TY  - JOUR
AU  - Dobutović, Branislava
AU  - Sudar, Emina
AU  - Tepavčević, Snežana
AU  - Đorđević, Jelena D.
AU  - Đorđević, Ana D.
AU  - Radoičić, Marija B.
AU  - Isenović, Esma R.
PY  - 2014
UR  - https://vinar.vin.bg.ac.rs/handle/123456789/93
AB  - Introduction: We investigated the effects of ghrelin on protein expression of the liver antioxidant enzymes superoxide dismutases (SODs), catalase (CAT), glutathione peroxidase (GPx), and glutathione reductase (GR), nuclear factor kappa B (NF kappa B) and inducible nitric oxide synthase (iNOS). Furthermore, we aimed to investigate whether extracellular regulated protein kinase (ERK1/2) and protein kinase B (Akt) are involved in ghrelin-regulated liver antioxidant enzymes and iNOS protein expression. Material and methods: Male Wistar rats were treated with ghrelin (0.3 nmol/5 mu l) injected into the lateral cerebral ventricle every 24 h for 5 days, and 2 h after the last treatment the animals were sacrificed and the liver excised. The Western blot method was used to determine expression of antioxidant enzymes, iNOS, phosphorylation of Akt, ERK1/2 and nuclear factor kappa B (NF kappa B) subunits 50 and 65. Results: There was significantly higher protein expression of CuZnSOD (p LT 0.001), MnSOD (p LT 0.001), CAT (p LT 0.001), GPx, (p LT 0.001), and GR (p LT 0.01) in the liver isolated from ghrelin-treated animals compared with control animals. In contrast, ghrelin significantly (p LT 0.01) reduced protein expression of iNOS. In addition, phosphorylation of NF kappa B subunits p65 and p50 was significantly (p LT 0.001 for p65; p LT 0.05 for p50) reduced by ghrelin when compared with controls. Phosphorylation of ERK1/2 and of Akt was significantly higher in ghrelin-treated than in control animals (p LT 0.05 for ERK1/2; p LT 0.01 for Akt). Conclusions: The results show that activation of Akt and ERK1/2 is involved in ghrelin-mediated regulation of protein expression of antioxidant enzymes and iNOS in the rat liver.
T2  - Archives of Medical Science
T1  - Effects of ghrelin on protein expression of antioxidative enzymes and iNOS in the rat liver
VL  - 10
IS  - 4
SP  - 806
EP  - 816
DO  - 10.5114/aoms.2014.44872
ER  - 

@article{
author = "Dobutović, Branislava and Sudar, Emina and Tepavčević, Snežana and Đorđević, Jelena D. and Đorđević, Ana D. and Radoičić, Marija B. and Isenović, Esma R.",
year = "2014",
abstract = "Introduction: We investigated the effects of ghrelin on protein expression of the liver antioxidant enzymes superoxide dismutases (SODs), catalase (CAT), glutathione peroxidase (GPx), and glutathione reductase (GR), nuclear factor kappa B (NF kappa B) and inducible nitric oxide synthase (iNOS). Furthermore, we aimed to investigate whether extracellular regulated protein kinase (ERK1/2) and protein kinase B (Akt) are involved in ghrelin-regulated liver antioxidant enzymes and iNOS protein expression. Material and methods: Male Wistar rats were treated with ghrelin (0.3 nmol/5 mu l) injected into the lateral cerebral ventricle every 24 h for 5 days, and 2 h after the last treatment the animals were sacrificed and the liver excised. The Western blot method was used to determine expression of antioxidant enzymes, iNOS, phosphorylation of Akt, ERK1/2 and nuclear factor kappa B (NF kappa B) subunits 50 and 65. Results: There was significantly higher protein expression of CuZnSOD (p LT 0.001), MnSOD (p LT 0.001), CAT (p LT 0.001), GPx, (p LT 0.001), and GR (p LT 0.01) in the liver isolated from ghrelin-treated animals compared with control animals. In contrast, ghrelin significantly (p LT 0.01) reduced protein expression of iNOS. In addition, phosphorylation of NF kappa B subunits p65 and p50 was significantly (p LT 0.001 for p65; p LT 0.05 for p50) reduced by ghrelin when compared with controls. Phosphorylation of ERK1/2 and of Akt was significantly higher in ghrelin-treated than in control animals (p LT 0.05 for ERK1/2; p LT 0.01 for Akt). Conclusions: The results show that activation of Akt and ERK1/2 is involved in ghrelin-mediated regulation of protein expression of antioxidant enzymes and iNOS in the rat liver.",
journal = "Archives of Medical Science",
title = "Effects of ghrelin on protein expression of antioxidative enzymes and iNOS in the rat liver",
volume = "10",
number = "4",
pages = "806-816",
doi = "10.5114/aoms.2014.44872"
}

Dobutović, B., Sudar, E., Tepavčević, S., Đorđević, J. D., Đorđević, A. D., Radoičić, M. B.,& Isenović, E. R.. (2014). Effects of ghrelin on protein expression of antioxidative enzymes and iNOS in the rat liver. in Archives of Medical Science, 10(4), 806-816.
https://doi.org/10.5114/aoms.2014.44872

Dobutović B, Sudar E, Tepavčević S, Đorđević JD, Đorđević AD, Radoičić MB, Isenović ER. Effects of ghrelin on protein expression of antioxidative enzymes and iNOS in the rat liver. in Archives of Medical Science. 2014;10(4):806-816.
doi:10.5114/aoms.2014.44872 .

Dobutović, Branislava, Sudar, Emina, Tepavčević, Snežana, Đorđević, Jelena D., Đorđević, Ana D., Radoičić, Marija B., Isenović, Esma R., "Effects of ghrelin on protein expression of antioxidative enzymes and iNOS in the rat liver" in Archives of Medical Science, 10, no. 4 (2014):806-816,
https://doi.org/10.5114/aoms.2014.44872 . .

