TY  - CONF
AU  - Stanišić, Jelena
AU  - Korićanac, Goran
AU  - Stojiljković, Mirjana
AU  - Ćulafić, Tijana
AU  - Kostić, Mirjana M.
AU  - Romić, Snježana Đ.
AU  - Pantelić, Marija
AU  - Tepavčević, Snežana
PY  - 2018
UR  - https://vinar.vin.bg.ac.rs/handle/123456789/7920
C3  - FEBS OPEN BIO
T1  - Low intensity exercise prevents disturbances in insulin regulation of alpha subunits of Na plus /K plus -ATPase in the heart of fructose-fed female rats
VL  - 8
IS  - Supplement 1
SP  - 224
DO  - 10.1002/2211-5463.12453
ER  - 

@conference{
author = "Stanišić, Jelena and Korićanac, Goran and Stojiljković, Mirjana and Ćulafić, Tijana and Kostić, Mirjana M. and Romić, Snježana Đ. and Pantelić, Marija and Tepavčević, Snežana",
year = "2018",
journal = "FEBS OPEN BIO",
title = "Low intensity exercise prevents disturbances in insulin regulation of alpha subunits of Na plus /K plus -ATPase in the heart of fructose-fed female rats",
volume = "8",
number = "Supplement 1",
pages = "224",
doi = "10.1002/2211-5463.12453"
}

Stanišić, J., Korićanac, G., Stojiljković, M., Ćulafić, T., Kostić, M. M., Romić, S. Đ., Pantelić, M.,& Tepavčević, S.. (2018). Low intensity exercise prevents disturbances in insulin regulation of alpha subunits of Na plus /K plus -ATPase in the heart of fructose-fed female rats. in FEBS OPEN BIO, 8(Supplement 1), 224.
https://doi.org/10.1002/2211-5463.12453

Stanišić J, Korićanac G, Stojiljković M, Ćulafić T, Kostić MM, Romić SĐ, Pantelić M, Tepavčević S. Low intensity exercise prevents disturbances in insulin regulation of alpha subunits of Na plus /K plus -ATPase in the heart of fructose-fed female rats. in FEBS OPEN BIO. 2018;8(Supplement 1):224.
doi:10.1002/2211-5463.12453 .

Stanišić, Jelena, Korićanac, Goran, Stojiljković, Mirjana, Ćulafić, Tijana, Kostić, Mirjana M., Romić, Snježana Đ., Pantelić, Marija, Tepavčević, Snežana, "Low intensity exercise prevents disturbances in insulin regulation of alpha subunits of Na plus /K plus -ATPase in the heart of fructose-fed female rats" in FEBS OPEN BIO, 8, no. Supplement 1 (2018):224,
https://doi.org/10.1002/2211-5463.12453 . .

TY  - CONF
AU  - Kostić, Milan
AU  - Korićanac, Goran
AU  - Tepavčević, Snežana
AU  - Ćulafić, Tijana
AU  - Romić, Snježana Đ.
AU  - Stanišić, Jelena
AU  - Pantelić, Marija
AU  - Stojiljković, Mirjana
PY  - 2018
UR  - https://vinar.vin.bg.ac.rs/handle/123456789/7922
C3  - FEBS OPEN BIO
T1  - Moderate physical activity alters cardiac lipid metabolism of male rats on high fructose diet
VL  - 8
IS  - Supplement 1
SP  - 223
DO  - 10.1002/2211-5463.12453
ER  - 

@conference{
author = "Kostić, Milan and Korićanac, Goran and Tepavčević, Snežana and Ćulafić, Tijana and Romić, Snježana Đ. and Stanišić, Jelena and Pantelić, Marija and Stojiljković, Mirjana",
year = "2018",
journal = "FEBS OPEN BIO",
title = "Moderate physical activity alters cardiac lipid metabolism of male rats on high fructose diet",
volume = "8",
number = "Supplement 1",
pages = "223",
doi = "10.1002/2211-5463.12453"
}

