TY  - JOUR
AU  - Nedeljković, N.
AU  - Banjac, Ana
AU  - Horvat, Anica
AU  - Stojiljković, Mirjana
AU  - Nikezić, Gordana S.
PY  - 2005
UR  - https://vinar.vin.bg.ac.rs/handle/123456789/2870
AB  - In the present study the developmental! profile of ATP-hydrolyzing activity promoted by NTPDase 1, its kinetic proper-ties and the enzyme protein abundance associated with synaptic plasma membrane from rat cerebral cortex were characterized. NTPDase I activity increased from birth to day 30; afterwards it decreased and remained unchanged from adulthood (90 days) to senescence (365 days). Kinetic analysis revealed that enzyme exhibited the highest specific activity at day 30 and highest apparent affinity for ATP at day 365; however, V-max/K-m values remained unchanged for each age studied. Immunoblot analysis demonstrated that relative abundance of NTPDase 1 is highest at day 15 during ontogeny. The discrepancy between maximum enzyme activity and maximum enzyme protein abundance indicates that NTPDase 1 may have an additional role,during development. (C) 2004 ISDN. Published by Elsevier Ltd. All rights reserved.
T2  - International Journal of Developmental Neuroscience
T1  - Developmental profile of NTPDase activity in synaptic plasma membranes isolated from rat cerebral cortex
VL  - 23
IS  - 1
SP  - 45
EP  - 51
DO  - 10.1016/j.ijdevneu.2004.09.001
ER  - 

@article{
author = "Nedeljković, N. and Banjac, Ana and Horvat, Anica and Stojiljković, Mirjana and Nikezić, Gordana S.",
year = "2005",
abstract = "In the present study the developmental! profile of ATP-hydrolyzing activity promoted by NTPDase 1, its kinetic proper-ties and the enzyme protein abundance associated with synaptic plasma membrane from rat cerebral cortex were characterized. NTPDase I activity increased from birth to day 30; afterwards it decreased and remained unchanged from adulthood (90 days) to senescence (365 days). Kinetic analysis revealed that enzyme exhibited the highest specific activity at day 30 and highest apparent affinity for ATP at day 365; however, V-max/K-m values remained unchanged for each age studied. Immunoblot analysis demonstrated that relative abundance of NTPDase 1 is highest at day 15 during ontogeny. The discrepancy between maximum enzyme activity and maximum enzyme protein abundance indicates that NTPDase 1 may have an additional role,during development. (C) 2004 ISDN. Published by Elsevier Ltd. All rights reserved.",
journal = "International Journal of Developmental Neuroscience",
title = "Developmental profile of NTPDase activity in synaptic plasma membranes isolated from rat cerebral cortex",
volume = "23",
number = "1",
pages = "45-51",
doi = "10.1016/j.ijdevneu.2004.09.001"
}

Nedeljković, N., Banjac, A., Horvat, A., Stojiljković, M.,& Nikezić, G. S.. (2005). Developmental profile of NTPDase activity in synaptic plasma membranes isolated from rat cerebral cortex. in International Journal of Developmental Neuroscience, 23(1), 45-51.
https://doi.org/10.1016/j.ijdevneu.2004.09.001

Nedeljković N, Banjac A, Horvat A, Stojiljković M, Nikezić GS. Developmental profile of NTPDase activity in synaptic plasma membranes isolated from rat cerebral cortex. in International Journal of Developmental Neuroscience. 2005;23(1):45-51.
doi:10.1016/j.ijdevneu.2004.09.001 .

Nedeljković, N., Banjac, Ana, Horvat, Anica, Stojiljković, Mirjana, Nikezić, Gordana S., "Developmental profile of NTPDase activity in synaptic plasma membranes isolated from rat cerebral cortex" in International Journal of Developmental Neuroscience, 23, no. 1 (2005):45-51,
https://doi.org/10.1016/j.ijdevneu.2004.09.001 . .

TY  - JOUR
AU  - Nedeljković, N.
AU  - Banjac, Ana
AU  - Horvat, Anica
AU  - Stojilkovic, M
AU  - Nikezić, Gordana S.
PY  - 2003
UR  - https://vinar.vin.bg.ac.rs/handle/123456789/2702
AB  - Enzymes that hydrolyze extracellular ATP, i.e. ecto-ATPase and ecto-ATP diphosphohydrolase (ATPDase), can be differentiated by ability of the latter to hydrolyze ADP and by slightly different kinetic properties of the two enzymes. Synaptic plasma membrane fractions isolated from rat hippocampus and caudate nucleus exhibit ADP-hydrolyzing activity, as revealed by the enzyme assay, and the presence of ecto-ATPase protein, as revealed by immunological identification on Western blot. These findings indicate that both enzymes are co-expressed in the synaptic membrane compartment of hippocampal and caudate nucleus neurons. Kinetic analysis was performed to determine the relative contribution of each enzyme to the total ATP-hydrolyzing activity, while an inhibition study was carried out in order to exclude the interference of other nonspecific ATPase and phosphatase activities. Based on the kinetic properties, sensitivity to inhibitors and V-ATP/V-ADP ratio of about 2, we concluded that a substantial portion of ATP-hydrolyzing activity in both synaptic membrane preparations can be ascribed to the catalytic action of ATPDase. On the other hand, the highest catalytic efficacy when ATP is the substrate and the greater abundance of ecto-ATPase protein in caudate nucleus preparation suggest that the relative contribution of ecto-ATPase to the total ATP-hydrolyzing activity in the caudate nucleus is higher than in the hippocampus.
T2  - Physiological Research
T1  - Ecto-ATPase and ecto-ATP-diphosphohydrolase are co-localized in rat hippocampal and caudate nucleus synaptic plasma membranes
VL  - 52
IS  - 6
SP  - 797
EP  - 804
UR  - https://hdl.handle.net/21.15107/rcub_vinar_2702
ER  - 

@article{
author = "Nedeljković, N. and Banjac, Ana and Horvat, Anica and Stojilkovic, M and Nikezić, Gordana S.",
year = "2003",
abstract = "Enzymes that hydrolyze extracellular ATP, i.e. ecto-ATPase and ecto-ATP diphosphohydrolase (ATPDase), can be differentiated by ability of the latter to hydrolyze ADP and by slightly different kinetic properties of the two enzymes. Synaptic plasma membrane fractions isolated from rat hippocampus and caudate nucleus exhibit ADP-hydrolyzing activity, as revealed by the enzyme assay, and the presence of ecto-ATPase protein, as revealed by immunological identification on Western blot. These findings indicate that both enzymes are co-expressed in the synaptic membrane compartment of hippocampal and caudate nucleus neurons. Kinetic analysis was performed to determine the relative contribution of each enzyme to the total ATP-hydrolyzing activity, while an inhibition study was carried out in order to exclude the interference of other nonspecific ATPase and phosphatase activities. Based on the kinetic properties, sensitivity to inhibitors and V-ATP/V-ADP ratio of about 2, we concluded that a substantial portion of ATP-hydrolyzing activity in both synaptic membrane preparations can be ascribed to the catalytic action of ATPDase. On the other hand, the highest catalytic efficacy when ATP is the substrate and the greater abundance of ecto-ATPase protein in caudate nucleus preparation suggest that the relative contribution of ecto-ATPase to the total ATP-hydrolyzing activity in the caudate nucleus is higher than in the hippocampus.",
journal = "Physiological Research",
title = "Ecto-ATPase and ecto-ATP-diphosphohydrolase are co-localized in rat hippocampal and caudate nucleus synaptic plasma membranes",
volume = "52",
number = "6",
pages = "797-804",
url = "https://hdl.handle.net/21.15107/rcub_vinar_2702"
}

