TY  - CONF
AU  - Brkić, Predrag
AU  - Jovanović, Tomislav
AU  - Krstić, Danijela Z.
AU  - Stojiljković, Mirjana
AU  - Čolović, Mirjana B.
AU  - Dacic, Sanja
AU  - Mitrovic, Ana
AU  - Bjelaobaba, Ivana
AU  - Savić, Danijela
AU  - Parbucki, Ana
AU  - Lavrnja, Irena
AU  - Rakić, Ljubisav
AU  - Peković, Sanja
PY  - 2012
UR  - https://vinar.vin.bg.ac.rs/handle/123456789/4847
C3  - Brain Injury
T1  - Hyperbaric oxygenation reduces neuronal degeneration by regulation of oxidant/antioxidant status in the rat brain tissue after cortical injury
VL  - 26
IS  - 4-5
SP  - 486
EP  - 487
UR  - https://hdl.handle.net/21.15107/rcub_vinar_4847
ER  - 

@conference{
author = "Brkić, Predrag and Jovanović, Tomislav and Krstić, Danijela Z. and Stojiljković, Mirjana and Čolović, Mirjana B. and Dacic, Sanja and Mitrovic, Ana and Bjelaobaba, Ivana and Savić, Danijela and Parbucki, Ana and Lavrnja, Irena and Rakić, Ljubisav and Peković, Sanja",
year = "2012",
journal = "Brain Injury",
title = "Hyperbaric oxygenation reduces neuronal degeneration by regulation of oxidant/antioxidant status in the rat brain tissue after cortical injury",
volume = "26",
number = "4-5",
pages = "486-487",
url = "https://hdl.handle.net/21.15107/rcub_vinar_4847"
}

Brkić, P., Jovanović, T., Krstić, D. Z., Stojiljković, M., Čolović, M. B., Dacic, S., Mitrovic, A., Bjelaobaba, I., Savić, D., Parbucki, A., Lavrnja, I., Rakić, L.,& Peković, S.. (2012). Hyperbaric oxygenation reduces neuronal degeneration by regulation of oxidant/antioxidant status in the rat brain tissue after cortical injury. in Brain Injury, 26(4-5), 486-487.
https://hdl.handle.net/21.15107/rcub_vinar_4847

Brkić P, Jovanović T, Krstić DZ, Stojiljković M, Čolović MB, Dacic S, Mitrovic A, Bjelaobaba I, Savić D, Parbucki A, Lavrnja I, Rakić L, Peković S. Hyperbaric oxygenation reduces neuronal degeneration by regulation of oxidant/antioxidant status in the rat brain tissue after cortical injury. in Brain Injury. 2012;26(4-5):486-487.
https://hdl.handle.net/21.15107/rcub_vinar_4847 .

Brkić, Predrag, Jovanović, Tomislav, Krstić, Danijela Z., Stojiljković, Mirjana, Čolović, Mirjana B., Dacic, Sanja, Mitrovic, Ana, Bjelaobaba, Ivana, Savić, Danijela, Parbucki, Ana, Lavrnja, Irena, Rakić, Ljubisav, Peković, Sanja, "Hyperbaric oxygenation reduces neuronal degeneration by regulation of oxidant/antioxidant status in the rat brain tissue after cortical injury" in Brain Injury, 26, no. 4-5 (2012):486-487,
https://hdl.handle.net/21.15107/rcub_vinar_4847 .

