MH1C1 rat hepatoma cells express the alpha isoenzyme as the only phorbol-ester sensitive isoform of protein kinase C (PKC). In this cell line, phorbol 12-myristate 13-acetate (PMA) induced a marked, dose-dependent growth inhibition. The administration of the PKC inhibitor staurosporine was able to mimic the effect of the phorbol ester on cell growth in a dose-dependent fashion, whereas the PKC activator arachidonic acid stimulated cell proliferation. Exposure of cells to an antisense oligonucleotide specific for alpha PKC caused a significant impairment of cell growth. These data suggest that the alpha PKC activity is required for proliferation of MH1C1 cells
Perletti, G., Smeraldi, C., Porro, D., Piccinini, F. (1994). Involvement Of The Alpha-Isoenzyme Of Protein-Kinase-C In The Growth-Inhibition Induced By Phorbol Esters In Mh1c1 Hepatoma-Cells. BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, 205(3), 1589-1594 [10.1006/bbrc.1994.2848].
Involvement Of The Alpha-Isoenzyme Of Protein-Kinase-C In The Growth-Inhibition Induced By Phorbol Esters In Mh1c1 Hepatoma-Cells
SMERALDI, CARLA;Porro, D;
1994
Abstract
MH1C1 rat hepatoma cells express the alpha isoenzyme as the only phorbol-ester sensitive isoform of protein kinase C (PKC). In this cell line, phorbol 12-myristate 13-acetate (PMA) induced a marked, dose-dependent growth inhibition. The administration of the PKC inhibitor staurosporine was able to mimic the effect of the phorbol ester on cell growth in a dose-dependent fashion, whereas the PKC activator arachidonic acid stimulated cell proliferation. Exposure of cells to an antisense oligonucleotide specific for alpha PKC caused a significant impairment of cell growth. These data suggest that the alpha PKC activity is required for proliferation of MH1C1 cells
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