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Oxidative stress oppositely modulates protein tyrosine phosphorylation stimulated by muscarinic G protein–coupled and epidermal growth factor receptors by Richard S. Jope; Ling Song; Carol A. Grimes; Liang Zhang is a Neuroscience article available to read on EtoBox.

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This study's goals were to more fully define the activation of protein tyrosine phosphorylation stimulated by muscarinic receptors, to test if this signaling process is affected by oxidative stress induced by H 2 O 2 , and to compare the effects of H 2 O 2 on protein tyrosine phosphorylation activated by epidermal growth factor (EGF) receptors. Experiments used human neuroblastoma SH-SY5Y cells which express endogenous M3 muscarinic and EGF receptors. Carbachol induced time-dependent increases in phosphotyrosine immunoreactivity of several protein bands, which were quantitated, and immunoprecipitation was used to identify the adhesion-related proteins focal adhesion kinase, p130Cas/HEF1, and paxillin, and three shc adapter proteins. Carbachol-induced tyrosine phosphorylation of the adhesion-related proteins was mediated by muscarinic receptors, and was inhibited by a src family kinase inhibitor, PP1. That carbachol can activate src family kinases was indicated further by the finding that carbachol induced an increase in tyrosine phosphorylation of p120-src substrate, which was inhibited by PP1. Oxidative stress induced by H 2 O 2 concentration dependently inhibited carbachol-induce

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Author

Richard S. Jope; Ling Song; Carol A. Grimes; Liang Zhang

Publisher

John Wiley and Sons; Wiley (John Wiley & Sons); John Wiley & Sons Inc.; Wiley (ISSN 0360-4012)

Published

1999

Language

EN

Field

Neuroscience (Life Sciences)