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Extracellular alkalosis activates ERK mitogen‐activated protein kinase of vascular smooth muscle cells through NADPH‐mediated formation of reactive oxygen species
Author(s) -
Susa Shinji,
Wakabayashi Ichiro
Publication year - 2003
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/s0014-5793(03)01198-0
Subject(s) - extracellular , mapk/erk pathway , nadph oxidase , chemistry , phosphorylation , microbiology and biotechnology , reactive oxygen species , kinase , biochemistry , protein kinase a , biology
Extracellular alkalosis induced phosphorylation of extracellular signal‐regulated kinase (ERK) and enhanced serum‐induced ERK phosphorylation in cultured rat aortic smooth muscle cells. While extracellular alkalinization increased verapamil‐sensitive 45 Ca 2+ uptake into the cells, ERK phosphorylation induced by extracellular alkalosis was not affected by verapamil. On the other hand, probes for oxidant signaling, such as superoxide dismutase, 4,5‐dihydroxy‐1,3‐benzene‐disulfonic acid, a cell‐permeable antioxidant, and diphenyliodonium, a NADPH oxidase inhibitor, inhibited extracellular alkalosis‐induced phosphorylation of ERK. These results suggest that activation of ERK induced by extracellular alkalosis is not dependent on transplasmalemmal Ca 2+ entry but is caused by reactive oxygen species derived from an activation of NADPH oxidase.