TY  - JOUR
AU  - Smiljanić, Katarina
AU  - Obradović, Milan M.
AU  - Jovanović, Aleksandra
AU  - Đorđević, Jelena D.
AU  - Dobutović, Branislava
AU  - Jevremovic, Danimir
AU  - Marche, Pierre
AU  - Isenović, Esma R.
PY  - 2014
UR  - https://vinar.vin.bg.ac.rs/handle/123456789/134
AB  - In this study, the role of epidermal growth factor receptor (EGFR), extracellular signal-regulated kinase (ERK1/2), heparin-binding EGF-like growth factor (HB-EGF), general metalloproteinases, matrix metalloproteinases-2 (MMP-2) in mediating the mitogenic action of thrombin in rat vascular smooth muscle cells (VSMC) was investigated. The incubation of rat VSMC with thrombin (1 U/ml) for 5 min resulted in significant (p LT 0.001) increase of ERK1/2 phosphorylation by 8.7 +/- A 0.9-fold, EGFR phosphorylation by 8.5 +/- A 1.3-fold (p LT 0.001) and DNA synthesis by 3.6 +/- A 0.4-fold (p LT 0.001). Separate 30-min pretreatments with EGFR tyrosine kinase irreversible inhibitor, 10 A mu M PD169540 (PD), and 20 A mu M anti-HB-EGF antibody significantly reduced thrombin-stimulated EGFR and ERK1/2 phosphorylation by 81, 72 % and by 48 and 61 %, respectively. Furthermore, the same pretreatments with PD or anti-HB-EGF antibody reduced thrombin-induced VSMC proliferation by 44 and 45 %, respectively. In addition, 30-min pretreatments with 10 A mu M specific MMP-2 inhibitor significantly reduced thrombin-stimulated phosphorylation of both EGFR and ERK1/2 by 25 %. Moreover, the same pretreatment with MMP-2 inhibitor reduced thrombin-induced VSMC proliferation by 45 %. These results show that the thrombin-induced DNA synthesis correlates with the level of ERK1/2 activation rather than EGFR activation. These results further suggest that thrombin acts through EGFR and ERK 1/2 signaling pathways involving MMP-2 to upregulate proliferation of VSMC.
T2  - Molecular and Cellular Biochemistry
T1  - Thrombin stimulates VSMC proliferation through an EGFR-dependent pathway: involvement of MMP-2
VL  - 396
IS  - 1-2
SP  - 147
EP  - 160
DO  - 10.1007/s11010-014-2151-y
ER  - 

@article{
author = "Smiljanić, Katarina and Obradović, Milan M. and Jovanović, Aleksandra and Đorđević, Jelena D. and Dobutović, Branislava and Jevremovic, Danimir and Marche, Pierre and Isenović, Esma R.",
year = "2014",
abstract = "In this study, the role of epidermal growth factor receptor (EGFR), extracellular signal-regulated kinase (ERK1/2), heparin-binding EGF-like growth factor (HB-EGF), general metalloproteinases, matrix metalloproteinases-2 (MMP-2) in mediating the mitogenic action of thrombin in rat vascular smooth muscle cells (VSMC) was investigated. The incubation of rat VSMC with thrombin (1 U/ml) for 5 min resulted in significant (p LT 0.001) increase of ERK1/2 phosphorylation by 8.7 +/- A 0.9-fold, EGFR phosphorylation by 8.5 +/- A 1.3-fold (p LT 0.001) and DNA synthesis by 3.6 +/- A 0.4-fold (p LT 0.001). Separate 30-min pretreatments with EGFR tyrosine kinase irreversible inhibitor, 10 A mu M PD169540 (PD), and 20 A mu M anti-HB-EGF antibody significantly reduced thrombin-stimulated EGFR and ERK1/2 phosphorylation by 81, 72 % and by 48 and 61 %, respectively. Furthermore, the same pretreatments with PD or anti-HB-EGF antibody reduced thrombin-induced VSMC proliferation by 44 and 45 %, respectively. In addition, 30-min pretreatments with 10 A mu M specific MMP-2 inhibitor significantly reduced thrombin-stimulated phosphorylation of both EGFR and ERK1/2 by 25 %. Moreover, the same pretreatment with MMP-2 inhibitor reduced thrombin-induced VSMC proliferation by 45 %. These results show that the thrombin-induced DNA synthesis correlates with the level of ERK1/2 activation rather than EGFR activation. These results further suggest that thrombin acts through EGFR and ERK 1/2 signaling pathways involving MMP-2 to upregulate proliferation of VSMC.",
journal = "Molecular and Cellular Biochemistry",
title = "Thrombin stimulates VSMC proliferation through an EGFR-dependent pathway: involvement of MMP-2",
volume = "396",
number = "1-2",
pages = "147-160",
doi = "10.1007/s11010-014-2151-y"
}

Smiljanić, K., Obradović, M. M., Jovanović, A., Đorđević, J. D., Dobutović, B., Jevremovic, D., Marche, P.,& Isenović, E. R.. (2014). Thrombin stimulates VSMC proliferation through an EGFR-dependent pathway: involvement of MMP-2. in Molecular and Cellular Biochemistry, 396(1-2), 147-160.
https://doi.org/10.1007/s11010-014-2151-y

Smiljanić K, Obradović MM, Jovanović A, Đorđević JD, Dobutović B, Jevremovic D, Marche P, Isenović ER. Thrombin stimulates VSMC proliferation through an EGFR-dependent pathway: involvement of MMP-2. in Molecular and Cellular Biochemistry. 2014;396(1-2):147-160.
doi:10.1007/s11010-014-2151-y .

Smiljanić, Katarina, Obradović, Milan M., Jovanović, Aleksandra, Đorđević, Jelena D., Dobutović, Branislava, Jevremovic, Danimir, Marche, Pierre, Isenović, Esma R., "Thrombin stimulates VSMC proliferation through an EGFR-dependent pathway: involvement of MMP-2" in Molecular and Cellular Biochemistry, 396, no. 1-2 (2014):147-160,
https://doi.org/10.1007/s11010-014-2151-y . .