Nedeljković, N., Banjac, A., Horvat, A., Stojilkovic, M.,& Nikezić, G. S.. (2003). Ecto-ATPase and ecto-ATP-diphosphohydrolase are co-localized in rat hippocampal and caudate nucleus synaptic plasma membranes. in Physiological Research, 52(6), 797-804.
https://hdl.handle.net/21.15107/rcub_vinar_2702

Nedeljković N, Banjac A, Horvat A, Stojilkovic M, Nikezić GS. Ecto-ATPase and ecto-ATP-diphosphohydrolase are co-localized in rat hippocampal and caudate nucleus synaptic plasma membranes. in Physiological Research. 2003;52(6):797-804.
https://hdl.handle.net/21.15107/rcub_vinar_2702 .

Nedeljković, N., Banjac, Ana, Horvat, Anica, Stojilkovic, M, Nikezić, Gordana S., "Ecto-ATPase and ecto-ATP-diphosphohydrolase are co-localized in rat hippocampal and caudate nucleus synaptic plasma membranes" in Physiological Research, 52, no. 6 (2003):797-804,
https://hdl.handle.net/21.15107/rcub_vinar_2702 .

TY  - JOUR
AU  - Čomor, Jožef J.
AU  - Dakovic, M
AU  - Rajcevic, M
AU  - Košutić, Duško D.
AU  - Spasic, M
AU  - Vidovic, A
AU  - Duricic, J
AU  - Nedeljković, N.
PY  - 2002
UR  - https://vinar.vin.bg.ac.rs/handle/123456789/6328
AB  - According to the concept of the TESLA Accelerator Installation, the channel for production of radioisotopes has to routinely produce Tl-201, In-111, Ga-67, I-123 and F-18, and a number of other radionuclides for experimental purposes. The production of I-123 and F-18 will be performed in dedicated, commercial target stations, while a versatile solid target irradiation system is designed for the routine and experimental production of all other radioisotopes. The solid target station is designed to accept targets for both the 7degrees and 90degrees irradiation geometry. The targets used for the routine production will be prepared by electroplating on a silver substrate. They can be irradiated with a 1.5 kW beam using the 7degrees geometry. The cooling of these targets is enhanced by fins on the back of the silver substrate designed so that the highest temperature on the surface of the target does not exceed 110degreesC. The irradiation procedures will conform to the GMP requirements for the production of radio pharmaceuticals. The irradiated targets will be transported directly into the appropriate hot cell for radiochemical processing, All cells will be equipped with a target dissolution unit for etching the irradiated, electroplated film. After decontamination and sufficient cooling down, these targets will be reused several times. (C) 2001 Elsevier Science B.V. All rights reserved.
T2  - Nuclear Instruments and Methods in Physics Research. Section A: Accelerators, Spectrometers, Detectors, and Associated Equipment
T1  - Solid targetry at the TESLA Accelerator Installation
VL  - 480
IS  - 1
SP  - 7
EP  - 15
DO  - 10.1016/S0168-9002(01)02040-X
ER  - 

@article{
author = "Čomor, Jožef J. and Dakovic, M and Rajcevic, M and Košutić, Duško D. and Spasic, M and Vidovic, A and Duricic, J and Nedeljković, N.",
year = "2002",
abstract = "According to the concept of the TESLA Accelerator Installation, the channel for production of radioisotopes has to routinely produce Tl-201, In-111, Ga-67, I-123 and F-18, and a number of other radionuclides for experimental purposes. The production of I-123 and F-18 will be performed in dedicated, commercial target stations, while a versatile solid target irradiation system is designed for the routine and experimental production of all other radioisotopes. The solid target station is designed to accept targets for both the 7degrees and 90degrees irradiation geometry. The targets used for the routine production will be prepared by electroplating on a silver substrate. They can be irradiated with a 1.5 kW beam using the 7degrees geometry. The cooling of these targets is enhanced by fins on the back of the silver substrate designed so that the highest temperature on the surface of the target does not exceed 110degreesC. The irradiation procedures will conform to the GMP requirements for the production of radio pharmaceuticals. The irradiated targets will be transported directly into the appropriate hot cell for radiochemical processing, All cells will be equipped with a target dissolution unit for etching the irradiated, electroplated film. After decontamination and sufficient cooling down, these targets will be reused several times. (C) 2001 Elsevier Science B.V. All rights reserved.",
journal = "Nuclear Instruments and Methods in Physics Research. Section A: Accelerators, Spectrometers, Detectors, and Associated Equipment",
title = "Solid targetry at the TESLA Accelerator Installation",
volume = "480",
number = "1",
pages = "7-15",
doi = "10.1016/S0168-9002(01)02040-X"
}

Čomor, J. J., Dakovic, M., Rajcevic, M., Košutić, D. D., Spasic, M., Vidovic, A., Duricic, J.,& Nedeljković, N.. (2002). Solid targetry at the TESLA Accelerator Installation. in Nuclear Instruments and Methods in Physics Research. Section A: Accelerators, Spectrometers, Detectors, and Associated Equipment, 480(1), 7-15.
https://doi.org/10.1016/S0168-9002(01)02040-X

Čomor JJ, Dakovic M, Rajcevic M, Košutić DD, Spasic M, Vidovic A, Duricic J, Nedeljković N. Solid targetry at the TESLA Accelerator Installation. in Nuclear Instruments and Methods in Physics Research. Section A: Accelerators, Spectrometers, Detectors, and Associated Equipment. 2002;480(1):7-15.
doi:10.1016/S0168-9002(01)02040-X .

Čomor, Jožef J., Dakovic, M, Rajcevic, M, Košutić, Duško D., Spasic, M, Vidovic, A, Duricic, J, Nedeljković, N., "Solid targetry at the TESLA Accelerator Installation" in Nuclear Instruments and Methods in Physics Research. Section A: Accelerators, Spectrometers, Detectors, and Associated Equipment, 480, no. 1 (2002):7-15,
https://doi.org/10.1016/S0168-9002(01)02040-X . .

