Abstract
Stimulation of CHO cells with phorbol ester caused transient activation of mitogen-activated protein kinase (MAP-kinases with 42 and 44 kDa). A similar treatment of CHO cells which overexpress a massive amount of the alpha- or delta-isoform of protein kinase C (PKC) resulted in the prolonged activation of MAP-kinase and eventually in the appearance of mostly dikaryotic, sometimes tetrakaryotic cells. The results suggest that the delta-isoform, as well as the alpha-isoform, has a potential to cause MAP kinase activation. Unusual activation of the PKC/MAP-kinase pathway, however, may lead to abnormal cytokinesis.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Sequence
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Animals
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Binding Sites
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CHO Cells
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Calcium-Calmodulin-Dependent Protein Kinases / isolation & purification
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Calcium-Calmodulin-Dependent Protein Kinases / metabolism*
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Cell Division / drug effects
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Chromatography
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Chromatography, Gel
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Chromatography, Ion Exchange
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Cricetinae
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Cytosol / enzymology
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Durapatite
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Enzyme Activation
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Immunoblotting
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Isoenzymes / biosynthesis
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Isoenzymes / isolation & purification
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Isoenzymes / metabolism*
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Kinetics
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Molecular Sequence Data
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Phorbol 12,13-Dibutyrate / metabolism
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Phosphotyrosine
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Protein Kinase C / biosynthesis
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Protein Kinase C / isolation & purification
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Protein Kinase C / metabolism*
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Tetradecanoylphorbol Acetate / pharmacology*
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Tyrosine / analogs & derivatives
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Tyrosine / analysis
Substances
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Isoenzymes
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Phosphotyrosine
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Phorbol 12,13-Dibutyrate
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Tyrosine
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Durapatite
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Protein Kinase C
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Calcium-Calmodulin-Dependent Protein Kinases
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Tetradecanoylphorbol Acetate