TY  - JOUR
AU  - Popović, Milan
AU  - Smiljanić, Katarina
AU  - Dobutović, Branislava
AU  - Syrovets, Tatiana
AU  - Simmet, Thomas
AU  - Isenović, Esma R.
PY  - 2012
UR  - https://vinar.vin.bg.ac.rs/handle/123456789/4578
AB  - Vascular endothelium is a key regulator of homeostasis. In physiological conditions it mediates vascular dilatation, prevents platelet adhesion, and inhibits thrombin generation. However, endothelial dysfunction caused by physical injury of the vascular wall, for example during balloon angioplasty, acute or chronic inflammation, such as in atherothrombosis, creates a proinflammatory environment which supports leukocyte transmigration toward inflammatory sites. At the same time, the dysfunction promotes thrombin generation, fibrin deposition, and coagulation. The serine protease thrombin plays a pivotal role in the coagulation cascade. However, thrombin is not only the key effector of coagulation cascade; it also plays a significant role in inflammatory diseases. It shows an array of effects on endothelial cells, vascular smooth muscle cells, monocytes, and platelets, all of which participate in the vascular pathophysiology such as atherothrombosis. Therefore, thrombin can be considered as an important modulatory molecule of vascular homeostasis. This review summarizes the existing evidence on the role of thrombin in vascular inflammation.
T2  - Molecular and Cellular Biochemistry
T1  - Thrombin and vascular inflammation
VL  - 359
IS  - 1-2
SP  - 301
EP  - 313
DO  - 10.1007/s11010-011-1024-x
ER  - 

@article{
author = "Popović, Milan and Smiljanić, Katarina and Dobutović, Branislava and Syrovets, Tatiana and Simmet, Thomas and Isenović, Esma R.",
year = "2012",
abstract = "Vascular endothelium is a key regulator of homeostasis. In physiological conditions it mediates vascular dilatation, prevents platelet adhesion, and inhibits thrombin generation. However, endothelial dysfunction caused by physical injury of the vascular wall, for example during balloon angioplasty, acute or chronic inflammation, such as in atherothrombosis, creates a proinflammatory environment which supports leukocyte transmigration toward inflammatory sites. At the same time, the dysfunction promotes thrombin generation, fibrin deposition, and coagulation. The serine protease thrombin plays a pivotal role in the coagulation cascade. However, thrombin is not only the key effector of coagulation cascade; it also plays a significant role in inflammatory diseases. It shows an array of effects on endothelial cells, vascular smooth muscle cells, monocytes, and platelets, all of which participate in the vascular pathophysiology such as atherothrombosis. Therefore, thrombin can be considered as an important modulatory molecule of vascular homeostasis. This review summarizes the existing evidence on the role of thrombin in vascular inflammation.",
journal = "Molecular and Cellular Biochemistry",
title = "Thrombin and vascular inflammation",
volume = "359",
number = "1-2",
pages = "301-313",
doi = "10.1007/s11010-011-1024-x"
}

Popović, M., Smiljanić, K., Dobutović, B., Syrovets, T., Simmet, T.,& Isenović, E. R.. (2012). Thrombin and vascular inflammation. in Molecular and Cellular Biochemistry, 359(1-2), 301-313.
https://doi.org/10.1007/s11010-011-1024-x

Popović M, Smiljanić K, Dobutović B, Syrovets T, Simmet T, Isenović ER. Thrombin and vascular inflammation. in Molecular and Cellular Biochemistry. 2012;359(1-2):301-313.
doi:10.1007/s11010-011-1024-x .

Popović, Milan, Smiljanić, Katarina, Dobutović, Branislava, Syrovets, Tatiana, Simmet, Thomas, Isenović, Esma R., "Thrombin and vascular inflammation" in Molecular and Cellular Biochemistry, 359, no. 1-2 (2012):301-313,
https://doi.org/10.1007/s11010-011-1024-x . .

TY  - JOUR
AU  - Popović, Milan
AU  - Smiljanić, Katarina
AU  - Dobutović, Branislava
AU  - Syrovets, Tatiana
AU  - Simmet, Thomas
AU  - Isenović, Esma R.
PY  - 2012
UR  - https://vinar.vin.bg.ac.rs/handle/123456789/4670
AB  - Vascular endothelium, as a key regulator of hemostasis, mediates vascular dilatation, prevents platelet adhesion, and inhibits thrombin generation. Endothelial dysfunction caused by acute or chronic inflammation, such as in atherosclerosis, creates a proinflammatory environment which supports leukocyte transmigration toward inflammatory sites, and at the same time promotes coagulation, thrombin generation, and fibrin deposition in an attempt to close the wound. Life-long persistent infection with human cytomegalovirus (HCMV) has been associated with atherosclerosis. In vivo studies have revealed that HCMV infection of the vessel wall affects various cells including monocytes/macrophages, smooth muscle cells (SMCs) and endothelial cells (ECs). HCMV-infected SMCs within vascular lesions display enhanced proliferation and impaired apoptosis, which contribute to intima-media thickening, plaque formation and restenosis. Monocytes play a central role in the process of viral dissemination, whereas ECs may represent a viral reservoir, maintaining persistent infection in HCMV-infected atherosclerotic patients following the primary infection. Persistent infection leads to dysfunction of ECs and activates proinflammatory signaling involving nuclear factor kappa B, specificity protein 1, and phosphatidylinositol 3-kinase, as well as expression of platelet-derived growth factor receptor. Activation of these pathways promotes enhanced proliferation and migration of monocytes and SMCs into the intima of the vascular wall as well as lipid accumulation and expansion of the atherosclerotic lesion. Moreover, HCMV infection induces enhanced expression of endothelial adhesion molecules and modifies the proteolytic balance in monocytes and macrophages. As a consequence, infected endothelium recruits naive monocytes from the blood stream, and the concomitant interaction between infected ECs and monocytes enables virus transfer to migrating monocytes. Endothelial damage promotes thrombin generation linking inflammation and coagulation. HCMV, in turn, enhances the thrombin generation. The virus carries on its surface the molecular machinery necessary to initiate thrombin generation, and in addition, may interact with the prothrombinase protein complex thereby facilitating thrombin generation. Thus, infection of endothelium may significantly increase the production of thrombin. This might not only contribute to thrombosis in patients with atherosclerosis, but might also induce thrombin-dependent proinflammatory cell activation. This review summarizes the existing evidence on the role of HCMV in vascular inflammation.
T2  - Journal of Thrombosis and Thrombolysis
T1  - Human cytomegalovirus infection and atherothrombosis
VL  - 33
IS  - 2
SP  - 160
EP  - 172
DO  - 10.1007/s11239-011-0662-x
ER  - 

