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Cell Growth & Differentiation, Vol 2, Issue 1 7-14, Copyright © 1991 by American Association of Cancer Research


ARTICLES

Protein kinase C gamma expression mimics phorbol ester-induced transcriptional activation of a murine VL30 enhancer element

DA Persons, RD Owen, MC Ostrowski and OJ Finn
Department of Microbiology and Immunology, Duke University Medical Center, Durham, North Carolina 27710.

Protein kinase C (PKC), a critical component in the regulation of cell growth, is thought to participate in transmitting the signals of certain cell surface receptor activation events to the nucleus. We have previously shown that stable expression of the PKC gamma isoenzyme in NIH 3T3 cells causes altered growth and enhanced tumorigenicity. In this report, we show that transient expression of the PKC gamma isoenzyme can trans-activate a murine VL30 enhancer element in a pattern similar to that of the phorbol ester tumor promoter 12-O-tetradecanoylphorbol-13-acetate. In contrast, ras activation of this element is distinct both quantitatively and qualitatively from PKC gamma and 12-O-tetradecanoylphorbol-13-acetate activation. These results provide direct evidence that PKC is the cellular mediator in the activation of phorbol ester-responsive genes and suggest a mechanism by which abnormal PKC expression might lead to altered growth control by changing the pattern of cellular gene expression.


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E. Mazzoni, A. Adam, E. Bal de Kier Joffe, and J. A. Aguirre-Ghiso
Immortalized Mammary Epithelial Cells Overexpressing Protein Kinase C {gamma} Acquire a Malignant Phenotype and Become Tumorigenic in Vivo
Mol. Cancer Res., August 1, 2003; 1(10): 776 - 787.
[Abstract] [Full Text] [PDF]




HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
Cancer Research Clinical Cancer Research
Cancer Epidemiology Biomarkers & Prevention Molecular Cancer Therapeutics
Molecular Cancer Research Cell Growth & Differentiation
Copyright © 1991 by the American Association of Cancer Research.