TY  - JOUR
AU  - Horvat, Anica
AU  - Orlić, T
AU  - Banjac, Ana
AU  - Momić, Tatjana
AU  - Petrović, S
AU  - Demajo, Miroslav
PY  - 2006
UR  - https://vinar.vin.bg.ac.rs/handle/123456789/3024
AB  - The in vitro effect of digoxin, verapamil, propranolol, carbamazepine, diazepam and promethazine were investigated on the ecto-ATPase activity of synaptosomal plasma membranes from the rat brain. ATP hydrolyzing activities of the enzyme were not affected by digoxin while the use of all other drugs resulted in significant and dose-dependent ihibition in ATP hydrolysis. According to values Of IC50 and K-iapp, the order of inhibitory potency of the drugs applied was: diazepam GT promethazine GT verapamil GT propranolol GT GT carbamazepine. Kinetic analysis of the nature of the ATPase inhibition revealed that it resulted from a direct action of drugs on the enzyme protein. The aim of the present study was to determine the potential neuromodulatory side effects of the drugs investigated. The results achieved indicated that all investigated drugs, except digoxin, may modulate neuronal activities via the purinergic receptors P2 by increasing extracellular concentrations of ATP as a consequence of inhibition of the ecto-ATPase activity. Our findings indicate that it may be useful to take into consideration the possible side effects of the investigated drugs, when they are used in treatment of different pathologies, particularly in the treatment of epilepsy by carbamazepine and diazepam.
T2  - General Physiology and Biophysics
T1  - Inhibition of rat brain ecto-ATPase activity by various drugs
VL  - 25
IS  - 1
SP  - 91
EP  - 105
UR  - https://hdl.handle.net/21.15107/rcub_vinar_3024
ER  - 

@article{
author = "Horvat, Anica and Orlić, T and Banjac, Ana and Momić, Tatjana and Petrović, S and Demajo, Miroslav",
year = "2006",
abstract = "The in vitro effect of digoxin, verapamil, propranolol, carbamazepine, diazepam and promethazine were investigated on the ecto-ATPase activity of synaptosomal plasma membranes from the rat brain. ATP hydrolyzing activities of the enzyme were not affected by digoxin while the use of all other drugs resulted in significant and dose-dependent ihibition in ATP hydrolysis. According to values Of IC50 and K-iapp, the order of inhibitory potency of the drugs applied was: diazepam GT promethazine GT verapamil GT propranolol GT GT carbamazepine. Kinetic analysis of the nature of the ATPase inhibition revealed that it resulted from a direct action of drugs on the enzyme protein. The aim of the present study was to determine the potential neuromodulatory side effects of the drugs investigated. The results achieved indicated that all investigated drugs, except digoxin, may modulate neuronal activities via the purinergic receptors P2 by increasing extracellular concentrations of ATP as a consequence of inhibition of the ecto-ATPase activity. Our findings indicate that it may be useful to take into consideration the possible side effects of the investigated drugs, when they are used in treatment of different pathologies, particularly in the treatment of epilepsy by carbamazepine and diazepam.",
journal = "General Physiology and Biophysics",
title = "Inhibition of rat brain ecto-ATPase activity by various drugs",
volume = "25",
number = "1",
pages = "91-105",
url = "https://hdl.handle.net/21.15107/rcub_vinar_3024"
}

Horvat, A., Orlić, T., Banjac, A., Momić, T., Petrović, S.,& Demajo, M.. (2006). Inhibition of rat brain ecto-ATPase activity by various drugs. in General Physiology and Biophysics, 25(1), 91-105.
https://hdl.handle.net/21.15107/rcub_vinar_3024

Horvat A, Orlić T, Banjac A, Momić T, Petrović S, Demajo M. Inhibition of rat brain ecto-ATPase activity by various drugs. in General Physiology and Biophysics. 2006;25(1):91-105.
https://hdl.handle.net/21.15107/rcub_vinar_3024 .

Horvat, Anica, Orlić, T, Banjac, Ana, Momić, Tatjana, Petrović, S, Demajo, Miroslav, "Inhibition of rat brain ecto-ATPase activity by various drugs" in General Physiology and Biophysics, 25, no. 1 (2006):91-105,
https://hdl.handle.net/21.15107/rcub_vinar_3024 .

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  - 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 .