TY  - JOUR
AU  - Banjac, Ana
AU  - Nedeljković, N.
AU  - Horvat, Anica
AU  - Kanazir, Dušan T.
AU  - Nikezić, Gordana S.
PY  - 2001
UR  - https://vinar.vin.bg.ac.rs/handle/123456789/2455
AB  - An ontogenetic study of ecto-ATPase activity and the content of enzyme proteins was assessed in the caudate nucleus and hippocampal synaptic plasma membranes isolated from rats at various ages (15, 30, 90, 180 and 365 days). The ontogenetic profile revealed that the enzyme activities in both brain areas were the highest on day 30 and 365, while the ecto-ATPase protein abundance was the highest on day 15 after birth. Possible explanation for obtained ontogenetic profile and the discrepancy between activity and abundance may reside in the fact that ecto-ATPase during development could exert additional roles other than those related to metabolism of ATP. It is likely that ecto-ATPase, regulating the concentration of ATP and adenosine in synaptic cleft, has important role in the processes of brain development and aging.
T2  - Physiological Research
T1  - Ontogenetic profile of ecto-ATPase activity in rat hippocampal and caudate nucleus synaptic plasma membrane fractions
VL  - 50
IS  - 4
SP  - 411
EP  - 417
UR  - https://hdl.handle.net/21.15107/rcub_vinar_2455
ER  - 

@article{
author = "Banjac, Ana and Nedeljković, N. and Horvat, Anica and Kanazir, Dušan T. and Nikezić, Gordana S.",
year = "2001",
abstract = "An ontogenetic study of ecto-ATPase activity and the content of enzyme proteins was assessed in the caudate nucleus and hippocampal synaptic plasma membranes isolated from rats at various ages (15, 30, 90, 180 and 365 days). The ontogenetic profile revealed that the enzyme activities in both brain areas were the highest on day 30 and 365, while the ecto-ATPase protein abundance was the highest on day 15 after birth. Possible explanation for obtained ontogenetic profile and the discrepancy between activity and abundance may reside in the fact that ecto-ATPase during development could exert additional roles other than those related to metabolism of ATP. It is likely that ecto-ATPase, regulating the concentration of ATP and adenosine in synaptic cleft, has important role in the processes of brain development and aging.",
journal = "Physiological Research",
title = "Ontogenetic profile of ecto-ATPase activity in rat hippocampal and caudate nucleus synaptic plasma membrane fractions",
volume = "50",
number = "4",
pages = "411-417",
url = "https://hdl.handle.net/21.15107/rcub_vinar_2455"
}

Banjac, A., Nedeljković, N., Horvat, A., Kanazir, D. T.,& Nikezić, G. S.. (2001). Ontogenetic profile of ecto-ATPase activity in rat hippocampal and caudate nucleus synaptic plasma membrane fractions. in Physiological Research, 50(4), 411-417.
https://hdl.handle.net/21.15107/rcub_vinar_2455

Banjac A, Nedeljković N, Horvat A, Kanazir DT, Nikezić GS. Ontogenetic profile of ecto-ATPase activity in rat hippocampal and caudate nucleus synaptic plasma membrane fractions. in Physiological Research. 2001;50(4):411-417.
https://hdl.handle.net/21.15107/rcub_vinar_2455 .

Banjac, Ana, Nedeljković, N., Horvat, Anica, Kanazir, Dušan T., Nikezić, Gordana S., "Ontogenetic profile of ecto-ATPase activity in rat hippocampal and caudate nucleus synaptic plasma membrane fractions" in Physiological Research, 50, no. 4 (2001):411-417,
https://hdl.handle.net/21.15107/rcub_vinar_2455 .

TY  - JOUR
AU  - Horvat, Anica
AU  - Petrović, S
AU  - Nedeljković, N.
AU  - Martinović, Jelena
AU  - Nikezić, Gordana S.
PY  - 2000
UR  - https://vinar.vin.bg.ac.rs/handle/123456789/2353
AB  - The effects of gonadal steroid hormone, 17 beta-estradiol (E-2), in vitro on rat brain mitochondria Ca2+ movement were investigated. Intrasynaptosomal mitochondria Ca2+ uptake via an energy-driven Ca2+ uniporter have K-m = 112.73 +/- 7.3 mu mol.l(-1) and V-max = 21.97 +/- 1.7 nmol Ca-45(2+) mg(-1). Ca2+ release trough a Na+/Ca2+ antiporter was measured with a K-m for Na+ of 43.7 +/- 2.6 mmol.l(-1), and V-max of 1.5 +/- 0.3 nmol Ca-45(2+) mg(-1). Addition of estradiol in preincubation mixture did not affect the uptake of Ca2+ mediated by the ruthenium red-sensitive uniporter, while it produced biphasic effect on Na-dependent Ca2+ efflux. Estradiol at concentrations up to 1 nmol.l(-1) decreased the efflux significantly (63% inhibition with respect to the control), and at concentrations above 10 nmol.l(-1) increased it exponentially. The maximum inhibiting concentration of estradiol (0.5 nmol.l(-1)) increased the affinity of the uniporter (K-m reduced by about 30%), without affecting significantly the capacity (V-max) for Na+. The results presented suggest that estradiol inhibits Na-dependent Ca2+ efflux from mitochondria and acts on mitochondrial retention of Ca2+, which may modulate mitochondrial and consequently synaptosomal content of Ca2+, and in this way exerts its role in the homeostasis of calcium in nerve terminals.
T2  - General Physiology and Biophysics
T1  - Estradiol affect Na-dependent Ca2+ efflux from synaptosomal mitochondria
VL  - 19
IS  - 1
SP  - 59
EP  - 71
UR  - https://hdl.handle.net/21.15107/rcub_vinar_2353
ER  - 

@article{
author = "Horvat, Anica and Petrović, S and Nedeljković, N. and Martinović, Jelena and Nikezić, Gordana S.",
year = "2000",
abstract = "The effects of gonadal steroid hormone, 17 beta-estradiol (E-2), in vitro on rat brain mitochondria Ca2+ movement were investigated. Intrasynaptosomal mitochondria Ca2+ uptake via an energy-driven Ca2+ uniporter have K-m = 112.73 +/- 7.3 mu mol.l(-1) and V-max = 21.97 +/- 1.7 nmol Ca-45(2+) mg(-1). Ca2+ release trough a Na+/Ca2+ antiporter was measured with a K-m for Na+ of 43.7 +/- 2.6 mmol.l(-1), and V-max of 1.5 +/- 0.3 nmol Ca-45(2+) mg(-1). Addition of estradiol in preincubation mixture did not affect the uptake of Ca2+ mediated by the ruthenium red-sensitive uniporter, while it produced biphasic effect on Na-dependent Ca2+ efflux. Estradiol at concentrations up to 1 nmol.l(-1) decreased the efflux significantly (63% inhibition with respect to the control), and at concentrations above 10 nmol.l(-1) increased it exponentially. The maximum inhibiting concentration of estradiol (0.5 nmol.l(-1)) increased the affinity of the uniporter (K-m reduced by about 30%), without affecting significantly the capacity (V-max) for Na+. The results presented suggest that estradiol inhibits Na-dependent Ca2+ efflux from mitochondria and acts on mitochondrial retention of Ca2+, which may modulate mitochondrial and consequently synaptosomal content of Ca2+, and in this way exerts its role in the homeostasis of calcium in nerve terminals.",
journal = "General Physiology and Biophysics",
title = "Estradiol affect Na-dependent Ca2+ efflux from synaptosomal mitochondria",
volume = "19",
number = "1",
pages = "59-71",
url = "https://hdl.handle.net/21.15107/rcub_vinar_2353"
}

