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Nitric oxide stimulates stress‐activated protein kinases in glomerular endothelial and mesangial cells
Author(s) -
Pfeilschifter Josef,
Huwiler Andrea
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)01070-8
Subject(s) - mesangial cell , nitric oxide , chemistry , kinase , phosphorylation , microbiology and biotechnology , genistein , medicine , protein kinase a , apoptosis , endocrinology , biology , biochemistry , in vitro
Exposure of rat glomerular mesangial cells and primary cultures of bovine glomerular endothelial cells to compounds releasing nitric oxide (NO), including MAHMANONOate, S ‐nitrosoglutathione, and spermine‐NO, results in a time‐ and concentration‐dependent activation of stress‐activated protein kinases (SAPK) as measured by the phosphorylation of c‐Jun in a solid phase kinase assay. Dibutyryl cGMP had no effect on SAPK activity. Pretreatment of the cells with the tyrosine kinase inhibitor genistein strongly attenuated NO‐induced c‐Jun phosphorylation. Furthermore, N ‐acetylcysteine markedly reduced the activation of SAPK in response to NO. These studies identify SAPK as a target for NO which may be critical for the NO‐induced apoptosis of glomerular mesangial and endothelial cells.

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