Kostić, M., Korićanac, G., Tepavčević, S., Ćulafić, T., Romić, S. Đ., Stanišić, J., Pantelić, M.,& Stojiljković, M.. (2018). Moderate physical activity alters cardiac lipid metabolism of male rats on high fructose diet. in FEBS OPEN BIO, 8(Supplement 1), 223.
https://doi.org/10.1002/2211-5463.12453

Kostić M, Korićanac G, Tepavčević S, Ćulafić T, Romić SĐ, Stanišić J, Pantelić M, Stojiljković M. Moderate physical activity alters cardiac lipid metabolism of male rats on high fructose diet. in FEBS OPEN BIO. 2018;8(Supplement 1):223.
doi:10.1002/2211-5463.12453 .

Kostić, Milan, Korićanac, Goran, Tepavčević, Snežana, Ćulafić, Tijana, Romić, Snježana Đ., Stanišić, Jelena, Pantelić, Marija, Stojiljković, Mirjana, "Moderate physical activity alters cardiac lipid metabolism of male rats on high fructose diet" in FEBS OPEN BIO, 8, no. Supplement 1 (2018):223,
https://doi.org/10.1002/2211-5463.12453 . .

TY  - JOUR
AU  - Laketa, Danijela
AU  - Savić, Jasmina
AU  - Bjelobaba, Ivana
AU  - Lavrnja, Irene
AU  - Vasić, Vesna M.
AU  - Stojiljković, Mirjana
AU  - Nedeljković, Nadežda
PY  - 2015
UR  - https://vinar.vin.bg.ac.rs/handle/123456789/385
AB  - Background: Cortical stab injury (CSI) induces changes in the activity, expression and cellular distribution of specific ectonucleotidases at the injury site. Also, several experimentally induced neuropathologies are associated with changes in soluble ectonucleotidase activities in the plasma and serum, whilst various insults to the brain alter purine compounds levels in cerebrospinal fluid, but also in serum, indicating that insults to the brain may induce alterations in nucleotides release and rate of their hydrolysis in the vascular system. Since adenine nucleotides and adenosine regulate diverse cellular functions in the vascular system, including vascular tone, platelet aggregation and inflammatory responses of lymphocytes and macrophages, alterations of ectonucleotidase activities in the vascular system may be relevant for the clinical outcome of the primary insult. Methods: We explored ectonucleotidase activities using specific enzyme assays and determined adenine nucleotides concentrations by the UPLC method in the rat serum after cortical stab injury. Results: At 4-h post-injury, ATP and AMP hydrolysis increased by about 60% and 40%, respectively, while phosphodiesterase activity remained unchanged. Also, at 4-h postinjury a marked decrease in ATP concentration and more than 2-fold increase in AMP concentration were recorded. Conclusions: CSI induces rapid up-regulation of nucleotide catabolizing soluble ectonucleotidases in rat serum, which leads to the observed shift in serum nucleotide levels. The results obtained imply that ectonucleotidases and adenine nucleotides participate in the communication between the brain and the vascular system in physiological and pathological conditions and thereby may be involved in the development of various human neuropathologies.
T2  - Journal of Medical Biochemistry
T1  - Brain Injury Alters Ectonucleotidase Activities and Adenine Nucleotide Levels in Rat Serum
VL  - 34
IS  - 2
SP  - 215
EP  - 222
DO  - 10.2478/jomb-2014-0025
ER  - 

