EGF receptor‐mediated signals are differentially modulated by concanavalin A

Rachel Hazan, Leslie Krushel, Kathryn L. Crossin

Research output: Contribution to journalArticle

22 Scopus citations

Abstract

NIH 3T3 cells expressing hgh levels of the human epidermal growth factor (EGF) receptor were used to examine the effects of the lectin concanavalin A (Con A) on EGF‐mediated signaling events. Proliferation of NIH 3T3 cells expressing high levels of the human EGF receptor was inhibited in a dose‐dependent manner by Con A. At the same time, Con A also inhibited both dimerization and tyrosine phosphorylation of the EGF receptor. Tyrosine phosphorylation of the enzyme phospholiphase C‐γ, a substrate of the phosphorylated EGF receptor kinase, was also inhibited. In contrast, EGF‐stimulated changes in pH, calcium, and levels of inositol phosphates were unaffected by the presence of Con A. These results indicate that certain signals (changes in the levels of intracellular calcium, pH, and inositol phosphates) mediated by EGF binding to its receptor still occur when receptor dimerization and phosphorylation are dramatically decreased, suggesting that multiple independent signals are transmitted by the binding of EGF to its receptor. © 1995 Wiley‐Liss, Inc.

Original languageEnglish (US)
Pages (from-to)74-85
Number of pages12
JournalJournal of Cellular Physiology
Volume162
Issue number1
DOIs
StatePublished - Jan 1995
Externally publishedYes

ASJC Scopus subject areas

  • Physiology
  • Clinical Biochemistry
  • Cell Biology

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