulation of cell processes and coordinate physiological response to diverse signals. These hormones, through interaction with specific intracellular receptors, coordinate components of physiological repertoires by activating the expression of gene networks. Thus hormone-receptor complexes may function as key constituent in regulation of specific cell functions as well as in provoking differentiation in already determined cells. Analysis of steroid receptors are important for understanding of molecular details of transcriptional control as well as providing the insight as to how an individual transcriptional factor such as glucocorticoid receptor, contributes to cell identity and function. The purpose of this review is to establish the general molecular mechanism of glucocorticoid action and mechanism associated hormone-receptor complexes with the control of differential patterns (i.e. "positive" and "negative") of gene expression. One of the examples of two signal pathways regulating opposite gene expression are NF-kB and GR-mediated signal pathways. These pathways have important and opposite roles in the immune function. NF-kB is transcription factor which induces the expression of many genes that participate in immune and inflamatory response, while GR is transcription factor that serves as antiinflammatory agent and immune suppressor. Their interactions within the cell, although not yet completely understood, appear to be an important, possibly even the primary mechanism of immune homeostasis. It has not been established that glucocorticoid sensitivity can be caused by mechanisms other than changes of GR number and properties, although recent studies have indicated that receptor isoforms and transcriptional factors may modulate glucocorticoid responsiveness by interacting with receptor protein or directly at the site of DNA binding. The aim of this review is also to describe the role of glucocorticoid receptors in mechanism of glucocorticoid action on cell functions, including immune responses, as well as to present emerging issues on clinical aspects of molecular mechanisms of glucocorticoid action.
AB  - Glikokortikoidni hormoni su uključeni u regulaciju ćelijskih procesa koji koordiniraju fiziološke odgovore na različite signale. Ovi hormoni u kompleksu sa specifičnim ćelijskim receptorima preko aktivacije ekspresije mreže različitih gena učestvuju u koordinaciji komponenti koje su u osnovi fizioloških odgovora. Na taj način kompleksi hormona i receptora funkcionišu kao ključni faktor u regulaciji specifičnih ćelijskih funkcija, a takođe podstiču i procese diferencijacije u već determinisanim ćelijama. Analize glikokortikoidnih receptora (GR) su značajne, kako za bolje upoznavanje transkripcione kontrole, tako i za objašnjenje kako pojedini transkripcioni faktori, kao što su GR, doprinose identitetu ćelije i njenom funkcionisanju. U ovom radu su prikazani opšti principi molekulskog mehanizma delovanja glikokortikoida, kao i mehanizmi koji povezuju komplekse hormona i receptora sa kontrolom različitog tipa („pozitivnom” ili „negativnom”) genske ekspresije. Jedan od primera za signalne puteve koji suprotno regulišu aktivnost gena su nukleusni faktor kapaB (NFκB) i signalni putevi posredovani sa GR. Ovi putevi imaju suprotne uloge u regulaciji funkcionisanja imunskog sistema. NFκB je transkripcioni faktor koji indukuje ekspresiju gena uključenih u imunske i zapaljenjske procese. GR je takođe transkripcioni faktor, ali deluje kao antiinflamacioni i imunosupresivni agens. Njihove interakcije su značajne u ćelijama imunskog sistema, iako još nisu potpuno objašnjene; one su možda čak i primarne u mehanizmu imunske homeostaze. Do sada nije dokazano da ćelijska senzitivnost na delovanje glikokortikoida zavisi od mehanizama koji ne uključuju promene količine i funkcionalnih osobina GR. Međutim, novija istraživanja pokazuju da izoforme receptora i transkripcioni faktori mogu da menjaju ćelijski odgovor na glikokortikoide preko interakcije sa receptornim proteinom ili direktno sa mestima vezivanja na DNK. U ovom radu su takođe prikazani podaci iz literature o ključnoj ulozi glikokortikoidnih receptora u mehanizmu delovanja glikokortikoida u regulaciji ćelijskih funkcija, uključujući i ćelije imunskog sistema, kao i podaci o kliničkim aspektima molekulskog delovanja glikokortikoida.
T2  - Srpski arhiv za celokupno lekarstvo
T1  - Molecular basis of glucocorticoid action
T1  - Molekulska osnova delovanja glikokortikoida
VL  - 133
IS  - Suppl. 1
SP  - 61
EP  - 66
DO  - 10.2298/SARH05S1061R
ER  - 

@article{
author = "Ribarac-Stepić, Nevena B. and Đurica, Snežana N. and Žakula, Zorica and Korićanac, Goran and Milošević, Dragoslav P.",
year = "2005",
abstract = "Glucocorticoid hormones are involved in regulation of cell processes and coordinate physiological response to diverse signals. These hormones, through interaction with specific intracellular receptors, coordinate components of physiological repertoires by activating the expression of gene networks. Thus hormone-receptor complexes may function as key constituent in regulation of specific cell functions as well as in provoking differentiation in already determined cells. Analysis of steroid receptors are important for understanding of molecular details of transcriptional control as well as providing the insight as to how an individual transcriptional factor such as glucocorticoid receptor, contributes to cell identity and function. The purpose of this review is to establish the general molecular mechanism of glucocorticoid action and mechanism associated hormone-receptor complexes with the control of differential patterns (i.e. "positive" and "negative") of gene expression. One of the examples of two signal pathways regulating opposite gene expression are NF-kB and GR-mediated signal pathways. These pathways have important and opposite roles in the immune function. NF-kB is transcription factor which induces the expression of many genes that participate in immune and inflamatory response, while GR is transcription factor that serves as antiinflammatory agent and immune suppressor. Their interactions within the cell, although not yet completely understood, appear to be an important, possibly even the primary mechanism of immune homeostasis. It has not been established that glucocorticoid sensitivity can be caused by mechanisms other than changes of GR number and properties, although recent studies have indicated that receptor isoforms and transcriptional factors may modulate glucocorticoid responsiveness by interacting with receptor protein or directly at the site of DNA binding. The aim of this review is also to describe the role of glucocorticoid receptors in mechanism of glucocorticoid action on cell functions, including immune responses, as well as to present emerging issues on clinical aspects of molecular mechanisms of glucocorticoid action., Glikokortikoidni hormoni su uključeni u regulaciju ćelijskih procesa koji koordiniraju fiziološke odgovore na različite signale. Ovi hormoni u kompleksu sa specifičnim ćelijskim receptorima preko aktivacije ekspresije mreže različitih gena učestvuju u koordinaciji komponenti koje su u osnovi fizioloških odgovora. Na taj način kompleksi hormona i receptora funkcionišu kao ključni faktor u regulaciji specifičnih ćelijskih funkcija, a takođe podstiču i procese diferencijacije u već determinisanim ćelijama. Analize glikokortikoidnih receptora (GR) su značajne, kako za bolje upoznavanje transkripcione kontrole, tako i za objašnjenje kako pojedini transkripcioni faktori, kao što su GR, doprinose identitetu ćelije i njenom funkcionisanju. U ovom radu su prikazani opšti principi molekulskog mehanizma delovanja glikokortikoida, kao i mehanizmi koji povezuju komplekse hormona i receptora sa kontrolom različitog tipa („pozitivnom” ili „negativnom”) genske ekspresije. Jedan od primera za signalne puteve koji suprotno regulišu aktivnost gena su nukleusni faktor kapaB (NFκB) i signalni putevi posredovani sa GR. Ovi putevi imaju suprotne uloge u regulaciji funkcionisanja imunskog sistema. NFκB je transkripcioni faktor koji indukuje ekspresiju gena uključenih u imunske i zapaljenjske procese. GR je takođe transkripcioni faktor, ali deluje kao antiinflamacioni i imunosupresivni agens. Njihove interakcije su značajne u ćelijama imunskog sistema, iako još nisu potpuno objašnjene; one su možda čak i primarne u mehanizmu imunske homeostaze. Do sada nije dokazano da ćelijska senzitivnost na delovanje glikokortikoida zavisi od mehanizama koji ne uključuju promene količine i funkcionalnih osobina GR. Međutim, novija istraživanja pokazuju da izoforme receptora i transkripcioni faktori mogu da menjaju ćelijski odgovor na glikokortikoide preko interakcije sa receptornim proteinom ili direktno sa mestima vezivanja na DNK. U ovom radu su takođe prikazani podaci iz literature o ključnoj ulozi glikokortikoidnih receptora u mehanizmu delovanja glikokortikoida u regulaciji ćelijskih funkcija, uključujući i ćelije imunskog sistema, kao i podaci o kliničkim aspektima molekulskog delovanja glikokortikoida.",
journal = "Srpski arhiv za celokupno lekarstvo",
title = "Molecular basis of glucocorticoid action, Molekulska osnova delovanja glikokortikoida",
volume = "133",
number = "Suppl. 1",
pages = "61-66",
doi = "10.2298/SARH05S1061R"
}

Ribarac-Stepić, N. B., Đurica, S. N., Žakula, Z., Korićanac, G.,& Milošević, D. P.. (2005). Molecular basis of glucocorticoid action. in Srpski arhiv za celokupno lekarstvo, 133(Suppl. 1), 61-66.
https://doi.org/10.2298/SARH05S1061R

Ribarac-Stepić NB, Đurica SN, Žakula Z, Korićanac G, Milošević DP. Molecular basis of glucocorticoid action. in Srpski arhiv za celokupno lekarstvo. 2005;133(Suppl. 1):61-66.
doi:10.2298/SARH05S1061R .