@article{
author = "Laketa, Danijela and Savić, Jasmina and Bjelobaba, Ivana and Lavrnja, Irene and Vasić, Vesna M. and Stojiljković, Mirjana and Nedeljković, Nadežda",
year = "2015",
abstract = "Background: Cortical stab injury (CSI) induces changes in the activity, expression and cellular distribution of specific ectonucleotidases at the injury site. Also, several experimentally induced neuropathologies are associated with changes in soluble ectonucleotidase activities in the plasma and serum, whilst various insults to the brain alter purine compounds levels in cerebrospinal fluid, but also in serum, indicating that insults to the brain may induce alterations in nucleotides release and rate of their hydrolysis in the vascular system. Since adenine nucleotides and adenosine regulate diverse cellular functions in the vascular system, including vascular tone, platelet aggregation and inflammatory responses of lymphocytes and macrophages, alterations of ectonucleotidase activities in the vascular system may be relevant for the clinical outcome of the primary insult. Methods: We explored ectonucleotidase activities using specific enzyme assays and determined adenine nucleotides concentrations by the UPLC method in the rat serum after cortical stab injury. Results: At 4-h post-injury, ATP and AMP hydrolysis increased by about 60% and 40%, respectively, while phosphodiesterase activity remained unchanged. Also, at 4-h postinjury a marked decrease in ATP concentration and more than 2-fold increase in AMP concentration were recorded. Conclusions: CSI induces rapid up-regulation of nucleotide catabolizing soluble ectonucleotidases in rat serum, which leads to the observed shift in serum nucleotide levels. The results obtained imply that ectonucleotidases and adenine nucleotides participate in the communication between the brain and the vascular system in physiological and pathological conditions and thereby may be involved in the development of various human neuropathologies.",
journal = "Journal of Medical Biochemistry",
title = "Brain Injury Alters Ectonucleotidase Activities and Adenine Nucleotide Levels in Rat Serum",
volume = "34",
number = "2",
pages = "215-222",
doi = "10.2478/jomb-2014-0025"
}

Laketa, D., Savić, J., Bjelobaba, I., Lavrnja, I., Vasić, V. M., Stojiljković, M.,& Nedeljković, N.. (2015). Brain Injury Alters Ectonucleotidase Activities and Adenine Nucleotide Levels in Rat Serum. in Journal of Medical Biochemistry, 34(2), 215-222.
https://doi.org/10.2478/jomb-2014-0025

Laketa D, Savić J, Bjelobaba I, Lavrnja I, Vasić VM, Stojiljković M, Nedeljković N. Brain Injury Alters Ectonucleotidase Activities and Adenine Nucleotide Levels in Rat Serum. in Journal of Medical Biochemistry. 2015;34(2):215-222.
doi:10.2478/jomb-2014-0025 .

Laketa, Danijela, Savić, Jasmina, Bjelobaba, Ivana, Lavrnja, Irene, Vasić, Vesna M., Stojiljković, Mirjana, Nedeljković, Nadežda, "Brain Injury Alters Ectonucleotidase Activities and Adenine Nucleotide Levels in Rat Serum" in Journal of Medical Biochemistry, 34, no. 2 (2015):215-222,
https://doi.org/10.2478/jomb-2014-0025 . .

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  - Filipović, Dragana
AU  - Martinović, Jelena
AU  - Inta, Dragos
AU  - Bjelobaba, I.
AU  - Stojiljković, Mirjana
AU  - Gass, Peter
PY  - 2011
UR  - https://vinar.vin.bg.ac.rs/handle/123456789/4409
AB  - Mitochondria are central integrators and transducers of proapoptotic signals for neuronal apoptosis. The tumor suppressor protein p53 can trigger apoptosis independently of its transcriptional activity, through subcellular translocation of cytochrome c and caspase activation. To define better the proapoptotic role of p53 under various stress conditions, we investigated the protein levels of p53 and cytochrome c in mitochondrial and cytosolic fractions, as well as caspase-3 activation and apoptosis, in the prefrontal cortex and hippocampus of male Wistar rats subjected to acute, chronic, or combined stressors. Mitochondrial p53 can suppress the antioxidant enzyme MnSOD, so its activity was also determined. In the prefrontal cortex, but not in hippocampus, increased protein levels of p53 were found in mitochondria, leading to cytochrome c release into cytoplasm, activation of caspase-3, and apoptotic cell death following combined stressors. Decreased mitochondrial MnSOD activity following combined stressors in both brain structures indicated a state of oxidative stress. This suggests that chronic isolation stress compromises mitochondrial MnSOD activity in both the prefrontal cortex and the hippocampus but likely results in mitochondrial-triggered proapoptotic signaling mediated by a transcription-independent p53 mechanism only in the prefrontal cortex. Thus, our data demonstrate a tissue-specific (prefrontal cortex vs. hippocampus) response to applied stressors. (C) 2011 Wiley-Liss, Inc.
T2  - Journal of Neuroscience Research
T1  - Chronic Isolation Stress Predisposes the Frontal Cortex but Not the Hippocampus to the Potentially Detrimental Release of Cytochrome c From Mitochondria and the Activation of Caspase-3
VL  - 89
IS  - 9
SP  - 1461
EP  - 1470
DO  - 10.1002/jnr.22687
ER  - 