Horvat, A., Petrović, S., Nedeljković, N., Martinović, J.,& Nikezić, G. S.. (2000). Estradiol affect Na-dependent Ca2+ efflux from synaptosomal mitochondria. in General Physiology and Biophysics, 19(1), 59-71.
https://hdl.handle.net/21.15107/rcub_vinar_2353

Horvat A, Petrović S, Nedeljković N, Martinović J, Nikezić GS. Estradiol affect Na-dependent Ca2+ efflux from synaptosomal mitochondria. in General Physiology and Biophysics. 2000;19(1):59-71.
https://hdl.handle.net/21.15107/rcub_vinar_2353 .

Horvat, Anica, Petrović, S, Nedeljković, N., Martinović, Jelena, Nikezić, Gordana S., "Estradiol affect Na-dependent Ca2+ efflux from synaptosomal mitochondria" in General Physiology and Biophysics, 19, no. 1 (2000):59-71,
https://hdl.handle.net/21.15107/rcub_vinar_2353 .

TY  - JOUR
AU  - Nedeljković, N.
AU  - Đorđević, V.
AU  - Horvat, Anica
AU  - Nikezić, Gordana S.
AU  - Kanazir, Dušan T.
PY  - 2000
UR  - https://vinar.vin.bg.ac.rs/handle/123456789/2376
AB  - Abundant evidence indicates that ATP and adenosine act as neurotransmitters or co-transmitters, influencing nerve cell physiology in various ways. Therefore, regulation of ATP-metabolizing enzymes is essential for the normal development and function of neuronal tissue. In the present study we have examined the effect of gonadal (OVX) or adrenal (ADX) steroid hormone deprivation on the activity and expression of synaptic membrane ecto-ATPase in three extrahypothalamic brain areas of female rats, primarily not associated with reproductive function. It was shown that OVX significantly increased ecto-ATPase activity and the relative abundance of this enzyme in the hippocampal (Hip) and caudate nucleus (CN), but not in brain stem (BS) membrane preparations. ADX was followed by an upregulation of the enzyme activity and its relative abundance in all the brain areas investigated. The highest enzyme activity and the most profound effects of OVX and ADX were detected in the CN. The results obtained indicate that ADX and OVX upregulate the expression of ecto-ATPase, potentiating the production of adenosine in synaptic cleft thus modulating the activity of numerous neurotransmitter systems in distinct areas of the CNS.
T2  - Physiological Research
T1  - Effect of steroid hormone deprivation on the expression of ecto-ATPase in distinct brain regions of female rats
VL  - 49
IS  - 4
SP  - 419
EP  - 426
UR  - https://hdl.handle.net/21.15107/rcub_vinar_2376
ER  - 

@article{
author = "Nedeljković, N. and Đorđević, V. and Horvat, Anica and Nikezić, Gordana S. and Kanazir, Dušan T.",
year = "2000",
abstract = "Abundant evidence indicates that ATP and adenosine act as neurotransmitters or co-transmitters, influencing nerve cell physiology in various ways. Therefore, regulation of ATP-metabolizing enzymes is essential for the normal development and function of neuronal tissue. In the present study we have examined the effect of gonadal (OVX) or adrenal (ADX) steroid hormone deprivation on the activity and expression of synaptic membrane ecto-ATPase in three extrahypothalamic brain areas of female rats, primarily not associated with reproductive function. It was shown that OVX significantly increased ecto-ATPase activity and the relative abundance of this enzyme in the hippocampal (Hip) and caudate nucleus (CN), but not in brain stem (BS) membrane preparations. ADX was followed by an upregulation of the enzyme activity and its relative abundance in all the brain areas investigated. The highest enzyme activity and the most profound effects of OVX and ADX were detected in the CN. The results obtained indicate that ADX and OVX upregulate the expression of ecto-ATPase, potentiating the production of adenosine in synaptic cleft thus modulating the activity of numerous neurotransmitter systems in distinct areas of the CNS.",
journal = "Physiological Research",
title = "Effect of steroid hormone deprivation on the expression of ecto-ATPase in distinct brain regions of female rats",
volume = "49",
number = "4",
pages = "419-426",
url = "https://hdl.handle.net/21.15107/rcub_vinar_2376"
}

Nedeljković, N., Đorđević, V., Horvat, A., Nikezić, G. S.,& Kanazir, D. T.. (2000). Effect of steroid hormone deprivation on the expression of ecto-ATPase in distinct brain regions of female rats. in Physiological Research, 49(4), 419-426.
https://hdl.handle.net/21.15107/rcub_vinar_2376

Nedeljković N, Đorđević V, Horvat A, Nikezić GS, Kanazir DT. Effect of steroid hormone deprivation on the expression of ecto-ATPase in distinct brain regions of female rats. in Physiological Research. 2000;49(4):419-426.
https://hdl.handle.net/21.15107/rcub_vinar_2376 .

Nedeljković, N., Đorđević, V., Horvat, Anica, Nikezić, Gordana S., Kanazir, Dušan T., "Effect of steroid hormone deprivation on the expression of ecto-ATPase in distinct brain regions of female rats" in Physiological Research, 49, no. 4 (2000):419-426,
https://hdl.handle.net/21.15107/rcub_vinar_2376 .