Ribarac-Stepić, Nevena B., Đurica, Snežana N., Žakula, Zorica, Korićanac, Goran, Milošević, Dragoslav P., "Molecular basis of glucocorticoid action" in Srpski arhiv za celokupno lekarstvo, 133, no. Suppl. 1 (2005):61-66,
https://doi.org/10.2298/SARH05S1061R . .

TY  - JOUR
AU  - Ribarac-Stepić, Nevena B.
AU  - Vulović, Mojca D.
AU  - Korićanac, Goran
AU  - Isenović, Esma R.
PY  - 2005
UR  - https://vinar.vin.bg.ac.rs/handle/123456789/2908
AB  - The characteristics of glucocorticoid receptors, their sensitivity to glucocorticoid as well as the basal and glucocorticoid induced thyrosine aminotranferase (TAT) and tryptophan oxygenase (TO) activities were studied in rat liver during aging. The concentration (N) and dissociation constant (K-d) of glucocorticoid receptor (GR) significantly change during the aging both in untreated and dexamethasone treated animals. The level of receptors was lower in dexamethasone treated rats of all analyzed aged groups compared to untreated animals. In comparison to untreated groups, there was no correlation between the changes of N and K-d during the lifespan. According to immunochemical analysis, the decline of receptor protein content occurs during lifespan. Dexamethasone treatment reduced the level of receptor protein compare to respective age group of untreated rats. The glucocorticoid-receptor (G-R) complexes from both untreated and treated animals underwent thermal activation, although the extent of activation was more pronounced in the case of untreated groups compared to treated animals. The magnitude of heat activation of receptor complexes was more pronounced in the liver of the youngest untreated rats compared to elderly ones, while the receptor activation between treated groups of studied ages has shown less significant differences. Besides, basal as well as induced TAT and TO activities after dexamethasone injection also showed age-related alterations. The observed alterations in GR might play a role in the changes of the cell responses to glucocorticoid during the age. This presumption is supported by detected changes in basal and dexamethasone induced TAT and TO activities during aging.
T2  - Biogerontology
T1  - Basal and glucocorticoid induced changes of hepatic glucocorticoid receptor during aging: relation to activities of tyrosine aminotransferase and tryptophan oxygenase
VL  - 6
IS  - 2
SP  - 113
EP  - 131
DO  - 10.1007/s10522-005-3498-y
ER  - 

@article{
author = "Ribarac-Stepić, Nevena B. and Vulović, Mojca D. and Korićanac, Goran and Isenović, Esma R.",
year = "2005",
abstract = "The characteristics of glucocorticoid receptors, their sensitivity to glucocorticoid as well as the basal and glucocorticoid induced thyrosine aminotranferase (TAT) and tryptophan oxygenase (TO) activities were studied in rat liver during aging. The concentration (N) and dissociation constant (K-d) of glucocorticoid receptor (GR) significantly change during the aging both in untreated and dexamethasone treated animals. The level of receptors was lower in dexamethasone treated rats of all analyzed aged groups compared to untreated animals. In comparison to untreated groups, there was no correlation between the changes of N and K-d during the lifespan. According to immunochemical analysis, the decline of receptor protein content occurs during lifespan. Dexamethasone treatment reduced the level of receptor protein compare to respective age group of untreated rats. The glucocorticoid-receptor (G-R) complexes from both untreated and treated animals underwent thermal activation, although the extent of activation was more pronounced in the case of untreated groups compared to treated animals. The magnitude of heat activation of receptor complexes was more pronounced in the liver of the youngest untreated rats compared to elderly ones, while the receptor activation between treated groups of studied ages has shown less significant differences. Besides, basal as well as induced TAT and TO activities after dexamethasone injection also showed age-related alterations. The observed alterations in GR might play a role in the changes of the cell responses to glucocorticoid during the age. This presumption is supported by detected changes in basal and dexamethasone induced TAT and TO activities during aging.",
journal = "Biogerontology",
title = "Basal and glucocorticoid induced changes of hepatic glucocorticoid receptor during aging: relation to activities of tyrosine aminotransferase and tryptophan oxygenase",
volume = "6",
number = "2",
pages = "113-131",
doi = "10.1007/s10522-005-3498-y"
}

Ribarac-Stepić, N. B., Vulović, M. D., Korićanac, G.,& Isenović, E. R.. (2005). Basal and glucocorticoid induced changes of hepatic glucocorticoid receptor during aging: relation to activities of tyrosine aminotransferase and tryptophan oxygenase. in Biogerontology, 6(2), 113-131.
https://doi.org/10.1007/s10522-005-3498-y

Ribarac-Stepić NB, Vulović MD, Korićanac G, Isenović ER. Basal and glucocorticoid induced changes of hepatic glucocorticoid receptor during aging: relation to activities of tyrosine aminotransferase and tryptophan oxygenase. in Biogerontology. 2005;6(2):113-131.
doi:10.1007/s10522-005-3498-y .

Ribarac-Stepić, Nevena B., Vulović, Mojca D., Korićanac, Goran, Isenović, Esma R., "Basal and glucocorticoid induced changes of hepatic glucocorticoid receptor during aging: relation to activities of tyrosine aminotransferase and tryptophan oxygenase" in Biogerontology, 6, no. 2 (2005):113-131,
https://doi.org/10.1007/s10522-005-3498-y . .

TY  - JOUR
AU  - Đurica, Snežana N.
AU  - Korićanac, Goran
AU  - Ribarac-Stepić, Nevena B.
AU  - Davidović, Mladen M.
AU  - Milošević, Dragoslav P.
AU  - Petrović, Miroljub
AU  - Rajić, Miodrag
PY  - 2004
UR  - http://www.doiserbia.nb.rs/Article.aspx?ID=0354-34470402161D
UR  - https://vinar.vin.bg.ac.rs/handle/123456789/7806
AB  - Changes in carbohydrate metabolism in elderly persons have drawn considerable attention but the findings from different studies are in contrast and are even controversial. The insulin receptors in erythrocytes were studied in elderly euglycaemic patients and in a middle-aged control group. The examined persons were also subjected to measurements of blood glucose, insulin and C-peptide concentrations, before and 3 hours after a dietetic meal. In the present study it was found that in spite of the maintained insulin level and C-peptide secretion, some structural and corresponding changes in membrane insulin receptors and the binding site caused differences in postreceptor responses in elderly persons. The examined groups, consisted of 29 males, average age of 66 years (65-70), with normal serum glucose level and 19 middle-aged males, average age of 42 years (32-48), with normal glycoregulation. In basal condition, elderly persons have both normal morning serum insulin (19.68 ± 4.00 mU/L) and C-peptide (2.04 ± 0.78 nmol/L) level. In elderly persons, the number of high affinity insulin receptors in erythrocytes membrane is 22.80 ± 6.18 but the formed insulin-high affinity receptors were not stable. Dissociation constant (Kd1) indicates its elevated dissociation (0.11 ± 0.04). At the same time the number of insulin low affinity binding sites is increased (13 273 ± 5 572) with a fast dissociation of the hormone (13.99 ± 3.37). Food intake raised the number of high affinity receptors compared to the basal value. Alteration in insulin binding affinity suggests the structural and corresponding changes in membrane receptors that may cause differences in postreceptors responses in elderly persons.
T2  - Jugoslovenska medicinska biohemija
T1  - Biochemical and molecular biological aspects of glucose intolerance in elderly persons
T1  - Biohemijski i molekularno biološki aspekti intolerancije glukoze kod starijih osoba
VL  - 23
IS  - 2
SP  - 161
EP  - 164
DO  - 10.2298/JMH0402161D
ER  - 

