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J. Biol. Chem., Vol. 267, Issue 33, 23443-23446, Nov, 1992
RA Mooney, GG Freund, BA Way and KL Bordwell
Tyrosine phosphorylation is a mechanism of signal transduction shared by
many growth factor receptors and oncogene products. Phosphotyrosine
phosphatases (PTPases) potentially modulate or counter-regulate these
signaling pathways. To test this hypothesis, the transmembrane PTPase CD45
(leukocyte common antigen) was expressed in the murine cell line C127.
Hormone-dependent autophosphorylation of the platelet-derived growth factor
(PDGF) and insulin-like growth factor-1 (IGF-1) receptors was markedly
reduced in cells expressing the transmembrane PTPase. Tyrosine
phosphorylation of other PDGF-dependent phosphoproteins (160, 140, and 55
kDa) and IGF-1-dependent phosphoproteins (145 kDa) was similarly decreased.
Interestingly, the pattern of growth factor- independent tyrosine
phosphorylations was comparable in cells expressing the PTPase and control
cells. This suggests a selectivity or accessibility of the PTPase limited
to a subset of cellular phosphotyrosyl proteins. The maximum mitogenic
response to PDGF and IGF- 1 in cells expressing the PTPase was decreased by
67 and 71%, respectively. These results demonstrate that a transmembrane
PTPase can both affect the tyrosine phosphorylation state of growth factor
receptors and modulate proximal and distal cellular responses to the growth
factors.
Expression of a transmembrane phosphotyrosine phosphatase inhibits cellular response to platelet-derived growth factor and insulin-like growth factor-1
Department of Pathology and Laboratory Medicine, University of Rochester School of Medicine and Dentistry, New York 14642.
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