Adhesion is Required for Protein Kinase C-dependent Activation of the Na+/H+ Antiporter by Platelet-derived Growth Factor

Overview

Journal Proc Natl Acad Sci U S A

Specialty Science

Date 1992 Jul 1

PMID 1378621

Citations 23

Authors

M A Schwartz

C Lechene

Affiliations

Soon will be listed here.

Abstract

Adhesion of normal, anchorage-dependent cells to a solid substratum leads to activation of the Na+/H+ antiporter and elevation of intracellular pH. These effects are mediated by extracellular matrix proteins, such as fibronectin, and their receptors, the integrins. Experiments using pharmacological inhibition and down-regulation of protein kinase C (PKC) in C3H 10T1/2 cells show that platelet-derived growth factor induces activation of the Na+/H+ antiporter by means of a PKC-dependent pathway in adherent cells but cannot do so in poorly adherent cells. Poorly adherent cells are, however, able to elevate intracellular pH in response to a phorbol ester, indicating that PKC and subsequent steps in the pathway are functional. These results indicate that coupling of platelet-derived growth factor to PKC activation requires cell adhesion.

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