@article{
author = "Đurica, Snežana N. and Korićanac, Goran and Ribarac-Stepić, Nevena B. and Davidović, Mladen M. and Milošević, Dragoslav P. and Petrović, Miroljub and Rajić, Miodrag",
year = "2004",
abstract = "Changes in carbohydrate metabolism in elderly persons have drawn considerable attention but the findings from different studies are in contrast and are even controversial. The insulin receptors in erythrocytes were studied in elderly euglycaemic patients and in a middle-aged control group. The examined persons were also subjected to measurements of blood glucose, insulin and C-peptide concentrations, before and 3 hours after a dietetic meal. In the present study it was found that in spite of the maintained insulin level and C-peptide secretion, some structural and corresponding changes in membrane insulin receptors and the binding site caused differences in postreceptor responses in elderly persons. The examined groups, consisted of 29 males, average age of 66 years (65-70), with normal serum glucose level and 19 middle-aged males, average age of 42 years (32-48), with normal glycoregulation. In basal condition, elderly persons have both normal morning serum insulin (19.68 ± 4.00 mU/L) and C-peptide (2.04 ± 0.78 nmol/L) level. In elderly persons, the number of high affinity insulin receptors in erythrocytes membrane is 22.80 ± 6.18 but the formed insulin-high affinity receptors were not stable. Dissociation constant (Kd1) indicates its elevated dissociation (0.11 ± 0.04). At the same time the number of insulin low affinity binding sites is increased (13 273 ± 5 572) with a fast dissociation of the hormone (13.99 ± 3.37). Food intake raised the number of high affinity receptors compared to the basal value. Alteration in insulin binding affinity suggests the structural and corresponding changes in membrane receptors that may cause differences in postreceptors responses in elderly persons.",
journal = "Jugoslovenska medicinska biohemija",
title = "Biochemical and molecular biological aspects of glucose intolerance in elderly persons, Biohemijski i molekularno biološki aspekti intolerancije glukoze kod starijih osoba",
volume = "23",
number = "2",
pages = "161-164",
doi = "10.2298/JMH0402161D"
}

Đurica, S. N., Korićanac, G., Ribarac-Stepić, N. B., Davidović, M. M., Milošević, D. P., Petrović, M.,& Rajić, M.. (2004). Biochemical and molecular biological aspects of glucose intolerance in elderly persons. in Jugoslovenska medicinska biohemija, 23(2), 161-164.
https://doi.org/10.2298/JMH0402161D

Đurica SN, Korićanac G, Ribarac-Stepić NB, Davidović MM, Milošević DP, Petrović M, Rajić M. Biochemical and molecular biological aspects of glucose intolerance in elderly persons. in Jugoslovenska medicinska biohemija. 2004;23(2):161-164.
doi:10.2298/JMH0402161D .

Đurica, Snežana N., Korićanac, Goran, Ribarac-Stepić, Nevena B., Davidović, Mladen M., Milošević, Dragoslav P., Petrović, Miroljub, Rajić, Miodrag, "Biochemical and molecular biological aspects of glucose intolerance in elderly persons" in Jugoslovenska medicinska biohemija, 23, no. 2 (2004):161-164,
https://doi.org/10.2298/JMH0402161D . .

TY  - JOUR
AU  - Đurica, Snežana N.
AU  - Korićanac, Goran
AU  - Ribarac-Stepić, Nevena B.
AU  - Davidović, Mladen M.
AU  - Milošević, Dragoslav P.
AU  - Petrović, Miroljub
AU  - Rajić, Miodrag
PY  - 2004
UR  - http://www.doiserbia.nb.rs/Article.aspx?ID=0354-34470402161D
UR  - https://vinar.vin.bg.ac.rs/handle/123456789/7824
AB  - Changes in carbohydrate metabolism in elderly persons have drawn considerable attention but the findings from different studies are in contrast and are even controversial. The insulin receptors in erythrocytes were studied in elderly euglycaemic patients and in a middle-aged control group. The examined persons were also subjected to measurements of blood glucose, insulin and C-peptide concentrations, before and 3 hours after a dietetic meal. In the present study it was found that in spite of the maintained insulin level and C-peptide secretion, some structural and corresponding changes in membrane insulin receptors and the binding site caused differences in postreceptor responses in elderly persons. The examined groups, consisted of 29 males, average age of 66 years (65-70), with normal serum glucose level and 19 middle-aged males, average age of 42 years (32-48), with normal glycoregulation. In basal condition, elderly persons have both normal morning serum insulin (19.68 ± 4.00 mU/L) and C-peptide (2.04 ± 0.78 nmol/L) level. In elderly persons, the number of high affinity insulin receptors in erythrocytes membrane is 22.80 ± 6.18 but the formed insulin-high affinity receptors were not stable. Dissociation constant (Kd1) indicates its elevated dissociation (0.11 ± 0.04). At the same time the number of insulin low affinity binding sites is increased (13 273 ± 5 572) with a fast dissociation of the hormone (13.99 ± 3.37). Food intake raised the number of high affinity receptors compared to the basal value. Alteration in insulin binding affinity suggests the structural and corresponding changes in membrane receptors that may cause differences in postreceptors responses in elderly persons.
T2  - Jugoslovenska medicinska biohemija
T1  - Biochemical and molecular biological aspects of glucose intolerance in elderly persons
VL  - 23
IS  - 2
SP  - 161
EP  - 164
DO  - 10.2298/JMH0402161D
ER  - 

@article{
author = "Đurica, Snežana N. and Korićanac, Goran and Ribarac-Stepić, Nevena B. and Davidović, Mladen M. and Milošević, Dragoslav P. and Petrović, Miroljub and Rajić, Miodrag",
year = "2004",
abstract = "Changes in carbohydrate metabolism in elderly persons have drawn considerable attention but the findings from different studies are in contrast and are even controversial. The insulin receptors in erythrocytes were studied in elderly euglycaemic patients and in a middle-aged control group. The examined persons were also subjected to measurements of blood glucose, insulin and C-peptide concentrations, before and 3 hours after a dietetic meal. In the present study it was found that in spite of the maintained insulin level and C-peptide secretion, some structural and corresponding changes in membrane insulin receptors and the binding site caused differences in postreceptor responses in elderly persons. The examined groups, consisted of 29 males, average age of 66 years (65-70), with normal serum glucose level and 19 middle-aged males, average age of 42 years (32-48), with normal glycoregulation. In basal condition, elderly persons have both normal morning serum insulin (19.68 ± 4.00 mU/L) and C-peptide (2.04 ± 0.78 nmol/L) level. In elderly persons, the number of high affinity insulin receptors in erythrocytes membrane is 22.80 ± 6.18 but the formed insulin-high affinity receptors were not stable. Dissociation constant (Kd1) indicates its elevated dissociation (0.11 ± 0.04). At the same time the number of insulin low affinity binding sites is increased (13 273 ± 5 572) with a fast dissociation of the hormone (13.99 ± 3.37). Food intake raised the number of high affinity receptors compared to the basal value. Alteration in insulin binding affinity suggests the structural and corresponding changes in membrane receptors that may cause differences in postreceptors responses in elderly persons.",
journal = "Jugoslovenska medicinska biohemija",
title = "Biochemical and molecular biological aspects of glucose intolerance in elderly persons",
volume = "23",
number = "2",
pages = "161-164",
doi = "10.2298/JMH0402161D"
}

Đurica, S. N., Korićanac, G., Ribarac-Stepić, N. B., Davidović, M. M., Milošević, D. P., Petrović, M.,& Rajić, M.. (2004). Biochemical and molecular biological aspects of glucose intolerance in elderly persons. in Jugoslovenska medicinska biohemija, 23(2), 161-164.
https://doi.org/10.2298/JMH0402161D

Đurica SN, Korićanac G, Ribarac-Stepić NB, Davidović MM, Milošević DP, Petrović M, Rajić M. Biochemical and molecular biological aspects of glucose intolerance in elderly persons. in Jugoslovenska medicinska biohemija. 2004;23(2):161-164.
doi:10.2298/JMH0402161D .

Đurica, Snežana N., Korićanac, Goran, Ribarac-Stepić, Nevena B., Davidović, Mladen M., Milošević, Dragoslav P., Petrović, Miroljub, Rajić, Miodrag, "Biochemical and molecular biological aspects of glucose intolerance in elderly persons" in Jugoslovenska medicinska biohemija, 23, no. 2 (2004):161-164,
https://doi.org/10.2298/JMH0402161D . .