@article{
author = "Filipović, Dragana and Martinović, Jelena and Inta, Dragos and Bjelobaba, I. and Stojiljković, Mirjana and Gass, Peter",
year = "2011",
abstract = "Mitochondria are central integrators and transducers of proapoptotic signals for neuronal apoptosis. The tumor suppressor protein p53 can trigger apoptosis independently of its transcriptional activity, through subcellular translocation of cytochrome c and caspase activation. To define better the proapoptotic role of p53 under various stress conditions, we investigated the protein levels of p53 and cytochrome c in mitochondrial and cytosolic fractions, as well as caspase-3 activation and apoptosis, in the prefrontal cortex and hippocampus of male Wistar rats subjected to acute, chronic, or combined stressors. Mitochondrial p53 can suppress the antioxidant enzyme MnSOD, so its activity was also determined. In the prefrontal cortex, but not in hippocampus, increased protein levels of p53 were found in mitochondria, leading to cytochrome c release into cytoplasm, activation of caspase-3, and apoptotic cell death following combined stressors. Decreased mitochondrial MnSOD activity following combined stressors in both brain structures indicated a state of oxidative stress. This suggests that chronic isolation stress compromises mitochondrial MnSOD activity in both the prefrontal cortex and the hippocampus but likely results in mitochondrial-triggered proapoptotic signaling mediated by a transcription-independent p53 mechanism only in the prefrontal cortex. Thus, our data demonstrate a tissue-specific (prefrontal cortex vs. hippocampus) response to applied stressors. (C) 2011 Wiley-Liss, Inc.",
journal = "Journal of Neuroscience Research",
title = "Chronic Isolation Stress Predisposes the Frontal Cortex but Not the Hippocampus to the Potentially Detrimental Release of Cytochrome c From Mitochondria and the Activation of Caspase-3",
volume = "89",
number = "9",
pages = "1461-1470",
doi = "10.1002/jnr.22687"
}

Filipović, D., Martinović, J., Inta, D., Bjelobaba, I., Stojiljković, M.,& Gass, P.. (2011). Chronic Isolation Stress Predisposes the Frontal Cortex but Not the Hippocampus to the Potentially Detrimental Release of Cytochrome c From Mitochondria and the Activation of Caspase-3. in Journal of Neuroscience Research, 89(9), 1461-1470.
https://doi.org/10.1002/jnr.22687

Filipović D, Martinović J, Inta D, Bjelobaba I, Stojiljković M, Gass P. Chronic Isolation Stress Predisposes the Frontal Cortex but Not the Hippocampus to the Potentially Detrimental Release of Cytochrome c From Mitochondria and the Activation of Caspase-3. in Journal of Neuroscience Research. 2011;89(9):1461-1470.
doi:10.1002/jnr.22687 .

Filipović, Dragana, Martinović, Jelena, Inta, Dragos, Bjelobaba, I., Stojiljković, Mirjana, Gass, Peter, "Chronic Isolation Stress Predisposes the Frontal Cortex but Not the Hippocampus to the Potentially Detrimental Release of Cytochrome c From Mitochondria and the Activation of Caspase-3" in Journal of Neuroscience Research, 89, no. 9 (2011):1461-1470,
https://doi.org/10.1002/jnr.22687 . .