@article{
author = "Popović, Milan and Smiljanić, Katarina and Dobutović, Branislava and Syrovets, Tatiana and Simmet, Thomas and Isenović, Esma R.",
year = "2012",
abstract = "Vascular endothelium, as a key regulator of hemostasis, mediates vascular dilatation, prevents platelet adhesion, and inhibits thrombin generation. Endothelial dysfunction caused by acute or chronic inflammation, such as in atherosclerosis, creates a proinflammatory environment which supports leukocyte transmigration toward inflammatory sites, and at the same time promotes coagulation, thrombin generation, and fibrin deposition in an attempt to close the wound. Life-long persistent infection with human cytomegalovirus (HCMV) has been associated with atherosclerosis. In vivo studies have revealed that HCMV infection of the vessel wall affects various cells including monocytes/macrophages, smooth muscle cells (SMCs) and endothelial cells (ECs). HCMV-infected SMCs within vascular lesions display enhanced proliferation and impaired apoptosis, which contribute to intima-media thickening, plaque formation and restenosis. Monocytes play a central role in the process of viral dissemination, whereas ECs may represent a viral reservoir, maintaining persistent infection in HCMV-infected atherosclerotic patients following the primary infection. Persistent infection leads to dysfunction of ECs and activates proinflammatory signaling involving nuclear factor kappa B, specificity protein 1, and phosphatidylinositol 3-kinase, as well as expression of platelet-derived growth factor receptor. Activation of these pathways promotes enhanced proliferation and migration of monocytes and SMCs into the intima of the vascular wall as well as lipid accumulation and expansion of the atherosclerotic lesion. Moreover, HCMV infection induces enhanced expression of endothelial adhesion molecules and modifies the proteolytic balance in monocytes and macrophages. As a consequence, infected endothelium recruits naive monocytes from the blood stream, and the concomitant interaction between infected ECs and monocytes enables virus transfer to migrating monocytes. Endothelial damage promotes thrombin generation linking inflammation and coagulation. HCMV, in turn, enhances the thrombin generation. The virus carries on its surface the molecular machinery necessary to initiate thrombin generation, and in addition, may interact with the prothrombinase protein complex thereby facilitating thrombin generation. Thus, infection of endothelium may significantly increase the production of thrombin. This might not only contribute to thrombosis in patients with atherosclerosis, but might also induce thrombin-dependent proinflammatory cell activation. This review summarizes the existing evidence on the role of HCMV in vascular inflammation.",
journal = "Journal of Thrombosis and Thrombolysis",
title = "Human cytomegalovirus infection and atherothrombosis",
volume = "33",
number = "2",
pages = "160-172",
doi = "10.1007/s11239-011-0662-x"
}

Popović, M., Smiljanić, K., Dobutović, B., Syrovets, T., Simmet, T.,& Isenović, E. R.. (2012). Human cytomegalovirus infection and atherothrombosis. in Journal of Thrombosis and Thrombolysis, 33(2), 160-172.
https://doi.org/10.1007/s11239-011-0662-x

Popović M, Smiljanić K, Dobutović B, Syrovets T, Simmet T, Isenović ER. Human cytomegalovirus infection and atherothrombosis. in Journal of Thrombosis and Thrombolysis. 2012;33(2):160-172.
doi:10.1007/s11239-011-0662-x .

Popović, Milan, Smiljanić, Katarina, Dobutović, Branislava, Syrovets, Tatiana, Simmet, Thomas, Isenović, Esma R., "Human cytomegalovirus infection and atherothrombosis" in Journal of Thrombosis and Thrombolysis, 33, no. 2 (2012):160-172,
https://doi.org/10.1007/s11239-011-0662-x . .

TY  - JOUR
AU  - Sudar, Emina
AU  - Dobutović, Branislava
AU  - Soskić, Sanja S.
AU  - Mandušić, Vesna
AU  - Žakula, Zorica
AU  - Misirkić, Maja
AU  - Vucicevic, Ljubica
AU  - Janjetović, Kristina D.
AU  - Trajković, Vladimir S.
AU  - Mikhailidis, Dimitri P.
AU  - Isenović, Esma R.
PY  - 2011
UR  - https://vinar.vin.bg.ac.rs/handle/123456789/4317
AB  - The purpose of this study was to examine the effects of ghrelin on protein kinase B (Akt) and mitogen-activated protein kinase p42/44 (ERK1/2) activation as well as ghrelin effects on inducible nitric oxide (NO) synthase (iNOS; for gene Nos2) activity/expression in rat hearts. Male Wistar rats were treated with ghrelin (0.3 nmol/5 mu l) or an equal volume of phosphate-buffered saline, injected every 24 h into the lateral cerebral ventricle for 5 days and 2 h after the last treatment the animals were sacrificed. Serum NO, l-arginine (l-Arg), and arginase activity were measured spectrophotometrically. For phosphorylation of Akt, ERK1/2, and iNOS protein expression, Western blot method was used. The expression of Nos2 mRNA was measured by the quantitative real-time polymerase chain reaction (qRT-PCR). Treatment with ghrelin significantly increased NO production in serum by 1.4-fold compared with control. The concentration of l-Arg was significantly higher in ghrelin-treated rats than in control while arginase activity was significantly lower in ghrelin-treated than in control hearts. Ghrelin treatment increased phosphorylation of Akt by 1.9-fold and ERK1/2 by 1.6-fold and increased iNOS expression by 2.5-fold compared with control. In addition, ghrelin treatment increased Nos2 gene expression by 2.2-fold as determined by qRT-PCR. These results indicate that ghrelin regulation of iNOS expression/activity is mediated via Akt/ERK1/2 signaling pathway. These results may be relevant to understanding molecular mechanisms underlying direct cardiovascular actions of ghrelin.
T2  - Journal of Physiology and Biochemistry
T1  - Regulation of inducible nitric oxide synthase activity/expression in rat hearts from ghrelin-treated rats
VL  - 67
IS  - 2
SP  - 195
EP  - 204
DO  - 10.1007/s13105-010-0063-1
ER  - 