TY  - JOUR
AU  - Korićanac, Goran
AU  - Vulović, Mojca D.
AU  - Radivojša, Snežana
AU  - Žakula, Zorica
AU  - Ribarac-Stepić, Nevena B.
PY  - 2004
UR  - https://vinar.vin.bg.ac.rs/handle/123456789/2827
AB  - The effects of aging on hepatic and erythrocyte insulin receptors have been investigated in 6, 12, 18 and 21-months-old compare to 3-months-old rats. Plasma insulin was elevated in 6, 12 and 18-months-old rats. Specific binding of insulin in liver was increased at the age of 18 months and accompanied with increase in concentration of low affinity binding sites, while specific binding to erythrocytes as well as concentration of both classes of binding sites was increased in 6-months-old rats. The protein and mRNA content of hepatic receptor were decreased only in the oldest animals. Plasma glucose was elevated starting from 12-months-old rats, while, after decrease in 6-months-old animals, citrulline was raised in the oldest group. The results demonstrating that specific binding of insulin in liver and erythrocytes and the concentration of binding sites in both tissues were not decreased during aging, as well as the absence of changes in affinity of insulin binding sites do not point out to occurrence of insulin resistance. However, the increase in insulinemia in the middle of lifespan, elevated plasma glucose and citrulline as well as decrease of hepatic receptor protein and mRNA content in the oldest animals indicate some age-related changes in insulin signaling.
T2  - Biogerontology
T1  - Age-related changes of insulin receptors, plasma insulin and glucose level
VL  - 5
IS  - 5
SP  - 345
EP  - 353
DO  - 10.1007/s10522-004-2576-x
ER  - 

@article{
author = "Korićanac, Goran and Vulović, Mojca D. and Radivojša, Snežana and Žakula, Zorica and Ribarac-Stepić, Nevena B.",
year = "2004",
abstract = "The effects of aging on hepatic and erythrocyte insulin receptors have been investigated in 6, 12, 18 and 21-months-old compare to 3-months-old rats. Plasma insulin was elevated in 6, 12 and 18-months-old rats. Specific binding of insulin in liver was increased at the age of 18 months and accompanied with increase in concentration of low affinity binding sites, while specific binding to erythrocytes as well as concentration of both classes of binding sites was increased in 6-months-old rats. The protein and mRNA content of hepatic receptor were decreased only in the oldest animals. Plasma glucose was elevated starting from 12-months-old rats, while, after decrease in 6-months-old animals, citrulline was raised in the oldest group. The results demonstrating that specific binding of insulin in liver and erythrocytes and the concentration of binding sites in both tissues were not decreased during aging, as well as the absence of changes in affinity of insulin binding sites do not point out to occurrence of insulin resistance. However, the increase in insulinemia in the middle of lifespan, elevated plasma glucose and citrulline as well as decrease of hepatic receptor protein and mRNA content in the oldest animals indicate some age-related changes in insulin signaling.",
journal = "Biogerontology",
title = "Age-related changes of insulin receptors, plasma insulin and glucose level",
volume = "5",
number = "5",
pages = "345-353",
doi = "10.1007/s10522-004-2576-x"
}

Korićanac, G., Vulović, M. D., Radivojša, S., Žakula, Z.,& Ribarac-Stepić, N. B.. (2004). Age-related changes of insulin receptors, plasma insulin and glucose level. in Biogerontology, 5(5), 345-353.
https://doi.org/10.1007/s10522-004-2576-x

Korićanac G, Vulović MD, Radivojša S, Žakula Z, Ribarac-Stepić NB. Age-related changes of insulin receptors, plasma insulin and glucose level. in Biogerontology. 2004;5(5):345-353.
doi:10.1007/s10522-004-2576-x .

Korićanac, Goran, Vulović, Mojca D., Radivojša, Snežana, Žakula, Zorica, Ribarac-Stepić, Nevena B., "Age-related changes of insulin receptors, plasma insulin and glucose level" in Biogerontology, 5, no. 5 (2004):345-353,
https://doi.org/10.1007/s10522-004-2576-x . .

TY  - JOUR
AU  - Sevaljevic, L
AU  - Dobric, S
AU  - Bogojevic, D
AU  - Petrović, M
AU  - Korićanac, Goran
AU  - Vulović, Mojca D.
AU  - Kanazir, DA
AU  - Ribarac-Stepić, Nevena B.
PY  - 2003
UR  - https://vinar.vin.bg.ac.rs/handle/123456789/2645
AB  - This work was aimed at the radioprotective efficacy of turpentine oil (TO), alpha(2)-Macroglobulin (alpha(2)-M), Amifostine (Ami) and/or dexamethasone (Dex). These agents were administrated, alone or in combination, prior to irradiation of rats with 6.7 Gy (LD50/30). The survival was recorded daily for 4 weeks after irradiation and body weight, peripheral leukocytes and thrombocytes were measured. The plasma concentration of alpha(2)-M and other acute phase proteins were determined by crossed immunoelectrophoresis. All rats receiving alpha(2)-M and Ami alone or in combination survived the radiation injury, whereas the rate of survival of TO-treated rats was 90%. Radiation and therapy-induced changes in the expression of acute phase protein genes were atypical for the acute phase reaction. Dex alone was lethal for 45% and 55% of control and irradiated rats, respectively. Pretreatment with 1mg Dex reduced radioprotective efficacy of TO and Ami to 30% and 40%, respectively. Given together TO and Ami provided 70% protection to rats receiving Dex. The TO and GYM enhanced the rate of survival from 50% to 90% and 100%, respectively. In the presence of 1 mg Dex the TO-induced radioprotectors and Ami exhibited radiosensitizing rather than radioprotecting activities.
T2  - Journal of Radiation Research
T1  - The radioprotective activities of turpentine-induced inflammation and alpha(2)-macroglobulin: The effect of dexamethasone on the radioprotective efficacy of the inflammation
VL  - 44
IS  - 1
SP  - 59
EP  - 67
UR  - https://hdl.handle.net/21.15107/rcub_vinar_2645
ER  - 

@article{
author = "Sevaljevic, L and Dobric, S and Bogojevic, D and Petrović, M and Korićanac, Goran and Vulović, Mojca D. and Kanazir, DA and Ribarac-Stepić, Nevena B.",
year = "2003",
abstract = "This work was aimed at the radioprotective efficacy of turpentine oil (TO), alpha(2)-Macroglobulin (alpha(2)-M), Amifostine (Ami) and/or dexamethasone (Dex). These agents were administrated, alone or in combination, prior to irradiation of rats with 6.7 Gy (LD50/30). The survival was recorded daily for 4 weeks after irradiation and body weight, peripheral leukocytes and thrombocytes were measured. The plasma concentration of alpha(2)-M and other acute phase proteins were determined by crossed immunoelectrophoresis. All rats receiving alpha(2)-M and Ami alone or in combination survived the radiation injury, whereas the rate of survival of TO-treated rats was 90%. Radiation and therapy-induced changes in the expression of acute phase protein genes were atypical for the acute phase reaction. Dex alone was lethal for 45% and 55% of control and irradiated rats, respectively. Pretreatment with 1mg Dex reduced radioprotective efficacy of TO and Ami to 30% and 40%, respectively. Given together TO and Ami provided 70% protection to rats receiving Dex. The TO and GYM enhanced the rate of survival from 50% to 90% and 100%, respectively. In the presence of 1 mg Dex the TO-induced radioprotectors and Ami exhibited radiosensitizing rather than radioprotecting activities.",
journal = "Journal of Radiation Research",
title = "The radioprotective activities of turpentine-induced inflammation and alpha(2)-macroglobulin: The effect of dexamethasone on the radioprotective efficacy of the inflammation",
volume = "44",
number = "1",
pages = "59-67",
url = "https://hdl.handle.net/21.15107/rcub_vinar_2645"
}

Sevaljevic, L., Dobric, S., Bogojevic, D., Petrović, M., Korićanac, G., Vulović, M. D., Kanazir, D.,& Ribarac-Stepić, N. B.. (2003). The radioprotective activities of turpentine-induced inflammation and alpha(2)-macroglobulin: The effect of dexamethasone on the radioprotective efficacy of the inflammation. in Journal of Radiation Research, 44(1), 59-67.
https://hdl.handle.net/21.15107/rcub_vinar_2645

Sevaljevic L, Dobric S, Bogojevic D, Petrović M, Korićanac G, Vulović MD, Kanazir D, Ribarac-Stepić NB. The radioprotective activities of turpentine-induced inflammation and alpha(2)-macroglobulin: The effect of dexamethasone on the radioprotective efficacy of the inflammation. in Journal of Radiation Research. 2003;44(1):59-67.
https://hdl.handle.net/21.15107/rcub_vinar_2645 .

