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

Basal protein phosphorylation is decreased and phosphatase activity increased by an antioxidant and a free radical trap in primary rat glia.
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原代大鼠神经胶质细胞中的抗氧化剂和自由基捕获可降低基础蛋白磷酸化并增加磷酸酶活性。

DOI:
10.1006/abbi.1999.1178
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发表时间:
1999
期刊:
Archives of biochemistry and biophysics.
影响因子:
--
通讯作者:
Hensley,K
Hensley,K
中科院分区:
--
文献类型:
--
作者:
Robinson,KA;Stewart,CA;Pye,Q;Floyd,RA;Hensley,K

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Reversible protein phosphorylation regulates a wide array of cellular functions. 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 primary glia cell culture, we show here that the antioxidantN-acetylcysteine (NAC) and the nitrone-based free radical trap, α-phenyl-N-tert-butyl nitrone (PBN), reduce total basal protein phosphorylation in a concentration-dependent manner as assessed by phosphotyrosine analysis and by [γ-32P]ATP transfer radioassay. In addition we show that NAC inhibits H2O2-induced phosphatase inactivation in glia cell lysate. The PBN- and NAC-induced reduction in protein phosphorylation is accompanied by an increase in phosphatase activity, suggesting that PBN and NAC reduce protein phosphorylation by globally augmenting oxidant-sensitive phosphatase activities. These results partly explain why certain antioxidants also possess anti-inflammatory actions.
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