@article{
author = "Sudar, Emina and Dobutović, Branislava and Soskić, Sanja S. and Mandušić, Vesna and Žakula, Zorica and Misirkić, Maja and Vucicevic, Ljubica and Janjetović, Kristina D. and Trajković, Vladimir S. and Mikhailidis, Dimitri P. and Isenović, Esma R.",
year = "2011",
abstract = "The purpose of this study was to examine the effects of ghrelin on protein kinase B (Akt) and mitogen-activated protein kinase p42/44 (ERK1/2) activation as well as ghrelin effects on inducible nitric oxide (NO) synthase (iNOS; for gene Nos2) activity/expression in rat hearts. Male Wistar rats were treated with ghrelin (0.3 nmol/5 mu l) or an equal volume of phosphate-buffered saline, injected every 24 h into the lateral cerebral ventricle for 5 days and 2 h after the last treatment the animals were sacrificed. Serum NO, l-arginine (l-Arg), and arginase activity were measured spectrophotometrically. For phosphorylation of Akt, ERK1/2, and iNOS protein expression, Western blot method was used. The expression of Nos2 mRNA was measured by the quantitative real-time polymerase chain reaction (qRT-PCR). Treatment with ghrelin significantly increased NO production in serum by 1.4-fold compared with control. The concentration of l-Arg was significantly higher in ghrelin-treated rats than in control while arginase activity was significantly lower in ghrelin-treated than in control hearts. Ghrelin treatment increased phosphorylation of Akt by 1.9-fold and ERK1/2 by 1.6-fold and increased iNOS expression by 2.5-fold compared with control. In addition, ghrelin treatment increased Nos2 gene expression by 2.2-fold as determined by qRT-PCR. These results indicate that ghrelin regulation of iNOS expression/activity is mediated via Akt/ERK1/2 signaling pathway. These results may be relevant to understanding molecular mechanisms underlying direct cardiovascular actions of ghrelin.",
journal = "Journal of Physiology and Biochemistry",
title = "Regulation of inducible nitric oxide synthase activity/expression in rat hearts from ghrelin-treated rats",
volume = "67",
number = "2",
pages = "195-204",
doi = "10.1007/s13105-010-0063-1"
}

Sudar, E., Dobutović, B., Soskić, S. S., Mandušić, V., Žakula, Z., Misirkić, M., Vucicevic, L., Janjetović, K. D., Trajković, V. S., Mikhailidis, D. P.,& Isenović, E. R.. (2011). Regulation of inducible nitric oxide synthase activity/expression in rat hearts from ghrelin-treated rats. in Journal of Physiology and Biochemistry, 67(2), 195-204.
https://doi.org/10.1007/s13105-010-0063-1

Sudar E, Dobutović B, Soskić SS, Mandušić V, Žakula Z, Misirkić M, Vucicevic L, Janjetović KD, Trajković VS, Mikhailidis DP, Isenović ER. Regulation of inducible nitric oxide synthase activity/expression in rat hearts from ghrelin-treated rats. in Journal of Physiology and Biochemistry. 2011;67(2):195-204.
doi:10.1007/s13105-010-0063-1 .

Sudar, Emina, Dobutović, Branislava, Soskić, Sanja S., Mandušić, Vesna, Žakula, Zorica, Misirkić, Maja, Vucicevic, Ljubica, Janjetović, Kristina D., Trajković, Vladimir S., Mikhailidis, Dimitri P., Isenović, Esma R., "Regulation of inducible nitric oxide synthase activity/expression in rat hearts from ghrelin-treated rats" in Journal of Physiology and Biochemistry, 67, no. 2 (2011):195-204,
https://doi.org/10.1007/s13105-010-0063-1 . .

TY  - JOUR
AU  - Haidara, Mohamed A.
AU  - Mikhailidis, Dimitri P.
AU  - Yassin, Hanaa Z.
AU  - Dobutović, Branislava
AU  - Smiljanić, Katarina
AU  - Soskić, Sanja S.
AU  - Mousa, Shaker A.
AU  - Rizzo, Manfredi
AU  - Isenović, Esma R.
PY  - 2011
UR  - https://vinar.vin.bg.ac.rs/handle/123456789/4662
AB  - The metabolic syndrome (MetS) is common, and its associated risk burdens of diabetes and cardiovascular disease (CVD) are a major public health problem. The hypothesis that main constituent parameters of the MetS share common pathophysiologic mechanisms provides a conceptual framework for the future research. Exercise and weight loss can prevent insulin resistance and reduce the risk of diseases associated with the MetS. Interrupting intracellular and extracellular reactive oxygen species (ROS) overproduction could also contribute to normalizing the activation of metabolic pathways leading to the onset of diabetes, endothelial dysfunction, and cardiovascular (CV) complications. On the other hand, it is difficult to counteract the development of CV complications by using conventional antioxidants. Indeed, interest has focused on strategies that enhance the removal of ROS using either antioxidants or drugs that enhance endogenous antioxidant defense. Although these strategies have been effective in laboratory experiments, several clinical trials have shown that they do not reduce CV events, and in some cases antioxidants have actually worsened the outcome. More research is needed in this field.
T2  - Current Pharmaceutical Design
T1  - Evaluation of the Possible Contribution of Antioxidants Administration in Metabolic Syndrome
VL  - 17
IS  - 33
SP  - 3699
EP  - 3712
DO  - 10.2174/138161211798220882
ER  - 

@article{
author = "Haidara, Mohamed A. and Mikhailidis, Dimitri P. and Yassin, Hanaa Z. and Dobutović, Branislava and Smiljanić, Katarina and Soskić, Sanja S. and Mousa, Shaker A. and Rizzo, Manfredi and Isenović, Esma R.",
year = "2011",
abstract = "The metabolic syndrome (MetS) is common, and its associated risk burdens of diabetes and cardiovascular disease (CVD) are a major public health problem. The hypothesis that main constituent parameters of the MetS share common pathophysiologic mechanisms provides a conceptual framework for the future research. Exercise and weight loss can prevent insulin resistance and reduce the risk of diseases associated with the MetS. Interrupting intracellular and extracellular reactive oxygen species (ROS) overproduction could also contribute to normalizing the activation of metabolic pathways leading to the onset of diabetes, endothelial dysfunction, and cardiovascular (CV) complications. On the other hand, it is difficult to counteract the development of CV complications by using conventional antioxidants. Indeed, interest has focused on strategies that enhance the removal of ROS using either antioxidants or drugs that enhance endogenous antioxidant defense. Although these strategies have been effective in laboratory experiments, several clinical trials have shown that they do not reduce CV events, and in some cases antioxidants have actually worsened the outcome. More research is needed in this field.",
journal = "Current Pharmaceutical Design",
title = "Evaluation of the Possible Contribution of Antioxidants Administration in Metabolic Syndrome",
volume = "17",
number = "33",
pages = "3699-3712",
doi = "10.2174/138161211798220882"
}

Haidara, M. A., Mikhailidis, D. P., Yassin, H. Z., Dobutović, B., Smiljanić, K., Soskić, S. S., Mousa, S. A., Rizzo, M.,& Isenović, E. R.. (2011). Evaluation of the Possible Contribution of Antioxidants Administration in Metabolic Syndrome. in Current Pharmaceutical Design, 17(33), 3699-3712.
https://doi.org/10.2174/138161211798220882

Haidara MA, Mikhailidis DP, Yassin HZ, Dobutović B, Smiljanić K, Soskić SS, Mousa SA, Rizzo M, Isenović ER. Evaluation of the Possible Contribution of Antioxidants Administration in Metabolic Syndrome. in Current Pharmaceutical Design. 2011;17(33):3699-3712.
doi:10.2174/138161211798220882 .