Sevaljevic, L, Dobric, S, Bogojevic, D, Petrović, M, Korićanac, Goran, Vulović, Mojca D., Kanazir, DA, Ribarac-Stepić, Nevena B., "The radioprotective activities of turpentine-induced inflammation and alpha(2)-macroglobulin: The effect of dexamethasone on the radioprotective efficacy of the inflammation" in Journal of Radiation Research, 44, no. 1 (2003):59-67,
https://hdl.handle.net/21.15107/rcub_vinar_2645 .

TY  - JOUR
AU  - Sevaljevic, L
AU  - Isenović, Esma R.
AU  - Vulović, Mojca D.
AU  - Mačvanin, Mirjana
AU  - Žakula, Zorica
AU  - Kanazir, Dušan T.
AU  - Ribarac-Stepić, Nevena B.
PY  - 2001
UR  - https://vinar.vin.bg.ac.rs/handle/123456789/2450
AB  - The responses of liver glucocorticoid receptor (GR) and genes coding for a glucocorticoid-inducible tyrosine aminotransferase (TAT) and two acute-phase proteins (APP) [alpha (2)-macroglobulin (alpha (2)-M) and gamma -fibrinogen (Fb)] to changes in glucocorticoid (GC) and proinflammatory (AP) cytokine contents have been examined in rats after single or combined treatments with turpentine oil, dexamethasone (Dex) and adrenalectomy. Activation of two APP genes in turpentine-induced inflammation was accompanied by an increase in the level of GR mRNA and a preferential translocation of GR-GC complexes to the nucleoplasm, while the expression of TAT remained unaltered. Dex alone caused a decrease in the levels of GR and Fb mRNAs, activation of TAT and alpha (2)-M genes, a decrease in the affinity of hormone binding sites and redistribution of translocated GR-Dex complexes within the nuclei. Inflammation potentiated the effect which Dex alone exerted on the GIR content and the number of GR binding sites but counteracted its influence on the affinity of GR binding sites and nuclear distribution of GR-Dex complexes.
T2  - Biological Signals and Receptors
T1  - The responses of rat liver glucocorticoid receptors and genes for tyrosine aminotransferase, alpha-2-macroglobulin and gamma-fibrinogen to adrenalectomy-, dexamethasone- and inflammation-induced changes in the levels of glucocorticoids and proinflammatory cytokines
VL  - 10
IS  - 5
SP  - 299
EP  - 309
UR  - https://hdl.handle.net/21.15107/rcub_vinar_2450
ER  - 

@article{
author = "Sevaljevic, L and Isenović, Esma R. and Vulović, Mojca D. and Mačvanin, Mirjana and Žakula, Zorica and Kanazir, Dušan T. and Ribarac-Stepić, Nevena B.",
year = "2001",
abstract = "The responses of liver glucocorticoid receptor (GR) and genes coding for a glucocorticoid-inducible tyrosine aminotransferase (TAT) and two acute-phase proteins (APP) [alpha (2)-macroglobulin (alpha (2)-M) and gamma -fibrinogen (Fb)] to changes in glucocorticoid (GC) and proinflammatory (AP) cytokine contents have been examined in rats after single or combined treatments with turpentine oil, dexamethasone (Dex) and adrenalectomy. Activation of two APP genes in turpentine-induced inflammation was accompanied by an increase in the level of GR mRNA and a preferential translocation of GR-GC complexes to the nucleoplasm, while the expression of TAT remained unaltered. Dex alone caused a decrease in the levels of GR and Fb mRNAs, activation of TAT and alpha (2)-M genes, a decrease in the affinity of hormone binding sites and redistribution of translocated GR-Dex complexes within the nuclei. Inflammation potentiated the effect which Dex alone exerted on the GIR content and the number of GR binding sites but counteracted its influence on the affinity of GR binding sites and nuclear distribution of GR-Dex complexes.",
journal = "Biological Signals and Receptors",
title = "The responses of rat liver glucocorticoid receptors and genes for tyrosine aminotransferase, alpha-2-macroglobulin and gamma-fibrinogen to adrenalectomy-, dexamethasone- and inflammation-induced changes in the levels of glucocorticoids and proinflammatory cytokines",
volume = "10",
number = "5",
pages = "299-309",
url = "https://hdl.handle.net/21.15107/rcub_vinar_2450"
}

Sevaljevic, L., Isenović, E. R., Vulović, M. D., Mačvanin, M., Žakula, Z., Kanazir, D. T.,& Ribarac-Stepić, N. B.. (2001). The responses of rat liver glucocorticoid receptors and genes for tyrosine aminotransferase, alpha-2-macroglobulin and gamma-fibrinogen to adrenalectomy-, dexamethasone- and inflammation-induced changes in the levels of glucocorticoids and proinflammatory cytokines. in Biological Signals and Receptors, 10(5), 299-309.
https://hdl.handle.net/21.15107/rcub_vinar_2450

Sevaljevic L, Isenović ER, Vulović MD, Mačvanin M, Žakula Z, Kanazir DT, Ribarac-Stepić NB. The responses of rat liver glucocorticoid receptors and genes for tyrosine aminotransferase, alpha-2-macroglobulin and gamma-fibrinogen to adrenalectomy-, dexamethasone- and inflammation-induced changes in the levels of glucocorticoids and proinflammatory cytokines. in Biological Signals and Receptors. 2001;10(5):299-309.
https://hdl.handle.net/21.15107/rcub_vinar_2450 .

Sevaljevic, L, Isenović, Esma R., Vulović, Mojca D., Mačvanin, Mirjana, Žakula, Zorica, Kanazir, Dušan T., Ribarac-Stepić, Nevena B., "The responses of rat liver glucocorticoid receptors and genes for tyrosine aminotransferase, alpha-2-macroglobulin and gamma-fibrinogen to adrenalectomy-, dexamethasone- and inflammation-induced changes in the levels of glucocorticoids and proinflammatory cytokines" in Biological Signals and Receptors, 10, no. 5 (2001):299-309,
https://hdl.handle.net/21.15107/rcub_vinar_2450 .

TY  - JOUR
AU  - Rosić, Mirko A.
AU  - Pantović, Suzana B.
AU  - Lučić, Aleksandra P.
AU  - Ribarac-Stepić, Nevena B.
AU  - Anđelković, Ivan Z.
PY  - 2001
UR  - https://vinar.vin.bg.ac.rs/handle/123456789/2413
AB  - The dynamics and kinetics of thyroid hormone transport in the isolated rat heart were examined using the modified unidirectional paired tracer dilution method. The uptake of I-125-thyroxine (I-115-T-4) and I-125-triiodothyronine (I-125-T-3) from the extracellular space into heart cells was measured relative to the extracellular space marker H-3-mannitol. The thyroid hormone maximal uptake was 54.4 % for I-125-T-4 and 52.15 % for I-125-T-3. The thyroid hormone net uptake was 25.69 % for I-125-T-4 and 25.49 % for I-125-T-3. Backflux from the intracellular space was 53.17 % for I-125-T-4 and 61.59 % for I-125-T-3. In the presence of unlabelled thyroid hormones, I-125-T-4 and I-125-T-3 maximal uptakes were reduced from 10.1 to 59.74 % and from 34.6 to 65.3 %, respectively, depending on the concentration of the unlabelled hormone, suggesting a saturable mechanism of the thyroid hormone uptake by the heart cells, with K-m(T4) = 105.46 muM and the maximal rate of I-125-thyroid hormone flax from the extracellular space to heart cells (V-max(T4))= 177.84 nM min(-1) for I-125-T-4 uptake, and K-m(T3) = 80.0 muM and V-max(T3) = 118.5 nM min(-1) for I-125-T-3 uptake.
T2  - Experimental Physiology
T1  - Kinetics of thyroxine (T-4) and triiodothyronine (T-3) transport in the isolated rat heart
VL  - 86
IS  - 1
SP  - 13
EP  - 18
DO  - 10.1113/eph8601835
ER  - 

