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Science 2 March 1990:
Vol. 247. no. 4946, pp. 1074 - 1077
DOI: 10.1126/science.2408147
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Articles

Science, Vol 247, Issue 4946, 1074-1077
Copyright © 1990 by American Association for the Advancement of Science

articles

Inhibition of serum- and ras-stimulated DNA synthesis by antibodies to phospholipase C

MR Smith, YL Liu, H Kim, SG Rhee, and HF Kung

Biological Carcinogenesis and Development Program, National Cancer Institute-Frederick Cancer Research Facility, MD 21701.

Several immunologically distinct isozymes of inositol phospholipid-specific phospholipase C (PLC) have been purified from bovine brain. Murine NIH 3T3 fibroblasts were found to express PLC-gamma, but the expression of PLC-beta was barely detectable by radioimmunoassay or protein immunoblot. A mixture of monoclonal antibodies was identified that neutralizes the biological activity of both endogenous and injected purified PLC-gamma. When co-injected with oncogenic Ras protein or PLC-gamma, this mixture of antibodies inhibited the induction of DNA synthesis that characteristically results from the injection of these proteins into quiescent 3T3 cells. However, when oncogenic Ras protein or PLC-gamma was co-injected with a neutralizing monoclonal antibody to Ras, only the DNA synthesis induced by the Ras protein was inhibited--that induced by PLC was unaffected. These results suggest that the Ras protein is an upstream effector of PLC activity in phosphoinositide-specific signal transduction and that PLC-gamma activity is necessary for Ras-mediated induction of DNA synthesis.


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