Haidara, Mohamed A., Mikhailidis, Dimitri P., Yassin, Hanaa Z., Dobutović, Branislava, Smiljanić, Katarina, Soskić, Sanja S., Mousa, Shaker A., Rizzo, Manfredi, Isenović, Esma R., "Evaluation of the Possible Contribution of Antioxidants Administration in Metabolic Syndrome" in Current Pharmaceutical Design, 17, no. 33 (2011):3699-3712,
https://doi.org/10.2174/138161211798220882 . .

TY  - JOUR
AU  - Isenović, Esma R.
AU  - Soskić, Sanja S.
AU  - Trpković, Andreja
AU  - Dobutović, Branislava
AU  - Popović, Milan
AU  - Gluvić, Zoran
AU  - Putniković, Biljana
AU  - Marche, Pierre
PY  - 2010
UR  - https://vinar.vin.bg.ac.rs/handle/123456789/4209
AB  - Vascular smooth muscle cells (VSMC) respond to arterial wall injury by intimal proliferation and play a key role in atherogenesis by proliferating and migrating excessively in response to repeated injury, such as hypertension and atherosclerosis. In contrast, fully differentiated, quiescent VSMC allow arterial vasodilatation and vasoconstriction. Exaggerated and uncontrolled VSMC proliferation appears therefore to be a common feature of both atherosclerosis and hypertension. Signal transduction pathways in eukaryotic cells integrate diverse extracellular signals, and regulate complex biological responses such as growth, differentiation and death. One group of proline-directed Ser/Thr protein kinases, the mitogen-activated protein kinases (MAPKs), plays a central role in these signalling pathways. Much attention has focused in recent years on subfamilies of MAPKs, the extracellular signal regulated kinases (ERKs). Here we overview the work on ERKs 1 to 2, emphasising when possible their biological activities in VSMC proliferation. It is clear from numerosus studies including our own, that ERK1/ERK2 pathway has an imoprtant role in VSMC proliferation induced by insulin (INS) and thrombin. Despite the physiological and pathophysiological importance of INS and thrombin, possible signal transduction pathways involved in INS and thrombin regulation of VSMCs proliferation remains poorly understood. Thus, this review examines recent findings in signalling mechanisms involved in INS and thrombin-triggered VSMCs proliferation with particular emphasis on ERK1/2 signalling pathways. Future investigations should now focus on the mechanisms of MAPK activation which might therefore represent a new mechanism involved in the antiproliferative effect revealed in this review.
T2  - Current Pharmaceutical Design
T1  - Insulin, Thrombin, ERK1/2 Kinase and Vascular Smooth Muscle Cells Proliferation
VL  - 16
IS  - 35
SP  - 3895
EP  - 3902
DO  - 10.2174/138161210794454987
ER  - 

@article{
author = "Isenović, Esma R. and Soskić, Sanja S. and Trpković, Andreja and Dobutović, Branislava and Popović, Milan and Gluvić, Zoran and Putniković, Biljana and Marche, Pierre",
year = "2010",
abstract = "Vascular smooth muscle cells (VSMC) respond to arterial wall injury by intimal proliferation and play a key role in atherogenesis by proliferating and migrating excessively in response to repeated injury, such as hypertension and atherosclerosis. In contrast, fully differentiated, quiescent VSMC allow arterial vasodilatation and vasoconstriction. Exaggerated and uncontrolled VSMC proliferation appears therefore to be a common feature of both atherosclerosis and hypertension. Signal transduction pathways in eukaryotic cells integrate diverse extracellular signals, and regulate complex biological responses such as growth, differentiation and death. One group of proline-directed Ser/Thr protein kinases, the mitogen-activated protein kinases (MAPKs), plays a central role in these signalling pathways. Much attention has focused in recent years on subfamilies of MAPKs, the extracellular signal regulated kinases (ERKs). Here we overview the work on ERKs 1 to 2, emphasising when possible their biological activities in VSMC proliferation. It is clear from numerosus studies including our own, that ERK1/ERK2 pathway has an imoprtant role in VSMC proliferation induced by insulin (INS) and thrombin. Despite the physiological and pathophysiological importance of INS and thrombin, possible signal transduction pathways involved in INS and thrombin regulation of VSMCs proliferation remains poorly understood. Thus, this review examines recent findings in signalling mechanisms involved in INS and thrombin-triggered VSMCs proliferation with particular emphasis on ERK1/2 signalling pathways. Future investigations should now focus on the mechanisms of MAPK activation which might therefore represent a new mechanism involved in the antiproliferative effect revealed in this review.",
journal = "Current Pharmaceutical Design",
title = "Insulin, Thrombin, ERK1/2 Kinase and Vascular Smooth Muscle Cells Proliferation",
volume = "16",
number = "35",
pages = "3895-3902",
doi = "10.2174/138161210794454987"
}

Isenović, E. R., Soskić, S. S., Trpković, A., Dobutović, B., Popović, M., Gluvić, Z., Putniković, B.,& Marche, P.. (2010). Insulin, Thrombin, ERK1/2 Kinase and Vascular Smooth Muscle Cells Proliferation. in Current Pharmaceutical Design, 16(35), 3895-3902.
https://doi.org/10.2174/138161210794454987

Isenović ER, Soskić SS, Trpković A, Dobutović B, Popović M, Gluvić Z, Putniković B, Marche P. Insulin, Thrombin, ERK1/2 Kinase and Vascular Smooth Muscle Cells Proliferation. in Current Pharmaceutical Design. 2010;16(35):3895-3902.
doi:10.2174/138161210794454987 .

Isenović, Esma R., Soskić, Sanja S., Trpković, Andreja, Dobutović, Branislava, Popović, Milan, Gluvić, Zoran, Putniković, Biljana, Marche, Pierre, "Insulin, Thrombin, ERK1/2 Kinase and Vascular Smooth Muscle Cells Proliferation" in Current Pharmaceutical Design, 16, no. 35 (2010):3895-3902,
https://doi.org/10.2174/138161210794454987 . .