@article{
author = "Rosić, Mirko A. and Pantović, Suzana B. and Lučić, Aleksandra P. and Ribarac-Stepić, Nevena B. and Anđelković, Ivan Z.",
year = "2001",
abstract = "The dynamics and kinetics of thyroid hormone transport in the isolated rat heart were examined using the modified unidirectional paired tracer dilution method. The uptake of I-125-thyroxine (I-115-T-4) and I-125-triiodothyronine (I-125-T-3) from the extracellular space into heart cells was measured relative to the extracellular space marker H-3-mannitol. The thyroid hormone maximal uptake was 54.4 % for I-125-T-4 and 52.15 % for I-125-T-3. The thyroid hormone net uptake was 25.69 % for I-125-T-4 and 25.49 % for I-125-T-3. Backflux from the intracellular space was 53.17 % for I-125-T-4 and 61.59 % for I-125-T-3. In the presence of unlabelled thyroid hormones, I-125-T-4 and I-125-T-3 maximal uptakes were reduced from 10.1 to 59.74 % and from 34.6 to 65.3 %, respectively, depending on the concentration of the unlabelled hormone, suggesting a saturable mechanism of the thyroid hormone uptake by the heart cells, with K-m(T4) = 105.46 muM and the maximal rate of I-125-thyroid hormone flax from the extracellular space to heart cells (V-max(T4))= 177.84 nM min(-1) for I-125-T-4 uptake, and K-m(T3) = 80.0 muM and V-max(T3) = 118.5 nM min(-1) for I-125-T-3 uptake.",
journal = "Experimental Physiology",
title = "Kinetics of thyroxine (T-4) and triiodothyronine (T-3) transport in the isolated rat heart",
volume = "86",
number = "1",
pages = "13-18",
doi = "10.1113/eph8601835"
}

Rosić, M. A., Pantović, S. B., Lučić, A. P., Ribarac-Stepić, N. B.,& Anđelković, I. Z.. (2001). Kinetics of thyroxine (T-4) and triiodothyronine (T-3) transport in the isolated rat heart. in Experimental Physiology, 86(1), 13-18.
https://doi.org/10.1113/eph8601835

Rosić MA, Pantović SB, Lučić AP, Ribarac-Stepić NB, Anđelković IZ. Kinetics of thyroxine (T-4) and triiodothyronine (T-3) transport in the isolated rat heart. in Experimental Physiology. 2001;86(1):13-18.
doi:10.1113/eph8601835 .

Rosić, Mirko A., Pantović, Suzana B., Lučić, Aleksandra P., Ribarac-Stepić, Nevena B., Anđelković, Ivan Z., "Kinetics of thyroxine (T-4) and triiodothyronine (T-3) transport in the isolated rat heart" in Experimental Physiology, 86, no. 1 (2001):13-18,
https://doi.org/10.1113/eph8601835 . .

TY  - JOUR
AU  - Ribarac-Stepić, Nevena B.
AU  - Isenović, Esma R.
AU  - Naumovic, R
AU  - Korićanac, Goran
AU  - Vulović, Mojca D.
AU  - Žakula, Zorica
AU  - Blagojevic, R
AU  - Djukanovic, L
PY  - 2001
UR  - https://vinar.vin.bg.ac.rs/handle/123456789/2514
AB  - The glucocorticoid receptors in lymphocytes of patients treated with glucocorticoids after kidney transplantation have been studied in order to determine whether abnormalities in corticosteroid binding and trans-activation of steroid-receptor complexes, i.e., their translocation into nuclei, may contribute to the resistance of patients to glucocorticoid therapy. The patients were divided into two groups, according to graft stability: patients with stable graft function and those with chronic allograft rejection. The study revealed changes in both level and binding affinity of glucocorticoid receptors in peripheral blood lymphocytes from patients with chronic graft rejection, compared with control level, as well as with values of patients with stable graft function. Those data indicate that sensitivity to glucocorticoids depends, at least in part, on the alterations of glucocorticoid receptors. The receptor translocation into nuclei indicates that unknown post-receptor events might also be involved in glucocorticoid resistance that seriously impair successive glucocorticoid therapy after organ transplantation. Further examination of glucocorticoid receptors in cases of organ transplantation seems warranted.
T2  - Clinical and Experimental Medicine
T1  - Glucocorticoid receptors in lymphocytes and stability of kidney graft function
VL  - 1
IS  - 4
SP  - 179
EP  - 186
DO  - 10.1007/s102380100001
ER  - 

@article{
author = "Ribarac-Stepić, Nevena B. and Isenović, Esma R. and Naumovic, R and Korićanac, Goran and Vulović, Mojca D. and Žakula, Zorica and Blagojevic, R and Djukanovic, L",
year = "2001",
abstract = "The glucocorticoid receptors in lymphocytes of patients treated with glucocorticoids after kidney transplantation have been studied in order to determine whether abnormalities in corticosteroid binding and trans-activation of steroid-receptor complexes, i.e., their translocation into nuclei, may contribute to the resistance of patients to glucocorticoid therapy. The patients were divided into two groups, according to graft stability: patients with stable graft function and those with chronic allograft rejection. The study revealed changes in both level and binding affinity of glucocorticoid receptors in peripheral blood lymphocytes from patients with chronic graft rejection, compared with control level, as well as with values of patients with stable graft function. Those data indicate that sensitivity to glucocorticoids depends, at least in part, on the alterations of glucocorticoid receptors. The receptor translocation into nuclei indicates that unknown post-receptor events might also be involved in glucocorticoid resistance that seriously impair successive glucocorticoid therapy after organ transplantation. Further examination of glucocorticoid receptors in cases of organ transplantation seems warranted.",
journal = "Clinical and Experimental Medicine",
title = "Glucocorticoid receptors in lymphocytes and stability of kidney graft function",
volume = "1",
number = "4",
pages = "179-186",
doi = "10.1007/s102380100001"
}

Ribarac-Stepić, N. B., Isenović, E. R., Naumovic, R., Korićanac, G., Vulović, M. D., Žakula, Z., Blagojevic, R.,& Djukanovic, L.. (2001). Glucocorticoid receptors in lymphocytes and stability of kidney graft function. in Clinical and Experimental Medicine, 1(4), 179-186.
https://doi.org/10.1007/s102380100001

Ribarac-Stepić NB, Isenović ER, Naumovic R, Korićanac G, Vulović MD, Žakula Z, Blagojevic R, Djukanovic L. Glucocorticoid receptors in lymphocytes and stability of kidney graft function. in Clinical and Experimental Medicine. 2001;1(4):179-186.
doi:10.1007/s102380100001 .

Ribarac-Stepić, Nevena B., Isenović, Esma R., Naumovic, R, Korićanac, Goran, Vulović, Mojca D., Žakula, Zorica, Blagojevic, R, Djukanovic, L, "Glucocorticoid receptors in lymphocytes and stability of kidney graft function" in Clinical and Experimental Medicine, 1, no. 4 (2001):179-186,
https://doi.org/10.1007/s102380100001 . .

TY  - CONF
AU  - Đurica, Snežana N.
AU  - Korićanac, Goran
AU  - Milosevic, D
AU  - Milanovic, P
AU  - Markovic, O
AU  - Ribarac-Stepić, Nevena B.
PY  - 1999
UR  - https://vinar.vin.bg.ac.rs/handle/123456789/2263
C3  - Zeitschrift fur Gerontologie und Geriatrie
T1  - Diminished peripheral glucose utilization in elderly persons
VL  - 32
IS  - 2
SP  - 118
EP  - 118
UR  - https://hdl.handle.net/21.15107/rcub_vinar_2263
ER  - 

@conference{
author = "Đurica, Snežana N. and Korićanac, Goran and Milosevic, D and Milanovic, P and Markovic, O and Ribarac-Stepić, Nevena B.",
year = "1999",
journal = "Zeitschrift fur Gerontologie und Geriatrie",
title = "Diminished peripheral glucose utilization in elderly persons",
volume = "32",
number = "2",
pages = "118-118",
url = "https://hdl.handle.net/21.15107/rcub_vinar_2263"
}

Đurica, S. N., Korićanac, G., Milosevic, D., Milanovic, P., Markovic, O.,& Ribarac-Stepić, N. B.. (1999). Diminished peripheral glucose utilization in elderly persons. in Zeitschrift fur Gerontologie und Geriatrie, 32(2), 118-118.
https://hdl.handle.net/21.15107/rcub_vinar_2263

Đurica SN, Korićanac G, Milosevic D, Milanovic P, Markovic O, Ribarac-Stepić NB. Diminished peripheral glucose utilization in elderly persons. in Zeitschrift fur Gerontologie und Geriatrie. 1999;32(2):118-118.
https://hdl.handle.net/21.15107/rcub_vinar_2263 .

