Basal protein phosphorylation is decreased and phosphatase activity increased by an antioxidant and a free radical trap in primary rat glia

Citation
Ka. Robinson et al., Basal protein phosphorylation is decreased and phosphatase activity increased by an antioxidant and a free radical trap in primary rat glia, ARCH BIOCH, 365(2), 1999, pp. 211-215
Citations number
16
Language
INGLESE
art.tipo
Article
Categorie Soggetti
Biochemistry & Biophysics
Journal title
ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS
ISSN journal
0003-9861 → ACNP
Volume
365
Issue
2
Year of publication
1999
Pages
211 - 215
Database
ISI
SICI code
0003-9861(19990515)365:2<211:BPPIDA>2.0.ZU;2-F
Abstract
Reversible protein phosphorylation regulates a wide array of cellular funct ions. Cells respond to cytokines and various stressors via phosphorylation and thus activation of one or more of the mitogen-activated protein kinase (MAPK) pathways. Involvement of these signal transduction pathways has been implicated in numerous pathologies, including inflammation. Using a primar y glia cell culture, we show here that the antioxidant N-acetylcysteine (NA C) and the nitrone-based free radical trap, alpha-phenyl-N-tert-butyl nitro ne (PBN), reduce total basal protein phosphorylation in a concentration-dep endent manner as assessed by phosphotyrosine analysis and by [gamma-P-32]AT P transfer radioassay. In addition we show that NAC inhibits H2O2-induced p hosphatase inactivation in glia cell lysate. The PBN- and NAG-induced reduc tion in protein phosphorylation is accompanied by an increase in phosphatas e activity, suggesting that PEN and NAC reduce protein phosphorylation by g lobally augmenting oxidant-sensitive phosphatase activities. These results partly explain why certain antioxidants also possess anti-inflammatory acti ons, (C) 1999 Academic Press.