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Science 4 May 1990:
Vol. 248. no. 4955, pp. 607 - 610
DOI: 10.1126/science.2333512
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Articles

Science, Vol 248, Issue 4955, 607-610
Copyright © 1990 by American Association for the Advancement of Science

articles

Effect of phospholipase C-gamma overexpression on PDGF-induced second messengers and mitogenesis

B Margolis, A Zilberstein, C Franks, S Felder, S Kremer, A Ullrich, SG Rhee, K Skorecki, and J Schlessinger

Rorer Biotechnology, King of Prussia, PA 19406.

Platelet-derived growth factor (PDGF) stimulates phospholipase C (PLC) activity and the phosphorylation of the gamma isozyme of PLC (PLC-gamma) in vitro and in living cells. The role of PLC-gamma in the phosphoinositide signaling pathway was addressed by examining the effect of overexpression of PLC-gamma on cellular responses to PDGF. Overexpression of PLC-gamma correlated with PDGF-induced tyrosine phosphorylation of PLC-gamma and with PDGF-induced breakdown of phosphatidylinositol 4,5-bisphosphate (PIP2). However, neither bradykinin- nor lysophosphatidic acid-induced phosphoinositide metabolism was enhanced in the transfected cells, suggesting that the G protein-coupled phosphoinositide responses to these ligands are mediated by other PLC isozymes. The enhanced PDGF-induced generation of inositol trisphosphate (IP3) did not enhance intracellular calcium signaling or influence PDGF-induced DNA synthesis. Thus, enzymes other than PLC-gamma may limit PDGF-induced calcium signaling and DNA synthesis. Alternatively, PDGF-induced calcium signaling and DNA synthesis may use biochemical pathways other than phosphoinositide metabolism for signal transduction.


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