TY  - JOUR
AU  - Stanojević, Ivana
AU  - Bjelobaba, Ivana
AU  - Nedeljković, Nadežda
AU  - Drakulić, Dunja R.
AU  - Petrović, Snježana
AU  - Stojiljković, Mirjana
AU  - Horvat, Anica
PY  - 2011
UR  - https://vinar.vin.bg.ac.rs/handle/123456789/4376
AB  - Ecto-5-nucleotidase (CD73; EC 3.1.3.5, e-5NT) is regarded as the key enzyme in the extracellular formation of adenosine, which acts as a neuromodulator and important trophic and homeostatic factor in the brain. In the present study, we have investigated e-5NT activity, kinetic properties concerning AMP hydrolysis and the enzyme protein abundance in the purified synaptic plasma membrane (SPM) preparations isolated from whole female rat brain at different ages. We observed pronounced increase in AMP hydrolyzing activity in SPM during maturation, with greatest increment between juvenile (15-day-old) and pre-pubertal (30-day-old) rats. Immunodetection of e-5NT protein in the SPM displayed the reverse pattern of expression, with the maximum relative abundance at juvenile and minimum relative abundance in the adult stage. Negative correlation between the enzyme activity and the enzyme protein abundance in the SPM indicates that e-5NT has additional roles in the synaptic compartment during postnatal brain development, other than those related to AMP hydrolysis. Determination of kinetic parameters, K(m) and V(max), suggested that the increase in the enzyme activity with maturation was entirely due to the increase in the enzyme catalytic efficiency (V(max)/K(m)). Finally, double immunofluorescence staining against e-5NT and presynaptic membrane marker syntaxin provided first direct evidence for the existence of this ecto-enzyme in the presynaptic compartment. The results of the study suggest that e-5NT may be a part of general scheme of brain development and synapse maturation and provide rationale for the previously reported inconsistencies between enzyme immunohistochemical and biochemical studies concerning localization of e-5NT in the brain. (C) 2011 ISDN. Published by Elsevier Ltd. All rights reserved.
T2  - International Journal of Developmental Neuroscience
T1  - Ontogenetic profile of ecto-5 -nucleotidase in rat brain synaptic plasma membranes
VL  - 29
IS  - 4
SP  - 397
EP  - 403
DO  - 10.1016/j.ijdevneu.2011.03.003
ER  - 

@article{
author = "Stanojević, Ivana and Bjelobaba, Ivana and Nedeljković, Nadežda and Drakulić, Dunja R. and Petrović, Snježana and Stojiljković, Mirjana and Horvat, Anica",
year = "2011",
abstract = "Ecto-5-nucleotidase (CD73; EC 3.1.3.5, e-5NT) is regarded as the key enzyme in the extracellular formation of adenosine, which acts as a neuromodulator and important trophic and homeostatic factor in the brain. In the present study, we have investigated e-5NT activity, kinetic properties concerning AMP hydrolysis and the enzyme protein abundance in the purified synaptic plasma membrane (SPM) preparations isolated from whole female rat brain at different ages. We observed pronounced increase in AMP hydrolyzing activity in SPM during maturation, with greatest increment between juvenile (15-day-old) and pre-pubertal (30-day-old) rats. Immunodetection of e-5NT protein in the SPM displayed the reverse pattern of expression, with the maximum relative abundance at juvenile and minimum relative abundance in the adult stage. Negative correlation between the enzyme activity and the enzyme protein abundance in the SPM indicates that e-5NT has additional roles in the synaptic compartment during postnatal brain development, other than those related to AMP hydrolysis. Determination of kinetic parameters, K(m) and V(max), suggested that the increase in the enzyme activity with maturation was entirely due to the increase in the enzyme catalytic efficiency (V(max)/K(m)). Finally, double immunofluorescence staining against e-5NT and presynaptic membrane marker syntaxin provided first direct evidence for the existence of this ecto-enzyme in the presynaptic compartment. The results of the study suggest that e-5NT may be a part of general scheme of brain development and synapse maturation and provide rationale for the previously reported inconsistencies between enzyme immunohistochemical and biochemical studies concerning localization of e-5NT in the brain. (C) 2011 ISDN. Published by Elsevier Ltd. All rights reserved.",
journal = "International Journal of Developmental Neuroscience",
title = "Ontogenetic profile of ecto-5 -nucleotidase in rat brain synaptic plasma membranes",
volume = "29",
number = "4",
pages = "397-403",
doi = "10.1016/j.ijdevneu.2011.03.003"
}