Đurica, Snežana N., Korićanac, Goran, Milosevic, D, Milanovic, P, Markovic, O, Ribarac-Stepić, Nevena B., "Diminished peripheral glucose utilization in elderly persons" in Zeitschrift fur Gerontologie und Geriatrie, 32, no. 2 (1999):118-118,
https://hdl.handle.net/21.15107/rcub_vinar_2263 .

TY  - JOUR
AU  - Rosić, Mirko A.
AU  - Pantović, Suzana B.
AU  - Lučić, Aleksandra P.
AU  - Ribarac-Stepić, Nevena B.
AU  - Trtić, Tatjana M.
AU  - Anđelković, Ivan Z.
AU  - Segal, Malcolm B.
PY  - 1998
UR  - https://vinar.vin.bg.ac.rs/handle/123456789/2144
T2  - Pharmazie
T1  - Triiodothyronine uptake by the isolated rat heart
VL  - 53
IS  - 5
SP  - 351
EP  - 352
UR  - https://hdl.handle.net/21.15107/rcub_vinar_2144
ER  - 

@article{
author = "Rosić, Mirko A. and Pantović, Suzana B. and Lučić, Aleksandra P. and Ribarac-Stepić, Nevena B. and Trtić, Tatjana M. and Anđelković, Ivan Z. and Segal, Malcolm B.",
year = "1998",
journal = "Pharmazie",
title = "Triiodothyronine uptake by the isolated rat heart",
volume = "53",
number = "5",
pages = "351-352",
url = "https://hdl.handle.net/21.15107/rcub_vinar_2144"
}

Rosić, M. A., Pantović, S. B., Lučić, A. P., Ribarac-Stepić, N. B., Trtić, T. M., Anđelković, I. Z.,& Segal, M. B.. (1998). Triiodothyronine uptake by the isolated rat heart. in Pharmazie, 53(5), 351-352.
https://hdl.handle.net/21.15107/rcub_vinar_2144

Rosić MA, Pantović SB, Lučić AP, Ribarac-Stepić NB, Trtić TM, Anđelković IZ, Segal MB. Triiodothyronine uptake by the isolated rat heart. in Pharmazie. 1998;53(5):351-352.
https://hdl.handle.net/21.15107/rcub_vinar_2144 .

Rosić, Mirko A., Pantović, Suzana B., Lučić, Aleksandra P., Ribarac-Stepić, Nevena B., Trtić, Tatjana M., Anđelković, Ivan Z., Segal, Malcolm B., "Triiodothyronine uptake by the isolated rat heart" in Pharmazie, 53, no. 5 (1998):351-352,
https://hdl.handle.net/21.15107/rcub_vinar_2144 .

TY  - JOUR
AU  - Sevaljevic, L
AU  - Mačvanin, Mirjana
AU  - Žakula, Zorica
AU  - Kanazir, Dušan T.
AU  - Ribarac-Stepić, Nevena B.
PY  - 1998
UR  - https://vinar.vin.bg.ac.rs/handle/123456789/2189
AB  - Hormonal requirements for full hepatic expression of alpha(2)-macroglobulin (alpha(2)M), alpha(1)-acid glycoprotein (AGP), haptoglobin (Hp) and gamma-fibrinogen (Fb) were assessed at the level of mRNA. Prior to exposure to turpentine-induced inflammation, rats were either depleted of glucocorticoids by adrenalectomy or supplemented with an excess of dexamethasone. Adrenalectomy alone did not affect the basal level of acute phase protein (APP) expression except for alpha(2)M mRNA, the level of which was enhanced. In contrast, dexamethasone treatment alone promoted full induction of alpha(2)M, significant, but not maximal increase of AGP and Hp mRNAs and suppression of Fb. In adrenalectomized rats, acute phase (AP)-cytokines, released in response to inflammation, promoted full expression of Fb and Hp and increased the level of AGP mRNA whereas alpha(2)M mRNA remained at the basal level. Inflammation in dexamethasone pretreated rats elicited changes which, in comparison to mRNA values for dexamethasone unpretreated inflamed rats, were seen as overexpression of alpha(2)M, full expression of AGP and incomplete expression of Hp, whereas Fb mRNA remained at the basal level. These data suggest that glucocorticoids are the principal inducers of a(2)M and AP-cytokines of Fb. For full induction of AGP, additive actions of glucocorticoids and AP-cytokines are required whereas expression of Hp is predominantly controlled by AP-cytokines. (C) 1998 Elsevier Science Ltd. All rights reserved.
T2  - Journal of Steroid Biochemistry and Molecular Biology
T1  - Adrenalectomy and dexamethasone treatment alter the patterns of basal and acute phase response-induced expression of acute phase protein genes in rat liver
VL  - 66
IS  - 5-6
SP  - 347
EP  - 353
DO  - 10.1016/S0960-0760(98)00060-0
ER  - 

@article{
author = "Sevaljevic, L and Mačvanin, Mirjana and Žakula, Zorica and Kanazir, Dušan T. and Ribarac-Stepić, Nevena B.",
year = "1998",
abstract = "Hormonal requirements for full hepatic expression of alpha(2)-macroglobulin (alpha(2)M), alpha(1)-acid glycoprotein (AGP), haptoglobin (Hp) and gamma-fibrinogen (Fb) were assessed at the level of mRNA. Prior to exposure to turpentine-induced inflammation, rats were either depleted of glucocorticoids by adrenalectomy or supplemented with an excess of dexamethasone. Adrenalectomy alone did not affect the basal level of acute phase protein (APP) expression except for alpha(2)M mRNA, the level of which was enhanced. In contrast, dexamethasone treatment alone promoted full induction of alpha(2)M, significant, but not maximal increase of AGP and Hp mRNAs and suppression of Fb. In adrenalectomized rats, acute phase (AP)-cytokines, released in response to inflammation, promoted full expression of Fb and Hp and increased the level of AGP mRNA whereas alpha(2)M mRNA remained at the basal level. Inflammation in dexamethasone pretreated rats elicited changes which, in comparison to mRNA values for dexamethasone unpretreated inflamed rats, were seen as overexpression of alpha(2)M, full expression of AGP and incomplete expression of Hp, whereas Fb mRNA remained at the basal level. These data suggest that glucocorticoids are the principal inducers of a(2)M and AP-cytokines of Fb. For full induction of AGP, additive actions of glucocorticoids and AP-cytokines are required whereas expression of Hp is predominantly controlled by AP-cytokines. (C) 1998 Elsevier Science Ltd. All rights reserved.",
journal = "Journal of Steroid Biochemistry and Molecular Biology",
title = "Adrenalectomy and dexamethasone treatment alter the patterns of basal and acute phase response-induced expression of acute phase protein genes in rat liver",
volume = "66",
number = "5-6",
pages = "347-353",
doi = "10.1016/S0960-0760(98)00060-0"
}

Sevaljevic, L., Mačvanin, M., Žakula, Z., Kanazir, D. T.,& Ribarac-Stepić, N. B.. (1998). Adrenalectomy and dexamethasone treatment alter the patterns of basal and acute phase response-induced expression of acute phase protein genes in rat liver. in Journal of Steroid Biochemistry and Molecular Biology, 66(5-6), 347-353.
https://doi.org/10.1016/S0960-0760(98)00060-0

Sevaljevic L, Mačvanin M, Žakula Z, Kanazir DT, Ribarac-Stepić NB. Adrenalectomy and dexamethasone treatment alter the patterns of basal and acute phase response-induced expression of acute phase protein genes in rat liver. in Journal of Steroid Biochemistry and Molecular Biology. 1998;66(5-6):347-353.
doi:10.1016/S0960-0760(98)00060-0 .

Sevaljevic, L, Mačvanin, Mirjana, Žakula, Zorica, Kanazir, Dušan T., Ribarac-Stepić, Nevena B., "Adrenalectomy and dexamethasone treatment alter the patterns of basal and acute phase response-induced expression of acute phase protein genes in rat liver" in Journal of Steroid Biochemistry and Molecular Biology, 66, no. 5-6 (1998):347-353,
https://doi.org/10.1016/S0960-0760(98)00060-0 . .

