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Susceptibility of protein kinase C to oxidative inactivation: Loss of both phosphotransferase activity and phorbol diester binding
Author(s) -
Gopalakrishna Rayudu,
Anderson Wayne B.
Publication year - 1987
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(87)81164-x
Subject(s) - cytosol , protein kinase c , protein kinase a , biochemistry , oxidative phosphorylation , kinase , cgmp dependent protein kinase , prkcq , chemistry , phorbol , enzyme , phorbol ester , mitogen activated protein kinase kinase , biology , microbiology and biotechnology
Exposure of protein kinase C to low concentrations of either N ‐chlorosuccinimide or H 2 O 2 resulted in rapid and parallel loss of phosphotransferase activity and phorbol ester binding. This oxidative inactivation of protein kinase C also occurred in intact cells exposed to a low concentration of H 2 O 2 . With H 2 O 2 treatment the rate of inactivation of protein kinase C in the cytosol of MCF‐7 cells was rather slower than that which occurred in the cytosol of PYS cells. However, in both cell types, the oxidative inactivation of membrane‐associated protein kinase C occurred rapidly in comparison to the enzyme in the cytosol. Prior treatment of cells with phorbol ester to induce membrane association (stabilization) of protein kinase C, followed by exposure to H 2 O 2 , resulted in increased inactivation of protein kinase C, suggesting that membrane association of protein kinase C increases its susceptibility to oxidative inactivation