TY  - JOUR
AU  - Vasić, Vesna M.
AU  - Jovanovic, D
AU  - Krstić, Danijela Z.
AU  - Nikezić, Gordana S.
AU  - Horvat, Anica
AU  - Vujisić Lj.
AU  - Nedeljković, N.
PY  - 1999
UR  - https://vinar.vin.bg.ac.rs/handle/123456789/2293
AB  - Enzymatic activities of Na+/K+-ATPase and Mg2+-ATPase from rat brain synaptic plasma membrane were studied in the absence and presence of EDTA. The aim of the study was to examine the ability of this strong chelator to prevent and recover the CuSO4-induced inhibition. The influence of experimentally added CuSO4 and EDTA on MgATP(2-) complex and free Cu2+ concentrations in the reaction mixture was calculated and discussed. CuSO4 induced dose-dependent inhibition of both enzymes in the absence and presence of 1 mM EDTA. In the absence of EDTA, the IC50 values of Cu2+, as calculated from the experimental curves, were 5.9 x 10(-7) M for Na+/K+- ATPase and 3.6 x 10(-6) M for Mg2+-ATPase. One millimolar EDTA prevented the enzyme inhibition induced by CuSO4, but also reversed the inhibited activity, in a concentration-dependent manner, following exposure of the enzymes to the metal ion, by lowering free Cu2+ concentration. Kinetic analysis showed that CuSO4, inhibits both the Na+/K+-ATPase and Mg2+-ATPase, by reducing their maximum enzymatic velocities (V-max), rather than apparent affinity for substrate MgATP(2-) (K-0.5), implying the noncompetitive nature of enzyme inhibition induced by the metal. The kinetic analysis also confirmed two distinct Mg2+-ATPase subtypes activated in the presence of low and high MgATP(2-) concentrations. K-0.5 and V-max were calculated using a computer-based program. The results of calculation showed that MgATP(2-) concentration in the kinetic experiments exceeded three times the apparent K-0.5 value for the enzyme activation. (C) 1999 Elsevier Science Ireland Ltd. All rights reserved.
T2  - Toxicology Letters
T1  - Prevention and recovery of CuSO4-induced inhibition of Na+/K+-ATPase and Mg2+-ATPase in rat brain synaptosomes by EDTA
VL  - 110
IS  - 1-2
SP  - 95
EP  - 104
DO  - 10.1016/S0378-4274(99)00144-7
ER  - 

@article{
author = "Vasić, Vesna M. and Jovanovic, D and Krstić, Danijela Z. and Nikezić, Gordana S. and Horvat, Anica and Vujisić Lj. and Nedeljković, N.",
year = "1999",
abstract = "Enzymatic activities of Na+/K+-ATPase and Mg2+-ATPase from rat brain synaptic plasma membrane were studied in the absence and presence of EDTA. The aim of the study was to examine the ability of this strong chelator to prevent and recover the CuSO4-induced inhibition. The influence of experimentally added CuSO4 and EDTA on MgATP(2-) complex and free Cu2+ concentrations in the reaction mixture was calculated and discussed. CuSO4 induced dose-dependent inhibition of both enzymes in the absence and presence of 1 mM EDTA. In the absence of EDTA, the IC50 values of Cu2+, as calculated from the experimental curves, were 5.9 x 10(-7) M for Na+/K+- ATPase and 3.6 x 10(-6) M for Mg2+-ATPase. One millimolar EDTA prevented the enzyme inhibition induced by CuSO4, but also reversed the inhibited activity, in a concentration-dependent manner, following exposure of the enzymes to the metal ion, by lowering free Cu2+ concentration. Kinetic analysis showed that CuSO4, inhibits both the Na+/K+-ATPase and Mg2+-ATPase, by reducing their maximum enzymatic velocities (V-max), rather than apparent affinity for substrate MgATP(2-) (K-0.5), implying the noncompetitive nature of enzyme inhibition induced by the metal. The kinetic analysis also confirmed two distinct Mg2+-ATPase subtypes activated in the presence of low and high MgATP(2-) concentrations. K-0.5 and V-max were calculated using a computer-based program. The results of calculation showed that MgATP(2-) concentration in the kinetic experiments exceeded three times the apparent K-0.5 value for the enzyme activation. (C) 1999 Elsevier Science Ireland Ltd. All rights reserved.",
journal = "Toxicology Letters",
title = "Prevention and recovery of CuSO4-induced inhibition of Na+/K+-ATPase and Mg2+-ATPase in rat brain synaptosomes by EDTA",
volume = "110",
number = "1-2",
pages = "95-104",
doi = "10.1016/S0378-4274(99)00144-7"
}

Vasić, V. M., Jovanovic, D., Krstić, D. Z., Nikezić, G. S., Horvat, A., Vujisić Lj.,& Nedeljković, N.. (1999). Prevention and recovery of CuSO4-induced inhibition of Na+/K+-ATPase and Mg2+-ATPase in rat brain synaptosomes by EDTA. in Toxicology Letters, 110(1-2), 95-104.
https://doi.org/10.1016/S0378-4274(99)00144-7

Vasić VM, Jovanovic D, Krstić DZ, Nikezić GS, Horvat A, Vujisić Lj., Nedeljković N. Prevention and recovery of CuSO4-induced inhibition of Na+/K+-ATPase and Mg2+-ATPase in rat brain synaptosomes by EDTA. in Toxicology Letters. 1999;110(1-2):95-104.
doi:10.1016/S0378-4274(99)00144-7 .

Vasić, Vesna M., Jovanovic, D, Krstić, Danijela Z., Nikezić, Gordana S., Horvat, Anica, Vujisić Lj., Nedeljković, N., "Prevention and recovery of CuSO4-induced inhibition of Na+/K+-ATPase and Mg2+-ATPase in rat brain synaptosomes by EDTA" in Toxicology Letters, 110, no. 1-2 (1999):95-104,
https://doi.org/10.1016/S0378-4274(99)00144-7 . .

TY  - JOUR
AU  - Nikezić, Gordana S.
AU  - Horvat, Anica
AU  - Nedeljković, N.
AU  - Todorović, S.
AU  - Nikolić, Vladimir M.
AU  - Kanazir, Dušan T.
AU  - Vujisić Lj.
AU  - Kopečni Miroslav
PY  - 1998
UR  - https://vinar.vin.bg.ac.rs/handle/123456789/2146
AB  - The neurotoxicity of pyridine and urea was investigated in respect to their ability to alter the activity of synaptosomal membrane Na+/K+-ATPase and Mg2+-ATPase. In vitro treatment with pyridine and urea stimulated Na+/K+-ATPase activity in a dose-dependent manner up to 40% and 60%, respectively. Mg2+-ATPase activity increased up to 40% after pyridine treatment, while urea had no effect at all. The neuroactive potencies of pyridine and urea were evaluated by estimating parameters K-m and Delta V-max for enzyme stimulation, as well as Hill coefficient to estimate the levels of cooperativity for pyridine and urea binding. The results suggest that pyridine stimulates both enzymes, probably by interacting with some neuronal membrane components, and altering the lipid micro-environment of the ATPases. In contrast, urea stimulates the Na+/K+-ATPase only, assumingly by acting on it directly or via some other regulatory mechanism. Stimulation of Na+/K+-ATPase and Mg2+-ATPase by the substances tested and subsequent alteration of neuronal cell functioning could contribute to the CNS dysfunction upon chronic exposure to pyridine and urea.
T2  - General Physiology and Biophysics
T1  - Influence of pyridine and urea on the rat brain ATPase activity
VL  - 17
IS  - 1
SP  - 15
EP  - 23
UR  - https://hdl.handle.net/21.15107/rcub_vinar_2146
ER  - 

