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J. Biol. Chem., Vol. 275, Issue 49, 38831-38841, December 8, 2000
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From the 12(S)-Hydroxyeicosatetraenoic acid
(12(S)-HETE), a 12-lipoxygenase metabolite of arachidonic
acid, has multiple effects on tumor and endothelial cells, including
stimulation of invasion and angiogenesis. However, the signaling
mechanisms controlling these physiological processes are poorly
understood. In a human epidermoid carcinoma cell line (i.e.
A431), 12(S)-HETE activates extracellular signal-regulated
kinases 1/2 (ERK1/2), which is mediated by upstream kinases MEK and
Raf. 12(S)-HETE stimulates phosphorylation of phospholipase
C
Eicosanoid Activation of Extracellular Signal-regulated
Kinase1/2 in Human Epidermoid Carcinoma Cells*
§,§,§, and§¶
Department of Radiation Oncology and the
¶ Departments of Pathology and Chemistry, Wayne State University,
Detroit and the § Karmanos Cancer Institute,
Detroit, Michigan 48202
1 and activity of protein kinase C
(PKC). In addition,
independent of PKC 12(S)-HETE increases tyrosine
phosphorylation of Shc, and Grb2, stimulates association between Shc
and Src, and increases the activity of Ras, via Src family kinases.
Furthermore, at low (10-100 nM) concentrations 12(S)-HETE counteracts epidermal growth factor-stimulated
activation of ERK1/2 via stimulating protein tyrosine phosphatases. We
also present evidence that 12(S)-HETE stimulates ERK1/2 via
G proteins and that A431 cells have multiple binding sites for
12(S)-HETE. Finally, inhibition of 12-lipoxygenase induced
apoptosis of A431 cells, which was reversed by addition of exogenous
12(S)-HETE. Collectively we demonstrate that the activation
of ERK1/2 by 12(S)-HETE may be regulated by multiple
receptors triggering PKC-dependent and PKC-independent
pathways in A431 cells.
*
This work was supported by National Institutes of Health
Grant CA 29997 (to K. V. H.).The costs of publication of this
article were defrayed in part by the
payment of page charges. The article must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
To whom correspondence should be addressed: 431 Chemistry
Bldg., Wayne State University, Detroit, MI 48202. Tel.: 313-577-1018; Fax: 313-577-0798; E-mail: k.v.honn@wayne.edu.
Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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