TY  - JOUR
AU  - Jozanov-Stankov, Olga
AU  - Đurić, Jovanka
AU  - Dobutović, Branislava
AU  - Isenović, Esma R.
PY  - 2009
UR  - https://vinar.vin.bg.ac.rs/handle/123456789/3784
AB  - Despite its importance for human health, the capacity of the antioxidative defense system (AOS) is still not included among regular biochemical analyses. In this study, we estimated the blood plasma level of the total antioxidant status (TAS) as an appropriate parameter for AOS monitoring with the aim of including it among other biochemical parameters in the regular control of health of the working population. We have applied a method developed by Randox Laboratories (England) that can be routinely performed on automatic chemical analyzers. The TAS level, in correlation with corresponding biochemical parameters, could contribute to better evaluation of the health of individuals and the working population.
T2  - Archives of Biological Sciences
T1  - Determination of Total Antioxidant Status (Tas) as a Biochemical Parameter in Control of Workers Health
VL  - 61
IS  - 3
SP  - 375
EP  - 382
DO  - 10.2298/ABS0903375J
ER  - 

@article{
author = "Jozanov-Stankov, Olga and Đurić, Jovanka and Dobutović, Branislava and Isenović, Esma R.",
year = "2009",
abstract = "Despite its importance for human health, the capacity of the antioxidative defense system (AOS) is still not included among regular biochemical analyses. In this study, we estimated the blood plasma level of the total antioxidant status (TAS) as an appropriate parameter for AOS monitoring with the aim of including it among other biochemical parameters in the regular control of health of the working population. We have applied a method developed by Randox Laboratories (England) that can be routinely performed on automatic chemical analyzers. The TAS level, in correlation with corresponding biochemical parameters, could contribute to better evaluation of the health of individuals and the working population.",
journal = "Archives of Biological Sciences",
title = "Determination of Total Antioxidant Status (Tas) as a Biochemical Parameter in Control of Workers Health",
volume = "61",
number = "3",
pages = "375-382",
doi = "10.2298/ABS0903375J"
}

Jozanov-Stankov, O., Đurić, J., Dobutović, B.,& Isenović, E. R.. (2009). Determination of Total Antioxidant Status (Tas) as a Biochemical Parameter in Control of Workers Health. in Archives of Biological Sciences, 61(3), 375-382.
https://doi.org/10.2298/ABS0903375J

Jozanov-Stankov O, Đurić J, Dobutović B, Isenović ER. Determination of Total Antioxidant Status (Tas) as a Biochemical Parameter in Control of Workers Health. in Archives of Biological Sciences. 2009;61(3):375-382.
doi:10.2298/ABS0903375J .

Jozanov-Stankov, Olga, Đurić, Jovanka, Dobutović, Branislava, Isenović, Esma R., "Determination of Total Antioxidant Status (Tas) as a Biochemical Parameter in Control of Workers Health" in Archives of Biological Sciences, 61, no. 3 (2009):375-382,
https://doi.org/10.2298/ABS0903375J . .

TY  - JOUR
AU  - Isenović, Esma R.
AU  - Fretaud, Maxence
AU  - Dobutović, Branislava
AU  - Sudar, Emina
AU  - Smiljanić, Katarina
AU  - Zarić, Božidarka
AU  - Trpković, Andreja
AU  - Marche, Pierre
PY  - 2009
UR  - https://vinar.vin.bg.ac.rs/handle/123456789/3644
AB  - Insulin (INS) via INS receptor acts as a mitogen in vascular smooth muscle cells (VSMCs) through stimulation of multiple signaling mechanisms, including p42/44 mitogen-activated protein kinase (ERK1/2) and phosphatidyl inositol-3 kinase (PI3K). In addition, cytosolic phospholipase 2 (cPLA(2)) is linked to VSMCs proliferation. However, the upstream mechanisms responsible for activation of cPLA(2) are not well defined. Therefore, this investigation used primary cultured rat VSMCs to examine the role of PI3K and ERK1/2 in the INS-dependent phosphorylation of cPLA(2) and proliferation induced by INS. Exposure of VSMCs to INS (100 nM) for 10 min increased the phosphorylation of cPLA(2) by 1.5-fold (p LT 0.01), which was blocked by the cPLA(2) inhibitor MAFP (10 mu M; 15 min). Similarly, the PI3K inhibitor LY294002 (10 mu M; 15 min) and ERK1/2 inhibitor PD98059 (20 mu M; 15 min) abolished the INS-mediated increase in cPLA(2) phosphorylation by 59% (p LT 0.001), and by 75% (p LT 0.001), respectively. Further, inhibition of cPLA2 with cPLA2 inhibitor MAFP abolished the INS-stimulated ERK1/2 phosphorylation by 65% (p LT 0.01). Incubation of rat VSMCs with INS resulted in an increase of VSMCs proliferation by 85% (p LT 0.001). The effect of INS on VSMCs proliferation was significantly (p LT 0.01) reduced by pretreatment with MAFP. Thus, we hypothesized that INS stimulates VSMCs proliferation via a mechanism involving the PI3K-dependent activation of cPLA(2) and release of arachidonic acid (AA), which activates ERK1/2 and further amplifies cPLA(2) activity. (C) 2009 International Federation for Cell Biology. Published by Elsevier Ltd. All rights reserved.
T2  - Cell Biology International
T1  - A novel hypothesis regarding the possible involvement of cytosolic phospholipase 2 in insulin-stimulated proliferation of vascular smooth muscle cells
VL  - 33
IS  - 3
SP  - 386
EP  - 392
DO  - 10.1016/j.cellbi.2009.01.010
ER  - 

