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Vanadate protects human neuroblastoma SH‐SY5Y cells against peroxynitrite‐induced cell death
Author(s) -
Saeki Makio,
Maeda Sadaaki,
Kamisaki Yoshinori
Publication year - 2002
Publication title -
journal of cellular biochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.028
H-Index - 165
eISSN - 1097-4644
pISSN - 0730-2312
DOI - 10.1002/jcb.10180
Subject(s) - vanadate , wortmannin , peroxynitrite , programmed cell death , protein tyrosine phosphatase , tyrosine phosphorylation , chemistry , sh sy5y , kinase , microbiology and biotechnology , biology , biochemistry , apoptosis , neuroblastoma , cell culture , phosphatidylinositol , superoxide , enzyme , genetics
We investigated the effect of vanadate, a tyrosine phosphatase inhibitor, on cell death induced by peroxynitrite in human neuroblastoma SH‐SY5Y cells. Vanadate prevented cell death induced by 3‐morpholinosydnonimine (SIN‐1), a peroxynitrite donor; whereas SIN‐1‐induced cell death was not prevented by neither okadaic acid, an inhibitor of serine/threonine phosphatases 1 and 2A, nor cyclosporin A, an inhibitor of serine/threonine phosphatase 2B. Vanadate did not prevent cell death induced by N‐ethyl‐2‐(1‐ethyl‐hydroxy‐2‐nitrosohydrazino)‐ethanamine, a nitric oxide donor. Wortmannin, an inhibitor of phosphatidylinositol 3‐kinase (PI3‐kinase), did not block the protective effect of vanadate, suggesting that the protective effect of vanadate is independent on PI3‐kinase. Vanadate increased tyrosine phosphorylation of several proteins including the focal adhesion protein p130 Crk‐associated substrate (p130 cas ). By the treatment with SIN‐1, the endogenous association of p130 cas and Crk was disrupted, and the association was restored by vanadate treatment. These results suggest that disruption of tyrosine phosphorylation signaling may be critical for peroxynitrite‐induced cell death, and that vanadate prevents cell death at least in part through the enhancement in tyrosine phosphorylation of the proteins including p130 cas . J. Cell. Biochem. 85: 721–727, 2002. © 2002 Wiley‐Liss, Inc.