@article{
author = "Nikezić, Gordana S. and Horvat, Anica and Nedeljković, N. and Todorović, S. and Nikolić, Vladimir M. and Kanazir, Dušan T. and Vujisić Lj. and Kopečni Miroslav",
year = "1998",
abstract = "The neurotoxicity of pyridine and urea was investigated in respect to their ability to alter the activity of synaptosomal membrane Na+/K+-ATPase and Mg2+-ATPase. In vitro treatment with pyridine and urea stimulated Na+/K+-ATPase activity in a dose-dependent manner up to 40% and 60%, respectively. Mg2+-ATPase activity increased up to 40% after pyridine treatment, while urea had no effect at all. The neuroactive potencies of pyridine and urea were evaluated by estimating parameters K-m and Delta V-max for enzyme stimulation, as well as Hill coefficient to estimate the levels of cooperativity for pyridine and urea binding. The results suggest that pyridine stimulates both enzymes, probably by interacting with some neuronal membrane components, and altering the lipid micro-environment of the ATPases. In contrast, urea stimulates the Na+/K+-ATPase only, assumingly by acting on it directly or via some other regulatory mechanism. Stimulation of Na+/K+-ATPase and Mg2+-ATPase by the substances tested and subsequent alteration of neuronal cell functioning could contribute to the CNS dysfunction upon chronic exposure to pyridine and urea.",
journal = "General Physiology and Biophysics",
title = "Influence of pyridine and urea on the rat brain ATPase activity",
volume = "17",
number = "1",
pages = "15-23",
url = "https://hdl.handle.net/21.15107/rcub_vinar_2146"
}

Nikezić, G. S., Horvat, A., Nedeljković, N., Todorović, S., Nikolić, V. M., Kanazir, D. T., Vujisić Lj.,& Kopečni Miroslav. (1998). Influence of pyridine and urea on the rat brain ATPase activity. in General Physiology and Biophysics, 17(1), 15-23.
https://hdl.handle.net/21.15107/rcub_vinar_2146

Nikezić GS, Horvat A, Nedeljković N, Todorović S, Nikolić VM, Kanazir DT, Vujisić Lj., Kopečni Miroslav. Influence of pyridine and urea on the rat brain ATPase activity. in General Physiology and Biophysics. 1998;17(1):15-23.
https://hdl.handle.net/21.15107/rcub_vinar_2146 .

Nikezić, Gordana S., Horvat, Anica, Nedeljković, N., Todorović, S., Nikolić, Vladimir M., Kanazir, Dušan T., Vujisić Lj., Kopečni Miroslav, "Influence of pyridine and urea on the rat brain ATPase activity" in General Physiology and Biophysics, 17, no. 1 (1998):15-23,
https://hdl.handle.net/21.15107/rcub_vinar_2146 .

TY  - JOUR
AU  - Nedeljković, N.
AU  - Nikezić, Gordana S.
AU  - Horvat, Anica
AU  - Peković, Sanja
AU  - Stojiljković, Mirjana
AU  - Martinović, Jelena
PY  - 1998
UR  - https://vinar.vin.bg.ac.rs/handle/123456789/2145
AB  - In the present study distribution and enzymatic properties of ecto-Mg2+-ATPase were determined in synaptic plasma membrane (SPM) preparations isolated from the hippocampus, caudate nucleus and whole brains of female rats. Western blot analysis using anti-ecto-Mg2+-ATPase antibody revealed the association of Mg2+-ATPase with SPM prepared from all the three brain sources, yet the enzyme was most abundant in caudate nucleus membranes, being 30% and 22% more abundant than in the hippocampal and whole brain tissue SPM, respectively. The evidence is also presented that kinetic properties of the brain Mg2+-ATPase are not under the control of circulating sex steroids. It was confirmed that the enzyme is activated by millimolar concentrations of Mg2+ and that it cannot be effectively inhibited by known ATPase inhibitors. The most pronounced differences in kinetic properties observed were 2.5 fold higher apparent affinity for ATP and 59% higher specific activity of Mg2+-ATPase of the caudate nucleus as compared with the enzyme from the hippocampus. On the other hand, the apparent enzyme affinity for Mg2+ was almost equal in all SPM preparations tested. Taken together, our results show that ecto-Mg2+-ATPase is not uniformly distributed and differs in respect to affinity for ATP in rat brain regions, thus indicating its substantial role in the process of signal transduction via controlling the levels of extracellular ATP.
T2  - General Physiology and Biophysics
T1  - Properties of Mg2+-ATPase in rat brain synaptic plasma membranes
VL  - 17
IS  - 1
SP  - 3
EP  - 13
UR  - https://hdl.handle.net/21.15107/rcub_vinar_2145
ER  - 

@article{
author = "Nedeljković, N. and Nikezić, Gordana S. and Horvat, Anica and Peković, Sanja and Stojiljković, Mirjana and Martinović, Jelena",
year = "1998",
abstract = "In the present study distribution and enzymatic properties of ecto-Mg2+-ATPase were determined in synaptic plasma membrane (SPM) preparations isolated from the hippocampus, caudate nucleus and whole brains of female rats. Western blot analysis using anti-ecto-Mg2+-ATPase antibody revealed the association of Mg2+-ATPase with SPM prepared from all the three brain sources, yet the enzyme was most abundant in caudate nucleus membranes, being 30% and 22% more abundant than in the hippocampal and whole brain tissue SPM, respectively. The evidence is also presented that kinetic properties of the brain Mg2+-ATPase are not under the control of circulating sex steroids. It was confirmed that the enzyme is activated by millimolar concentrations of Mg2+ and that it cannot be effectively inhibited by known ATPase inhibitors. The most pronounced differences in kinetic properties observed were 2.5 fold higher apparent affinity for ATP and 59% higher specific activity of Mg2+-ATPase of the caudate nucleus as compared with the enzyme from the hippocampus. On the other hand, the apparent enzyme affinity for Mg2+ was almost equal in all SPM preparations tested. Taken together, our results show that ecto-Mg2+-ATPase is not uniformly distributed and differs in respect to affinity for ATP in rat brain regions, thus indicating its substantial role in the process of signal transduction via controlling the levels of extracellular ATP.",
journal = "General Physiology and Biophysics",
title = "Properties of Mg2+-ATPase in rat brain synaptic plasma membranes",
volume = "17",
number = "1",
pages = "3-13",
url = "https://hdl.handle.net/21.15107/rcub_vinar_2145"
}

Nedeljković, N., Nikezić, G. S., Horvat, A., Peković, S., Stojiljković, M.,& Martinović, J.. (1998). Properties of Mg2+-ATPase in rat brain synaptic plasma membranes. in General Physiology and Biophysics, 17(1), 3-13.
https://hdl.handle.net/21.15107/rcub_vinar_2145

Nedeljković N, Nikezić GS, Horvat A, Peković S, Stojiljković M, Martinović J. Properties of Mg2+-ATPase in rat brain synaptic plasma membranes. in General Physiology and Biophysics. 1998;17(1):3-13.
https://hdl.handle.net/21.15107/rcub_vinar_2145 .

