Abstract Title:

Inhibition of ligand-induced activation of epidermal growth factor receptor tyrosine phosphorylation by curcumin.

Abstract Source:

Carcinogenesis. 1995 Aug;16(8):1741-5. PMID: 7634398

Abstract Author(s):

L Korutla, J Y Cheung, J Mendelsohn, R Kumar

Article Affiliation:

Department of Medicine, Pennsylvania State University College of Medicine, Hershey 17033, USA.

Abstract:

We explored the regulation of epidermal growth factor (EGF)-mediated activation of EGF receptor (EGF-R) phosphorylation by curcumin (diferuloyl-methane), a recently identified kinase inhibitor, in cultured NIH 3T3 cells expressing human EGF-R. Treatment of cells with a saturating concentration of EGF for 5-15 min induced increased EGF-R tyrosine phosphorylation by 4- to 11-fold and this was inhibited in a dose- and time-dependent manner by up to 90% by curcumin, which also inhibited the growth of EGF-stimulated cells. There was no effect of curcumin treatment on the amount of surface expression of labeled EGF-R and inhibition of EGF-mediated tyrosine phosphorylation of EGF-R by curcumin was mediated by a reversible mechanism. In addition, curcumin also inhibited EGF-induced, but not bradykinin-induced, calcium release. These findings demonstrate that curcumin is a potent inhibitor of a growth stimulatory pathway, the ligand-induced activation of EGF-R, and may potentially be useful in developing anti-proliferative strategies to control tumor cell growth.

Study Type : In Vitro Study

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