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Adhesion is Required for Protein Kinase C-Dependent Activation of the Na+/H+ Antiporter by Platelet-Derived Growth Factor
Martin Alexander Schwartz and Claude Lechene
Proceedings of the National Academy of Sciences of the United States of America
Vol. 89, No. 13 (Jul. 1, 1992), pp. 6138-6141
Published by: National Academy of Sciences
Stable URL: http://www.jstor.org/stable/2359508
Page Count: 4
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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.
Proceedings of the National Academy of Sciences of the United States of America © 1992 National Academy of Sciences