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Uneven distribution of protein kinase C‐α and ‐β isozymes in human sarcomas and carcinomas
Author(s) -
Cuadrado Antonio,
Issing Wolfgang,
Fleming Timothy P.,
Molloy Christopher J.
Publication year - 1994
Publication title -
journal of cellular physiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.529
H-Index - 174
eISSN - 1097-4652
pISSN - 0021-9541
DOI - 10.1002/jcp.1041590307
Subject(s) - protein kinase c , isozyme , biology , gene isoform , cell culture , sarcoma , cell growth , kinase , cancer research , messenger rna , microbiology and biotechnology , enzyme , gene , pathology , biochemistry , genetics , medicine
Protein kinase C (PKC) represents a family of structurally related Ser/Tre kinases which are involved in mitogenic signalling and may contribute to human neoplasia. To address this issue, the messenger RNA and protein levels of PKC isoenzymes α and β were analyzed in several human sarcoma‐ and carcinoma‐derived cell lines. Carcinomas contained low or undetectable levels of either PKC‐α or PKC‐β. Sarcomas exhibited similar or increased PKC expression compared to human diploid fibroblasts. Moreover, sarcoma cell lines expressing one PKC isoform did not contain detectable levels of the other. When PKC was depleted from the tumor cells, we observed that the PKC overexpressing sarcomas had reduced their malignant properties as determined by their ability to grow in semisolid medium. In addition, epidermal growth factor‐stimulated and erbB2‐transformed fibroblasts exhibited enhanced cell growth in the absence of PKC. We propose a model for the effect of PKC as a negative regulator of proliferation in epithelial cells and a growth promoter in fibroblasts. © 1994 wiley‐Liss, Inc.