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The phosphorylation state of MAP‐kinases modulates the cytotoxic response of smooth muscle cells to hydrogen peroxide
Author(s) -
Cantoni Orazio,
Boscoboinik Daniel,
Fiorani Mara,
Stäuble Barbara,
Azzi Angelo
Publication year - 1996
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(96)00605-9
Subject(s) - phosphorylation , kinase , mitogen activated protein kinase , protein kinase c , chemistry , microbiology and biotechnology , hydrogen peroxide , biochemistry , biology
Micromolar concentrations of hydrogen peroxide induced the phosphorylation of mitogen‐activated protein (MAP) kinases and a lethal response in growth‐arrested smooth muscle cells (A7r5). The H 2 O 2 ‐induced phosphorylation of MAP‐kinases was markedly lower in the presence of protein tyrosine kinase (PTK) inhibitors or in protein kinase C (PKC) down‐regulated cells. Similarly, the toxicity of H 2 O 2 was diminished by concomitant addition of either PKC or PTK inhibitors and was also lower in PKC down‐regulated cells. These results are consistent with the possibility that phosphorylation of MAP‐kinases is a critical event in the toxic response of cultured smooth muscle cells to H 2 O 2 .