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EGF receptor‐mediated signals are differentially modulated by concanavalin A
Author(s) -
Hazan Rachel,
Krushel Leslie,
Crossin Kathryn L.
Publication year - 1995
Publication title -
journal of cellular physiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.529
H-Index - 174
eISSN - 1097-4652
pISSN - 0021-9541
DOI - 10.1002/jcp.1041620110
Subject(s) - tyrosine phosphorylation , epidermal growth factor , phosphorylation , receptor , concanavalin a , phospholipase c , tyrosine kinase , microbiology and biotechnology , receptor tyrosine kinase , biology , inositol , signal transduction , tyrosine , inositol phosphate , biochemistry , in vitro
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.