Stanojević, I., Bjelobaba, I., Nedeljković, N., Drakulić, D. R., Petrović, S., Stojiljković, M.,& Horvat, A.. (2011). Ontogenetic profile of ecto-5 -nucleotidase in rat brain synaptic plasma membranes. in International Journal of Developmental Neuroscience, 29(4), 397-403.
https://doi.org/10.1016/j.ijdevneu.2011.03.003

Stanojević I, Bjelobaba I, Nedeljković N, Drakulić DR, Petrović S, Stojiljković M, Horvat A. Ontogenetic profile of ecto-5 -nucleotidase in rat brain synaptic plasma membranes. in International Journal of Developmental Neuroscience. 2011;29(4):397-403.
doi:10.1016/j.ijdevneu.2011.03.003 .

Stanojević, Ivana, Bjelobaba, Ivana, Nedeljković, Nadežda, Drakulić, Dunja R., Petrović, Snježana, Stojiljković, Mirjana, Horvat, Anica, "Ontogenetic profile of ecto-5 -nucleotidase in rat brain synaptic plasma membranes" in International Journal of Developmental Neuroscience, 29, no. 4 (2011):397-403,
https://doi.org/10.1016/j.ijdevneu.2011.03.003 . .

TY  - JOUR
AU  - Laketa, Danijela
AU  - Bjelobaba, Ivana
AU  - Savić, Jasmina
AU  - Lavrnja, Irena
AU  - Stojiljković, Mirjana
AU  - Rakić, Ljubisav
AU  - Nedeljković, Nadežda
PY  - 2010
UR  - https://vinar.vin.bg.ac.rs/handle/123456789/3996
AB  - Biochemical properties of nucleotide pyrophosphatase/phosphodiesterase (NPP) in rat serum have been described by assessing its nucleotide phosphodiesterase activity, using p-nitrophenyl-5-thymidine monophosphate (p-Nph-5-TMP) as a substrate. It was demonstrated that NPP activity shares some typical characteristics described for other soluble NPP, such as divalent cation dependence, strong alkaline pH optimum (pH 10.5), inhibition by glycosaminoglycans, and K (m) for p-Nph-5-TMP hydrolysis of 61.8 +/- A 5.2 mu M. In order to characterize the relation between phosphodiesterase and pyrophosphatase activities of NPP, we have analyzed the effects of different natural nucleotides and nucleotide analogs. ATP, ADP, and AMP competitively inhibited p-Nph-5-TMP hydrolysis with K (i) values ranging 13-43 mu M. Nucleotide analogs, alpha,beta-metATP, BzATP, 2-MeSATP, and dialATP behaved as competitive inhibitors, whereas alpha,beta-metADP induced mixed inhibition, with K (i) ranging from 2 to 20 mu M. Chromatographic analysis revealed that alpha,beta-metATP, BzATP, and 2-MeSATP were catalytically degraded in the serum, whereas dialATP and alpha,beta-metADP resisted hydrolysis, implying that the former act as substrates and the latter as true competitive inhibitors of serum NPP activity. Since NPP activity is involved in generation, breakdown, and recycling of extracellular adenine nucleotides in the vascular compartment, the results suggest that both hydrolyzable and non-hydrolyzable nucleotide analogs could alter the amplitude and direction of ATP actions and could have potential therapeutic application.
T2  - Molecular and Cellular Biochemistry
T1  - Biochemical characterization of soluble nucleotide pyrophosphatase/phosphodiesterase activity in rat serum
VL  - 339
IS  - 1-2
SP  - 99
EP  - 106
DO  - 10.1007/s11010-009-0373-1
ER  - 

