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Evidence for autocrine activation of a tyrosine kinase in a human gastric carcinoma cell line

✍ Scribed by Silvia Giordano; Maria Flavia Di Renzo; Radha P. Narsimhan; Luca Tamagnone; Elena V. Gerbaudo; Loredana Chiadó-Piat; Paolo M. Comoglio

Publisher
John Wiley and Sons
Year
1988
Tongue
English
Weight
480 KB
Volume
38
Category
Article
ISSN
0730-2312

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✦ Synopsis

Phosphotyrosine (P-Tyr) antibodies have been used to identify the phosphorylated forms of growth factor receptors and oncogene-coded tyrosine kinases. Western blot analysis of a gastric carcinoma cell line with P-Tyr antibodies revealed a tyrosine-phosphorylated protein of M, 145,000 (P145). In addition, in vitro phosphorylation with (Y-~*P)ATP of P-Tyr immunoprecipitates of the same cells resulted in labelling of this protein on tyrosine. P145 appears to be a transmembrane glycoprotein, with features suggestive of a growth factor receptor. However, the in vivo or in vitro addition of known growth factors did not affect P145 tyrosine phosphorylation. We now report that PI45 is rapidly dephosphorylated in vivo when cells are exposed to low pH, a condition known to dissociate ligands from their receptors. The addition of serum-free medium, conditioned .by the gastric carcinoma cells, fully restores the tyrosine phosphorylation lost with acid treatment. These data suggest that the activity responsible for P145 phosphorylation on tyrosine, whether intrinsic to P145 itself or due to an associated kinase, is stimulated by a factor secreted by the tumor cells themselves.

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