@article{
author = "Isenović, Esma R. and Fretaud, Maxence and Dobutović, Branislava and Sudar, Emina and Smiljanić, Katarina and Zarić, Božidarka and Trpković, Andreja and Marche, Pierre",
year = "2009",
abstract = "Insulin (INS) via INS receptor acts as a mitogen in vascular smooth muscle cells (VSMCs) through stimulation of multiple signaling mechanisms, including p42/44 mitogen-activated protein kinase (ERK1/2) and phosphatidyl inositol-3 kinase (PI3K). In addition, cytosolic phospholipase 2 (cPLA(2)) is linked to VSMCs proliferation. However, the upstream mechanisms responsible for activation of cPLA(2) are not well defined. Therefore, this investigation used primary cultured rat VSMCs to examine the role of PI3K and ERK1/2 in the INS-dependent phosphorylation of cPLA(2) and proliferation induced by INS. Exposure of VSMCs to INS (100 nM) for 10 min increased the phosphorylation of cPLA(2) by 1.5-fold (p LT 0.01), which was blocked by the cPLA(2) inhibitor MAFP (10 mu M; 15 min). Similarly, the PI3K inhibitor LY294002 (10 mu M; 15 min) and ERK1/2 inhibitor PD98059 (20 mu M; 15 min) abolished the INS-mediated increase in cPLA(2) phosphorylation by 59% (p LT 0.001), and by 75% (p LT 0.001), respectively. Further, inhibition of cPLA2 with cPLA2 inhibitor MAFP abolished the INS-stimulated ERK1/2 phosphorylation by 65% (p LT 0.01). Incubation of rat VSMCs with INS resulted in an increase of VSMCs proliferation by 85% (p LT 0.001). The effect of INS on VSMCs proliferation was significantly (p LT 0.01) reduced by pretreatment with MAFP. Thus, we hypothesized that INS stimulates VSMCs proliferation via a mechanism involving the PI3K-dependent activation of cPLA(2) and release of arachidonic acid (AA), which activates ERK1/2 and further amplifies cPLA(2) activity. (C) 2009 International Federation for Cell Biology. Published by Elsevier Ltd. All rights reserved.",
journal = "Cell Biology International",
title = "A novel hypothesis regarding the possible involvement of cytosolic phospholipase 2 in insulin-stimulated proliferation of vascular smooth muscle cells",
volume = "33",
number = "3",
pages = "386-392",
doi = "10.1016/j.cellbi.2009.01.010"
}

Isenović, E. R., Fretaud, M., Dobutović, B., Sudar, E., Smiljanić, K., Zarić, B., Trpković, A.,& Marche, P.. (2009). A novel hypothesis regarding the possible involvement of cytosolic phospholipase 2 in insulin-stimulated proliferation of vascular smooth muscle cells. in Cell Biology International, 33(3), 386-392.
https://doi.org/10.1016/j.cellbi.2009.01.010

Isenović ER, Fretaud M, Dobutović B, Sudar E, Smiljanić K, Zarić B, Trpković A, Marche P. A novel hypothesis regarding the possible involvement of cytosolic phospholipase 2 in insulin-stimulated proliferation of vascular smooth muscle cells. in Cell Biology International. 2009;33(3):386-392.
doi:10.1016/j.cellbi.2009.01.010 .

Isenović, Esma R., Fretaud, Maxence, Dobutović, Branislava, Sudar, Emina, Smiljanić, Katarina, Zarić, Božidarka, Trpković, Andreja, Marche, Pierre, "A novel hypothesis regarding the possible involvement of cytosolic phospholipase 2 in insulin-stimulated proliferation of vascular smooth muscle cells" in Cell Biology International, 33, no. 3 (2009):386-392,
https://doi.org/10.1016/j.cellbi.2009.01.010 . .

TY  - JOUR
AU  - Sudar, Emina
AU  - Dobutović, Branislava
AU  - Milosavljević, Tijana
AU  - Putniković, Biljana
AU  - Gluvić, Zoran
AU  - Isenović, Esma R.
PY  - 2009
UR  - https://vinar.vin.bg.ac.rs/handle/123456789/3804
AB  - Insulin (INS) and beta-estradiol (E(2)) have vascular effects partially through stimulation of protein kinase B (Akt) phosphorylation. Employing adult rat cardiomyocytes (ARC), the effects of acute (15 min) stimulation with INS (10 mIU/ml) and prolonged (2 hours and 24 hours) stimulation with E(2) alone or in combination, were assessed with respect to protein levels of Akt. Exposure to INS for 15 minutes enhanced Akt Ser(473) phosphorylation. The combined treatment had a greater effect on Akt phosphorylation then the effect of INS alone. The results suggest that INS and E(2) may interact through Akt in regulating metabolic processes.
T2  - Acta Chimica Slovenica
T1  - Interactive Effects of Insulin and beta-Estradiol on Protein Kinase B Phosphorylation in Adult Rat Cardiomyocytes
VL  - 56
IS  - 3
SP  - 723
EP  - 728
UR  - https://hdl.handle.net/21.15107/rcub_vinar_3804
ER  - 

@article{
author = "Sudar, Emina and Dobutović, Branislava and Milosavljević, Tijana and Putniković, Biljana and Gluvić, Zoran and Isenović, Esma R.",
year = "2009",
abstract = "Insulin (INS) and beta-estradiol (E(2)) have vascular effects partially through stimulation of protein kinase B (Akt) phosphorylation. Employing adult rat cardiomyocytes (ARC), the effects of acute (15 min) stimulation with INS (10 mIU/ml) and prolonged (2 hours and 24 hours) stimulation with E(2) alone or in combination, were assessed with respect to protein levels of Akt. Exposure to INS for 15 minutes enhanced Akt Ser(473) phosphorylation. The combined treatment had a greater effect on Akt phosphorylation then the effect of INS alone. The results suggest that INS and E(2) may interact through Akt in regulating metabolic processes.",
journal = "Acta Chimica Slovenica",
title = "Interactive Effects of Insulin and beta-Estradiol on Protein Kinase B Phosphorylation in Adult Rat Cardiomyocytes",
volume = "56",
number = "3",
pages = "723-728",
url = "https://hdl.handle.net/21.15107/rcub_vinar_3804"
}

Sudar, E., Dobutović, B., Milosavljević, T., Putniković, B., Gluvić, Z.,& Isenović, E. R.. (2009). Interactive Effects of Insulin and beta-Estradiol on Protein Kinase B Phosphorylation in Adult Rat Cardiomyocytes. in Acta Chimica Slovenica, 56(3), 723-728.
https://hdl.handle.net/21.15107/rcub_vinar_3804

Sudar E, Dobutović B, Milosavljević T, Putniković B, Gluvić Z, Isenović ER. Interactive Effects of Insulin and beta-Estradiol on Protein Kinase B Phosphorylation in Adult Rat Cardiomyocytes. in Acta Chimica Slovenica. 2009;56(3):723-728.
https://hdl.handle.net/21.15107/rcub_vinar_3804 .

Sudar, Emina, Dobutović, Branislava, Milosavljević, Tijana, Putniković, Biljana, Gluvić, Zoran, Isenović, Esma R., "Interactive Effects of Insulin and beta-Estradiol on Protein Kinase B Phosphorylation in Adult Rat Cardiomyocytes" in Acta Chimica Slovenica, 56, no. 3 (2009):723-728,
https://hdl.handle.net/21.15107/rcub_vinar_3804 .