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Volume 271, Number 22, Issue of May 31, 1996 pp. 13008-13012
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.

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Differential Translocation of Protein Kinase C during HeLa Cell Adhesion to a Gelatin Substratum

(Received for publication, March 12, 1996)

Jang-Soo Chun , Mahn-Joon Ha ^§ and Bruce S. Jacobson ^¶

From the  Department of Biology, Kyungpook National University, Taegu 702-701, Korea, the ^§ Laboratory of Medical Genetics, Institute for Medical Science, Ajou University, Suwon 441-749, Korea, and the ^¶ Department of Biochemistry and Molecular Biology, University of Massachusetts, Amherst, Massachusetts 01003

The spreading of HeLa cells, following attachment to a collagen or gelatin substratum, requires the activation of protein kinase C (PKC). Membrane-bound PKC was previously shown to be activated during cell attachment and in response to the activation of a series of lipid second messengers turned on by the ligation of 1-integrin collagen receptors. HeLa cells express the , , , , , and isozymes of PKC as determined by Western blotting with specific antibodies. Only PKC redistributed from the cytosol to the membrane during cell adhesion. Most of the PKC in cells that were in suspension was in the cytosolic fraction. During cell attachment to a gelatin matrix, all of the PKC moved out of the cytosol, with most going to the membrane fraction. After the cells became fully spread, PKC began to reappear in the cytosol. Translocation of PKC was not observed during the adhesion of cells to culture dishes where cells nonspecifically attach but do not spread. The conventional PKC and - isozymes were translocated from the cytosol to the membrane only when phorbol ester was present at a concentration that increases the rate and extent of cell spreading. Under normal conditions, i.e. in the absence of phorbol ester, PKC appears to be the PKC isozyme responsible for the regulation of HeLa cell adhesion to the extracellular matrix.

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