Jovanović, N.

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  • Jovanović, N. (1)
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Kinetic characterization of ecto-nucleoside triphosphate diphosphohydrolases in brain nerve terminals during rat postnatal development

Stanojević, Ivana; Drakulić, Dunja R.; Petrovic, S.; Milošević, Maja; Jovanović, N.; Horvat, Anica

(2011)

TY  - JOUR
AU  - Stanojević, Ivana
AU  - Drakulić, Dunja R.
AU  - Petrovic, S.
AU  - Milošević, Maja
AU  - Jovanović, N.
AU  - Horvat, Anica
PY  - 2011
UR  - https://vinar.vin.bg.ac.rs/handle/123456789/4603
AB  - A family of enzymes named ecto-nucleoside triphosphate diphosphohydrolase (NTPDases) catalyzes the termination of ATP and ADP actions. Three different NTPDases (NTPDase 1-3), differing in their preference for a substrate, have been localized in the brain of adult mammals. The goal of our study was to clarify ATP and ADP hydrolyzing activities and kinetic parameters of NTPDases in synaptic plasma membranes (SPM) isolated from 15-, 30-, 60- and 90-days-old female rat brains. ATP and ADP hydrolysis were maximal in the presence of Mg(2+) and showed insensitivity to ion-transporting ATPase inhibitors. The pronounced increase in both, ATP and ADP hydrolysis, were found in the SPM isolated from rats in the first month of life, stayed at the same level in the second month, and then decreased in adulthood. Kinetic analysis are also developmental-dependent, and together with the rate of ATP:ADP hydrolysis, point that all three NTPDases are present in SPM isolated from different developmental stages, with different, developmental-dependent proportion of activities. The lowest velocity and the highest affinity were observed for ATP hydrolyses, while the highest velocity and lowest affinity were detected for ADP hydrolyses in SPM isolated from 15-day old rats. Since specific ATP and ADP hydrolysis were lowest in this stage, we concluded that velocity is crucial for ATPase-, while affinity is for ADPase-part of NTPDases. Increased NTPDases activities, changes in their hydrolysis velocity and substrates affinities during rat postnatal development indicate involvement of adenine nucleotides in processes implicated to neuronal maturation and augmented neuroprotection.
T2  - Russian Journal of Physical Chemistry A
T1  - Kinetic characterization of ecto-nucleoside triphosphate diphosphohydrolases in brain nerve terminals during rat postnatal development
VL  - 85
IS  - 13
SP  - 2416
EP  - 2421
DO  - 10.1134/S0036024411130292
ER  - 
@article{
author = "Stanojević, Ivana and Drakulić, Dunja R. and Petrovic, S. and Milošević, Maja and Jovanović, N. and Horvat, Anica",
year = "2011",
abstract = "A family of enzymes named ecto-nucleoside triphosphate diphosphohydrolase (NTPDases) catalyzes the termination of ATP and ADP actions. Three different NTPDases (NTPDase 1-3), differing in their preference for a substrate, have been localized in the brain of adult mammals. The goal of our study was to clarify ATP and ADP hydrolyzing activities and kinetic parameters of NTPDases in synaptic plasma membranes (SPM) isolated from 15-, 30-, 60- and 90-days-old female rat brains. ATP and ADP hydrolysis were maximal in the presence of Mg(2+) and showed insensitivity to ion-transporting ATPase inhibitors. The pronounced increase in both, ATP and ADP hydrolysis, were found in the SPM isolated from rats in the first month of life, stayed at the same level in the second month, and then decreased in adulthood. Kinetic analysis are also developmental-dependent, and together with the rate of ATP:ADP hydrolysis, point that all three NTPDases are present in SPM isolated from different developmental stages, with different, developmental-dependent proportion of activities. The lowest velocity and the highest affinity were observed for ATP hydrolyses, while the highest velocity and lowest affinity were detected for ADP hydrolyses in SPM isolated from 15-day old rats. Since specific ATP and ADP hydrolysis were lowest in this stage, we concluded that velocity is crucial for ATPase-, while affinity is for ADPase-part of NTPDases. Increased NTPDases activities, changes in their hydrolysis velocity and substrates affinities during rat postnatal development indicate involvement of adenine nucleotides in processes implicated to neuronal maturation and augmented neuroprotection.",
journal = "Russian Journal of Physical Chemistry A",
title = "Kinetic characterization of ecto-nucleoside triphosphate diphosphohydrolases in brain nerve terminals during rat postnatal development",
volume = "85",
number = "13",
pages = "2416-2421",
doi = "10.1134/S0036024411130292"
}
Stanojević, I., Drakulić, D. R., Petrovic, S., Milošević, M., Jovanović, N.,& Horvat, A.. (2011). Kinetic characterization of ecto-nucleoside triphosphate diphosphohydrolases in brain nerve terminals during rat postnatal development. in Russian Journal of Physical Chemistry A, 85(13), 2416-2421.
https://doi.org/10.1134/S0036024411130292
Stanojević I, Drakulić DR, Petrovic S, Milošević M, Jovanović N, Horvat A. Kinetic characterization of ecto-nucleoside triphosphate diphosphohydrolases in brain nerve terminals during rat postnatal development. in Russian Journal of Physical Chemistry A. 2011;85(13):2416-2421.
doi:10.1134/S0036024411130292 .
Stanojević, Ivana, Drakulić, Dunja R., Petrovic, S., Milošević, Maja, Jovanović, N., Horvat, Anica, "Kinetic characterization of ecto-nucleoside triphosphate diphosphohydrolases in brain nerve terminals during rat postnatal development" in Russian Journal of Physical Chemistry A, 85, no. 13 (2011):2416-2421,
https://doi.org/10.1134/S0036024411130292 . .
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