INHIBITORY EFFECT OF VANADATE ON PROTEIN PHOSPHATASE, GLYCOGEN-PHOSPHORYLASE AND PROTEIN-KINASE IN EXTRACTS FROM SEVERAL RAT-TISSUES

Citation
Hk. Parsadanian et al., INHIBITORY EFFECT OF VANADATE ON PROTEIN PHOSPHATASE, GLYCOGEN-PHOSPHORYLASE AND PROTEIN-KINASE IN EXTRACTS FROM SEVERAL RAT-TISSUES, Toxicology in vitro, 11(5), 1997, pp. 527-530
Citations number
13
Categorie Soggetti
Toxicology
Journal title
ISSN journal
08872333
Volume
11
Issue
5
Year of publication
1997
Pages
527 - 530
Database
ISI
SICI code
0887-2333(1997)11:5<527:IEOVOP>2.0.ZU;2-0
Abstract
The purpose of this study was to determine the in vitro effect of incr easing vanadate concentrations (1 nM-1 mM) on protein phosphatase (PP) and glycogen phosphorylase (GP) of extracts from several rat tissues. PP activity was inhibited in various brain structures by moderate con centrations of vanadate: however, in the spinal cord, comparatively lo w concentrations (10 nM) of vanadate caused a steep increase in enzyme activity. Only at a high concentration (1 mM) did vanadate produce mo derate PP inhibition. Reciprocal correlation was obtained between vana date effects on PP and GP in various parts of the nervous system. In t he last series of experiments the effect of vanadate upon protein kina se (PK) activity in various regions of the CNS was determined; low and intermediate vanadate concentrations produced a moderate activation; higher vanadate concentrations suppressed the enzyme activity. Vanadat e at a concentration of 0.1 mM produced activation of PK in the medull a oblongata, whereas at mM vanadate there was significant inhibition o f PK. The spinal cord enzyme was more sensitive to vanadate, being inh ibited at concentrations of 10 nM-1 mM. (C) 1997 Published by Elsevier Science Ltd.