@article{
author = "Laketa, Danijela and Bjelobaba, Ivana and Savić, Jasmina and Lavrnja, Irena and Stojiljković, Mirjana and Rakić, Ljubisav and Nedeljković, Nadežda",
year = "2010",
abstract = "Biochemical properties of nucleotide pyrophosphatase/phosphodiesterase (NPP) in rat serum have been described by assessing its nucleotide phosphodiesterase activity, using p-nitrophenyl-5-thymidine monophosphate (p-Nph-5-TMP) as a substrate. It was demonstrated that NPP activity shares some typical characteristics described for other soluble NPP, such as divalent cation dependence, strong alkaline pH optimum (pH 10.5), inhibition by glycosaminoglycans, and K (m) for p-Nph-5-TMP hydrolysis of 61.8 +/- A 5.2 mu M. In order to characterize the relation between phosphodiesterase and pyrophosphatase activities of NPP, we have analyzed the effects of different natural nucleotides and nucleotide analogs. ATP, ADP, and AMP competitively inhibited p-Nph-5-TMP hydrolysis with K (i) values ranging 13-43 mu M. Nucleotide analogs, alpha,beta-metATP, BzATP, 2-MeSATP, and dialATP behaved as competitive inhibitors, whereas alpha,beta-metADP induced mixed inhibition, with K (i) ranging from 2 to 20 mu M. Chromatographic analysis revealed that alpha,beta-metATP, BzATP, and 2-MeSATP were catalytically degraded in the serum, whereas dialATP and alpha,beta-metADP resisted hydrolysis, implying that the former act as substrates and the latter as true competitive inhibitors of serum NPP activity. Since NPP activity is involved in generation, breakdown, and recycling of extracellular adenine nucleotides in the vascular compartment, the results suggest that both hydrolyzable and non-hydrolyzable nucleotide analogs could alter the amplitude and direction of ATP actions and could have potential therapeutic application.",
journal = "Molecular and Cellular Biochemistry",
title = "Biochemical characterization of soluble nucleotide pyrophosphatase/phosphodiesterase activity in rat serum",
volume = "339",
number = "1-2",
pages = "99-106",
doi = "10.1007/s11010-009-0373-1"
}

Laketa, D., Bjelobaba, I., Savić, J., Lavrnja, I., Stojiljković, M., Rakić, L.,& Nedeljković, N.. (2010). Biochemical characterization of soluble nucleotide pyrophosphatase/phosphodiesterase activity in rat serum. in Molecular and Cellular Biochemistry, 339(1-2), 99-106.
https://doi.org/10.1007/s11010-009-0373-1

Laketa D, Bjelobaba I, Savić J, Lavrnja I, Stojiljković M, Rakić L, Nedeljković N. Biochemical characterization of soluble nucleotide pyrophosphatase/phosphodiesterase activity in rat serum. in Molecular and Cellular Biochemistry. 2010;339(1-2):99-106.
doi:10.1007/s11010-009-0373-1 .

Laketa, Danijela, Bjelobaba, Ivana, Savić, Jasmina, Lavrnja, Irena, Stojiljković, Mirjana, Rakić, Ljubisav, Nedeljković, Nadežda, "Biochemical characterization of soluble nucleotide pyrophosphatase/phosphodiesterase activity in rat serum" in Molecular and Cellular Biochemistry, 339, no. 1-2 (2010):99-106,
https://doi.org/10.1007/s11010-009-0373-1 . .

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  - 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 . .