Uneven distribution of protein kinase C‐α and ‐β isozymes in human sarcomas and carcinomas

Antonio Cuadrado, Wolfgang Issing, Timothy P. Fleming, Christopher J. Molloy

Research output: Contribution to journalArticlepeer-review

7 Scopus citations

Abstract

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.

Original languageEnglish (US)
Pages (from-to)434-440
Number of pages7
JournalJournal of Cellular Physiology
Volume159
Issue number3
DOIs
StatePublished - Jun 1994
Externally publishedYes

ASJC Scopus subject areas

  • Physiology
  • Clinical Biochemistry
  • Cell Biology

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