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  - Stojiljković, Mirjana
AU  - Blagojević, T.
AU  - Vukosavić, S.
AU  - Zvezdina, Nataliya D.
AU  - Peković, Sanja
AU  - Nikezić, Gordana S.
AU  - Rakić, Ljubisav
PY  - 1996
UR  - https://vinar.vin.bg.ac.rs/handle/123456789/1967
AB  - The distribution of GM1 and GM3 gangliosides in human brain development between gestational week (g.w.) 6 and 15 was demonstrated by an immunocytochemical approach using polyclonal anti-GM1 and anti-GM3 antibodies. The first appearance of GM1- and GM3-positive cells was recorded as early as in g.w. 6. Both antibodies labeled the cells in the ventricular zone of the telencephalic wall, with radially oriented fibers toward the pial surface, which represent radial glia cells with glia fibers. The intensive GM3 immunoreactivity was also exhibited in proliferating cells in the ventricular zone between g.w. 6 and 12. During the period from g.w. 12 to 15, characterized by a rapid multiplication of neurons and glia cells, an increased number of GM1- and GM3-positive cells was observed. Prominent GM1 ganglioside staining was observed at the surface of the cell bodies in the ventricular zone. Besides surface labeling in migrating cells, GM1 immunoreactivity was identified inside the soma in the regions of cortical plate and subplate. GM1 immunoreactivity was more pronounced on the membrane of neuronal cells migrating along radial glia fibers, especially at the contact site between neuronal and glial cells. The GM3 ganglioside was localized mostly inside the soma, showing a granular immunoreactivity pattern. Our observations confirm the presence of GM1 and GM3 gangliosides in neuronal and glial cells in early human brain development. The involvement. especially of GM1 ganglioside in glia-neuronal contacts during migration of neuroblasts to their final destination, as well as the presence of GM3 ganglioside in proliferative cells in the ventricular zone of the telencephalic wall was also recorded.
T2  - International Journal of Developmental Neuroscience
T1  - Ganglioside GM1 and GM3 in early human brain development: An immunocytochemical study
VL  - 14
IS  - 1
SP  - 35
EP  - 44
DO  - 10.1016/0736-5748(95)00078-X
ER  - 

@article{
author = "Stojiljković, Mirjana and Blagojević, T. and Vukosavić, S. and Zvezdina, Nataliya D. and Peković, Sanja and Nikezić, Gordana S. and Rakić, Ljubisav",
year = "1996",
abstract = "The distribution of GM1 and GM3 gangliosides in human brain development between gestational week (g.w.) 6 and 15 was demonstrated by an immunocytochemical approach using polyclonal anti-GM1 and anti-GM3 antibodies. The first appearance of GM1- and GM3-positive cells was recorded as early as in g.w. 6. Both antibodies labeled the cells in the ventricular zone of the telencephalic wall, with radially oriented fibers toward the pial surface, which represent radial glia cells with glia fibers. The intensive GM3 immunoreactivity was also exhibited in proliferating cells in the ventricular zone between g.w. 6 and 12. During the period from g.w. 12 to 15, characterized by a rapid multiplication of neurons and glia cells, an increased number of GM1- and GM3-positive cells was observed. Prominent GM1 ganglioside staining was observed at the surface of the cell bodies in the ventricular zone. Besides surface labeling in migrating cells, GM1 immunoreactivity was identified inside the soma in the regions of cortical plate and subplate. GM1 immunoreactivity was more pronounced on the membrane of neuronal cells migrating along radial glia fibers, especially at the contact site between neuronal and glial cells. The GM3 ganglioside was localized mostly inside the soma, showing a granular immunoreactivity pattern. Our observations confirm the presence of GM1 and GM3 gangliosides in neuronal and glial cells in early human brain development. The involvement. especially of GM1 ganglioside in glia-neuronal contacts during migration of neuroblasts to their final destination, as well as the presence of GM3 ganglioside in proliferative cells in the ventricular zone of the telencephalic wall was also recorded.",
journal = "International Journal of Developmental Neuroscience",
title = "Ganglioside GM1 and GM3 in early human brain development: An immunocytochemical study",
volume = "14",
number = "1",
pages = "35-44",
doi = "10.1016/0736-5748(95)00078-X"
}

Stojiljković, M., Blagojević, T., Vukosavić, S., Zvezdina, N. D., Peković, S., Nikezić, G. S.,& Rakić, L.. (1996). Ganglioside GM1 and GM3 in early human brain development: An immunocytochemical study. in International Journal of Developmental Neuroscience, 14(1), 35-44.
https://doi.org/10.1016/0736-5748(95)00078-X

Stojiljković M, Blagojević T, Vukosavić S, Zvezdina ND, Peković S, Nikezić GS, Rakić L. Ganglioside GM1 and GM3 in early human brain development: An immunocytochemical study. in International Journal of Developmental Neuroscience. 1996;14(1):35-44.
doi:10.1016/0736-5748(95)00078-X .

Stojiljković, Mirjana, Blagojević, T., Vukosavić, S., Zvezdina, Nataliya D., Peković, Sanja, Nikezić, Gordana S., Rakić, Ljubisav, "Ganglioside GM1 and GM3 in early human brain development: An immunocytochemical study" in International Journal of Developmental Neuroscience, 14, no. 1 (1996):35-44,
https://doi.org/10.1016/0736-5748(95)00078-X . .