TY  - CONF
AU  - Isenović, Esma R.
AU  - Vulović, Mojca D.
AU  - Kanazir, Dušan T.
AU  - Ribarac-Stepić, Nevena B.
PY  - 1997
UR  - https://vinar.vin.bg.ac.rs/handle/123456789/51
C3  - FASEB Journal
T1  - Effects of insulin on glucocorticoid receptors in adrenalectomy
VL  - 11
IS  - 9
SP  - A1049
EP  - A1049
UR  - https://hdl.handle.net/21.15107/rcub_vinar_51
ER  - 

@conference{
author = "Isenović, Esma R. and Vulović, Mojca D. and Kanazir, Dušan T. and Ribarac-Stepić, Nevena B.",
year = "1997",
journal = "FASEB Journal",
title = "Effects of insulin on glucocorticoid receptors in adrenalectomy",
volume = "11",
number = "9",
pages = "A1049-A1049",
url = "https://hdl.handle.net/21.15107/rcub_vinar_51"
}

Isenović, E. R., Vulović, M. D., Kanazir, D. T.,& Ribarac-Stepić, N. B.. (1997). Effects of insulin on glucocorticoid receptors in adrenalectomy. in FASEB Journal, 11(9), A1049-A1049.
https://hdl.handle.net/21.15107/rcub_vinar_51

Isenović ER, Vulović MD, Kanazir DT, Ribarac-Stepić NB. Effects of insulin on glucocorticoid receptors in adrenalectomy. in FASEB Journal. 1997;11(9):A1049-A1049.
https://hdl.handle.net/21.15107/rcub_vinar_51 .

Isenović, Esma R., Vulović, Mojca D., Kanazir, Dušan T., Ribarac-Stepić, Nevena B., "Effects of insulin on glucocorticoid receptors in adrenalectomy" in FASEB Journal, 11, no. 9 (1997):A1049-A1049,
https://hdl.handle.net/21.15107/rcub_vinar_51 .

TY  - CONF
AU  - Ribarac-Stepić, Nevena B.
AU  - Isenović, Esma R.
AU  - Korićanac, Goran
AU  - Kanazir, Dušan T.
PY  - 1997
UR  - https://vinar.vin.bg.ac.rs/handle/123456789/50
AB  - The goal of this study was to examine the possible effects of the insulin on the functional properties of the glucocorticoid receptor (GR), in the rat liver, as well as its equilibrium binding constant (Kd) and number of binding sites (q), in order to contribute to elucidation of the molecular basis of the relationship between insulin and glucocorticoids in regulation of cell processes. Biological consequences of their interactions were judged on the basis of changes in GR as well as in the activity of Tryptophan oxygenase (TO). The experiments were perfomed on male nonadrenalectomized Wistar strain rats, treated by streptozotocin as well as adrenalectomized animals These group of animals were injected by insulin (25ug/100g b.w.) 18 hours before analysis. The obtained results have shown that the Kd in all experimental groups of animal was in the interval: 1.87-4.027nM. However, the injected insulin in all experimental groups increased the number of GR, while in streptozotocin treated rats, this increase was 1.5 fold, compared to the values obtained for corresponding controls. TO activity was increased (2-3 fold), in liver of insulin treated rats, except in the case of adrenalectomized animals, while the enzyme activity in streptozotocin treated rats was up to 3 fold, in respect to the appropriate control value. These evidences suggest that mechanisms of cooperative effects of insulin and glucocorticoid on regulation of cell function involve the modulation of hormone signals transmited through changes in number and functionality of GR proteins.
C3  - FASEB Journal
T1  - Glucocorticoid receptor and Tryptophan oxygenase activity in streptozotocin treated rats.
VL  - 11
IS  - 9
SP  - A1048
EP  - A1048
UR  - https://hdl.handle.net/21.15107/rcub_vinar_50
ER  - 

@conference{
author = "Ribarac-Stepić, Nevena B. and Isenović, Esma R. and Korićanac, Goran and Kanazir, Dušan T.",
year = "1997",
abstract = "The goal of this study was to examine the possible effects of the insulin on the functional properties of the glucocorticoid receptor (GR), in the rat liver, as well as its equilibrium binding constant (Kd) and number of binding sites (q), in order to contribute to elucidation of the molecular basis of the relationship between insulin and glucocorticoids in regulation of cell processes. Biological consequences of their interactions were judged on the basis of changes in GR as well as in the activity of Tryptophan oxygenase (TO). The experiments were perfomed on male nonadrenalectomized Wistar strain rats, treated by streptozotocin as well as adrenalectomized animals These group of animals were injected by insulin (25ug/100g b.w.) 18 hours before analysis. The obtained results have shown that the Kd in all experimental groups of animal was in the interval: 1.87-4.027nM. However, the injected insulin in all experimental groups increased the number of GR, while in streptozotocin treated rats, this increase was 1.5 fold, compared to the values obtained for corresponding controls. TO activity was increased (2-3 fold), in liver of insulin treated rats, except in the case of adrenalectomized animals, while the enzyme activity in streptozotocin treated rats was up to 3 fold, in respect to the appropriate control value. These evidences suggest that mechanisms of cooperative effects of insulin and glucocorticoid on regulation of cell function involve the modulation of hormone signals transmited through changes in number and functionality of GR proteins.",
journal = "FASEB Journal",
title = "Glucocorticoid receptor and Tryptophan oxygenase activity in streptozotocin treated rats.",
volume = "11",
number = "9",
pages = "A1048-A1048",
url = "https://hdl.handle.net/21.15107/rcub_vinar_50"
}

Ribarac-Stepić, N. B., Isenović, E. R., Korićanac, G.,& Kanazir, D. T.. (1997). Glucocorticoid receptor and Tryptophan oxygenase activity in streptozotocin treated rats.. in FASEB Journal, 11(9), A1048-A1048.
https://hdl.handle.net/21.15107/rcub_vinar_50

Ribarac-Stepić NB, Isenović ER, Korićanac G, Kanazir DT. Glucocorticoid receptor and Tryptophan oxygenase activity in streptozotocin treated rats.. in FASEB Journal. 1997;11(9):A1048-A1048.
https://hdl.handle.net/21.15107/rcub_vinar_50 .

Ribarac-Stepić, Nevena B., Isenović, Esma R., Korićanac, Goran, Kanazir, Dušan T., "Glucocorticoid receptor and Tryptophan oxygenase activity in streptozotocin treated rats." in FASEB Journal, 11, no. 9 (1997):A1048-A1048,
https://hdl.handle.net/21.15107/rcub_vinar_50 .

TY  - JOUR
AU  - Ristić-Fira, Aleksandra
AU  - Đorđević Marković, R.
AU  - Radojčić, Marija
AU  - Ribarac-Stepić, Nevena B.
AU  - Kanazir, Dušan T.
PY  - 1996
UR  - https://vinar.vin.bg.ac.rs/handle/123456789/2031
T2  - Jugoslovenska Medicinska Biohemija
T1  - Glucocorticoid effects on B16/F10 and B16/C3 mouse melanoma cell growth
VL  - 15
IS  - 4
SP  - 320
EP  - 321
UR  - https://hdl.handle.net/21.15107/rcub_vinar_2031
ER  - 

@article{
author = "Ristić-Fira, Aleksandra and Đorđević Marković, R. and Radojčić, Marija and Ribarac-Stepić, Nevena B. and Kanazir, Dušan T.",
year = "1996",
journal = "Jugoslovenska Medicinska Biohemija",
title = "Glucocorticoid effects on B16/F10 and B16/C3 mouse melanoma cell growth",
volume = "15",
number = "4",
pages = "320-321",
url = "https://hdl.handle.net/21.15107/rcub_vinar_2031"
}

Ristić-Fira, A., Đorđević Marković, R., Radojčić, M., Ribarac-Stepić, N. B.,& Kanazir, D. T.. (1996). Glucocorticoid effects on B16/F10 and B16/C3 mouse melanoma cell growth. in Jugoslovenska Medicinska Biohemija, 15(4), 320-321.
https://hdl.handle.net/21.15107/rcub_vinar_2031

Ristić-Fira A, Đorđević Marković R, Radojčić M, Ribarac-Stepić NB, Kanazir DT. Glucocorticoid effects on B16/F10 and B16/C3 mouse melanoma cell growth. in Jugoslovenska Medicinska Biohemija. 1996;15(4):320-321.
https://hdl.handle.net/21.15107/rcub_vinar_2031 .

Ristić-Fira, Aleksandra, Đorđević Marković, R., Radojčić, Marija, Ribarac-Stepić, Nevena B., Kanazir, Dušan T., "Glucocorticoid effects on B16/F10 and B16/C3 mouse melanoma cell growth" in Jugoslovenska Medicinska Biohemija, 15, no. 4 (1996):320-321,
https://hdl.handle.net/21.15107/rcub_vinar_2031 .