TY - JOUR
T1 - EGF receptor‐mediated signals are differentially modulated by concanavalin A
AU - Hazan, Rachel
AU - Krushel, Leslie
AU - Crossin, Kathryn L.
PY - 1995/1
Y1 - 1995/1
N2 - 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.
AB - 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.
UR - http://www.scopus.com/inward/record.url?scp=0028936286&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0028936286&partnerID=8YFLogxK
U2 - 10.1002/jcp.1041620110
DO - 10.1002/jcp.1041620110
M3 - Article
C2 - 7814452
AN - SCOPUS:0028936286
SN - 0021-9541
VL - 162
SP - 74
EP - 85
JO - Journal of Cellular Physiology
JF - Journal of Cellular Physiology
IS - 1
ER -