Nedeljković, N., Nikezić, Gordana S., Horvat, Anica, Peković, Sanja, Stojiljković, Mirjana, Martinović, Jelena, "Properties of Mg2+-ATPase in rat brain synaptic plasma membranes" in General Physiology and Biophysics, 17, no. 1 (1998):3-13,
https://hdl.handle.net/21.15107/rcub_vinar_2145 .

TY  - JOUR
AU  - Peković, Sanja
AU  - Nedeljković, N.
AU  - Nikezić, Gordana S.
AU  - Horvat, Anica
AU  - Stojiljković, Mirjana
AU  - Rakić, Ljubisav
AU  - Martinović, Jelena
PY  - 1997
UR  - https://vinar.vin.bg.ac.rs/handle/123456789/2098
AB  - The activities and basic enzymatic properties of Na,K-ATPase were examined in synaptosomal plasma membranes (SPM) prepared from rat hippocampus and striatum. A kinetic analysis showed profound differences in apparent affinities for ATP (K-m) between hippocampal (1.21 mmol/l) and striatal (0.76 mmol/l) enzyme preparations, as well as in the corresponding V-max values. However, physiological efficiencies were almost the same. The complex pattern of dose-response curves to ouabain indicated the presence of two high-affinity forms of Na,K-ATPase in the striatum (very high-:K-i = 3.73 x 10(-8) mol/l and high-:K-i = 4.21 x 10(-5) mol/l), and one high affinity form in the hippocampus (K-i = 6.6 x 10(-7) mol/l). In addition, both SPM preparations contained one low affinity form with similar K-i. The very high-affinity form had positive cooperativity for ouabain inhibition of Na,K-ATPase activity, in contrast to high- and low-affinity forms, which exhibited negative cooperativity. The respective contributions of ouabain-sensitive forms to the total activity were estimated as 22%, 46%, 19% for the striatum and 36%, 45% for the hippocampus. These data clearly demonstrate striking differences in kinetic properties of the hippocampal and striatal Na,K-ATPase that may be due to the isoenzyme diversity and adaptation to specific physiological demands of the examined rat brain regions.
T2  - General Physiology and Biophysics
T1  - Biochemical characterization of the hippocampal and striatal Na,K-ATPase reveals striking differences in kinetic properties
VL  - 16
IS  - 3
SP  - 227
EP  - 240
UR  - https://hdl.handle.net/21.15107/rcub_vinar_2098
ER  - 

@article{
author = "Peković, Sanja and Nedeljković, N. and Nikezić, Gordana S. and Horvat, Anica and Stojiljković, Mirjana and Rakić, Ljubisav and Martinović, Jelena",
year = "1997",
abstract = "The activities and basic enzymatic properties of Na,K-ATPase were examined in synaptosomal plasma membranes (SPM) prepared from rat hippocampus and striatum. A kinetic analysis showed profound differences in apparent affinities for ATP (K-m) between hippocampal (1.21 mmol/l) and striatal (0.76 mmol/l) enzyme preparations, as well as in the corresponding V-max values. However, physiological efficiencies were almost the same. The complex pattern of dose-response curves to ouabain indicated the presence of two high-affinity forms of Na,K-ATPase in the striatum (very high-:K-i = 3.73 x 10(-8) mol/l and high-:K-i = 4.21 x 10(-5) mol/l), and one high affinity form in the hippocampus (K-i = 6.6 x 10(-7) mol/l). In addition, both SPM preparations contained one low affinity form with similar K-i. The very high-affinity form had positive cooperativity for ouabain inhibition of Na,K-ATPase activity, in contrast to high- and low-affinity forms, which exhibited negative cooperativity. The respective contributions of ouabain-sensitive forms to the total activity were estimated as 22%, 46%, 19% for the striatum and 36%, 45% for the hippocampus. These data clearly demonstrate striking differences in kinetic properties of the hippocampal and striatal Na,K-ATPase that may be due to the isoenzyme diversity and adaptation to specific physiological demands of the examined rat brain regions.",
journal = "General Physiology and Biophysics",
title = "Biochemical characterization of the hippocampal and striatal Na,K-ATPase reveals striking differences in kinetic properties",
volume = "16",
number = "3",
pages = "227-240",
url = "https://hdl.handle.net/21.15107/rcub_vinar_2098"
}

Peković, S., Nedeljković, N., Nikezić, G. S., Horvat, A., Stojiljković, M., Rakić, L.,& Martinović, J.. (1997). Biochemical characterization of the hippocampal and striatal Na,K-ATPase reveals striking differences in kinetic properties. in General Physiology and Biophysics, 16(3), 227-240.
https://hdl.handle.net/21.15107/rcub_vinar_2098

Peković S, Nedeljković N, Nikezić GS, Horvat A, Stojiljković M, Rakić L, Martinović J. Biochemical characterization of the hippocampal and striatal Na,K-ATPase reveals striking differences in kinetic properties. in General Physiology and Biophysics. 1997;16(3):227-240.
https://hdl.handle.net/21.15107/rcub_vinar_2098 .

Peković, Sanja, Nedeljković, N., Nikezić, Gordana S., Horvat, Anica, Stojiljković, Mirjana, Rakić, Ljubisav, Martinović, Jelena, "Biochemical characterization of the hippocampal and striatal Na,K-ATPase reveals striking differences in kinetic properties" in General Physiology and Biophysics, 16, no. 3 (1997):227-240,
https://hdl.handle.net/21.15107/rcub_vinar_2098 .

TY  - JOUR
AU  - Nikezić, Gordana S.
AU  - Nedeljković, N.
AU  - Horvat, Anica
AU  - Kanazir, Dušan T.
AU  - Martinović, Jelena
PY  - 1997
UR  - https://vinar.vin.bg.ac.rs/handle/123456789/2108
AB  - Membrane vesicles loaded with [Na+], prepared from synaptosomal plasma membranes (SPM) of whole brains (WE), hippocampi (Hip) and caudate nuclei (NC) of female rats, were used to study Na+-dependent Ca2+ transport across SPM vesicles under the influence of 17 beta-estradiol (E-2) in vitro. In concentrations near to physiologic, E-2 significantly increased Ca-45(2+) uptake by SPM vesicles from all the brain tissues investigated. The maximum increase was observed for WE (21%) and Hip (33%) at 10(-9) mol/l, and for NC (31%) at 5 x 10(-9) mol/l of E-2. These results (a) confirm our earlier finding that E, in vitro modulates Na+-dependent Ca2+ transport across synaptosomal membrane in rat brain regions, and (b) suggest Na+/Ca2+ exchange as principal mechanism of the E-2-stimulated Na+-dependent Ca2+ uptake by membrane vesicles. The involvement of any ATPases as possible mediators is discussed. (C) 1997, Editrice Kurtis.
T2  - Journal of Endocrinological Investigation
T1  - Estradiol in vitro modulates Na+-dependent Ca2+ uptake by synaptic plasma membrane vesicles of rat brain regions
VL  - 20
IS  - 11
SP  - 664
EP  - 668
DO  - 10.1007/BF03348028
ER  - 

