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Oxidative stress-induced apoptosis is mediated by ERK1/2 phosphorylation

Title
Oxidative stress-induced apoptosis is mediated by ERK1/2 phosphorylation
Authors
Lee Y.-J.Cho H.-N.Soh J.-W.Jhon G.J.Cho C.-K.Chung H.-Y.Bae S.Lee S.-J.Lee Y.-S.
Ewha Authors
전길자
SCOPUS Author ID
전길자scopus
Issue Date
2003
Journal Title
Experimental Cell Research
ISSN
0014-4827JCR Link
Citation
vol. 291, no. 1, pp. 251 - 266
Indexed
SCI; SCIE; SCOPUS WOS scopus
Abstract
Oxidative stress is known to induce apoptosis in a wide variety of cell types, apparently by modulating intracellular signaling pathways. High concentrations of H2O2 have been found to induce apoptosis in L929 mouse fibroblast cells. To elucidate the mechanisms of H 2O2-mediated apoptosis, ERK1/2, p38-MAPK, and JNK1/2 phosphorylation was examined, and ERK1/2 and JNK1/2 were found to be activated by H2O2. Inhibition of ERK1/2 activation by treatment of L929 cells with PD98059 or dominant-negative ERK2 transfection blocked H 2O2-induced apoptosis, while inhibition of JNK1/2 by dominant-negative JNK1 or JNK2 or MKK4 or MKK7 transfection did not affect H2O2-mediated apoptosis. H2O 2-mediated ERK1/2 activation was not only Ras-Raf dependent, but also both tyrosine kinase (PDGFβ receptor and Src) and PKCδ dependent. H2O2-mediated PKCδ-dependent and tyrosine kinase-dependent ERK1/2 activations were independent from each other. Based on the above results, we suggest for the first time that oxidative damage-induced apoptosis is mediated by ERK1/2 phosphorylation which is not only Ras-Raf dependent, but also both tyrosine kinase and PKCδ dependent. © 2003 Elsevier Inc. All rights reserved.
DOI
10.1016/S0014-4827(03)00391-4
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자연과학대학 > 화학·나노과학전공 > Journal papers
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