@article{
author = "Nikezić, Gordana S. and Nedeljković, N. and Horvat, Anica and Kanazir, Dušan T. and Martinović, Jelena",
year = "1997",
abstract = "Membrane vesicles loaded with [Na+], prepared from synaptosomal plasma membranes (SPM) of whole brains (WE), hippocampi (Hip) and caudate nuclei (NC) of female rats, were used to study Na+-dependent Ca2+ transport across SPM vesicles under the influence of 17 beta-estradiol (E-2) in vitro. In concentrations near to physiologic, E-2 significantly increased Ca-45(2+) uptake by SPM vesicles from all the brain tissues investigated. The maximum increase was observed for WE (21%) and Hip (33%) at 10(-9) mol/l, and for NC (31%) at 5 x 10(-9) mol/l of E-2. These results (a) confirm our earlier finding that E, in vitro modulates Na+-dependent Ca2+ transport across synaptosomal membrane in rat brain regions, and (b) suggest Na+/Ca2+ exchange as principal mechanism of the E-2-stimulated Na+-dependent Ca2+ uptake by membrane vesicles. The involvement of any ATPases as possible mediators is discussed. (C) 1997, Editrice Kurtis.",
journal = "Journal of Endocrinological Investigation",
title = "Estradiol in vitro modulates Na+-dependent Ca2+ uptake by synaptic plasma membrane vesicles of rat brain regions",
volume = "20",
number = "11",
pages = "664-668",
doi = "10.1007/BF03348028"
}

Nikezić, G. S., Nedeljković, N., Horvat, A., Kanazir, D. T.,& Martinović, J.. (1997). Estradiol in vitro modulates Na+-dependent Ca2+ uptake by synaptic plasma membrane vesicles of rat brain regions. in Journal of Endocrinological Investigation, 20(11), 664-668.
https://doi.org/10.1007/BF03348028

Nikezić GS, Nedeljković N, Horvat A, Kanazir DT, Martinović J. Estradiol in vitro modulates Na+-dependent Ca2+ uptake by synaptic plasma membrane vesicles of rat brain regions. in Journal of Endocrinological Investigation. 1997;20(11):664-668.
doi:10.1007/BF03348028 .

Nikezić, Gordana S., Nedeljković, N., Horvat, Anica, Kanazir, Dušan T., Martinović, Jelena, "Estradiol in vitro modulates Na+-dependent Ca2+ uptake by synaptic plasma membrane vesicles of rat brain regions" in Journal of Endocrinological Investigation, 20, no. 11 (1997):664-668,
https://doi.org/10.1007/BF03348028 . .

TY  - JOUR
AU  - Nikezić, Gordana S.
AU  - Horvat, Anica
AU  - Nedeljković, N.
AU  - Martinović, Jelena
PY  - 1996
UR  - https://vinar.vin.bg.ac.rs/handle/123456789/1968
AB  - Effects of 17 beta-estradiol (E(2)) in vitro on Na-dependent Ca2+ efflux from, and depolarization-induced Ca2+ uptake into, the nerve cell were studied with the use of synaptosomes isolated from the brain stem, mesencephalic reticular formation (MRF), caudate nucleus and the hippocampus of long-term ovariectomized adult female rats. It was found that E(2) (1) at a concentration of 10 nM or lower, stimulates Na-dependent Ca2+ efflux in the caudate nucleus and hippocampus, and does not affect the efflux in MRF and brain stem; (2) at concentrations above 10 nM has no effect on the Ca2+ efflux in any of the four structures investigated; and (3) produces a biphasic effect on the depolarization-induced Ca2+ uptake, increasing it in all structures except MRF at 10 nM concentration, and decreasing it at concentrations higher than 10 nM, irrespective of the structure investigated. These results suggest that E(2), acting at extranuclear sites, modulates synaptic transmission via alterations of Ca2+ transport mechanisms in nerve endings.
T2  - Experientia
T1  - 17 beta-Estradiol in vitro affects Na-dependent and depolarization-induced Ca2+ transport in rat brain synaptosomes
VL  - 52
IS  - 3
SP  - 217
EP  - 220
DO  - 10.1007/BF01920709
UR  - https://hdl.handle.net/21.15107/rcub_vinar_1968
ER  - 

@article{
author = "Nikezić, Gordana S. and Horvat, Anica and Nedeljković, N. and Martinović, Jelena",
year = "1996",
abstract = "Effects of 17 beta-estradiol (E(2)) in vitro on Na-dependent Ca2+ efflux from, and depolarization-induced Ca2+ uptake into, the nerve cell were studied with the use of synaptosomes isolated from the brain stem, mesencephalic reticular formation (MRF), caudate nucleus and the hippocampus of long-term ovariectomized adult female rats. It was found that E(2) (1) at a concentration of 10 nM or lower, stimulates Na-dependent Ca2+ efflux in the caudate nucleus and hippocampus, and does not affect the efflux in MRF and brain stem; (2) at concentrations above 10 nM has no effect on the Ca2+ efflux in any of the four structures investigated; and (3) produces a biphasic effect on the depolarization-induced Ca2+ uptake, increasing it in all structures except MRF at 10 nM concentration, and decreasing it at concentrations higher than 10 nM, irrespective of the structure investigated. These results suggest that E(2), acting at extranuclear sites, modulates synaptic transmission via alterations of Ca2+ transport mechanisms in nerve endings.",
journal = "Experientia",
title = "17 beta-Estradiol in vitro affects Na-dependent and depolarization-induced Ca2+ transport in rat brain synaptosomes",
volume = "52",
number = "3",
pages = "217-220",
doi = "10.1007/BF01920709",
url = "https://hdl.handle.net/21.15107/rcub_vinar_1968"
}

Nikezić, G. S., Horvat, A., Nedeljković, N.,& Martinović, J.. (1996). 17 beta-Estradiol in vitro affects Na-dependent and depolarization-induced Ca2+ transport in rat brain synaptosomes. in Experientia, 52(3), 217-220.
https://doi.org/10.1007/BF01920709
https://hdl.handle.net/21.15107/rcub_vinar_1968

Nikezić GS, Horvat A, Nedeljković N, Martinović J. 17 beta-Estradiol in vitro affects Na-dependent and depolarization-induced Ca2+ transport in rat brain synaptosomes. in Experientia. 1996;52(3):217-220.
doi:10.1007/BF01920709
https://hdl.handle.net/21.15107/rcub_vinar_1968 .

Nikezić, Gordana S., Horvat, Anica, Nedeljković, N., Martinović, Jelena, "17 beta-Estradiol in vitro affects Na-dependent and depolarization-induced Ca2+ transport in rat brain synaptosomes" in Experientia, 52, no. 3 (1996):217-220,
https://doi.org/10.1007/BF01920709 .,
https://hdl.handle.net/21.15107/rcub_vinar_1968 .