Abstract
The incubation of rat liver homogenates in the presence of oleate induces the translocation of protein kinase C from the cytosol to the endoplasmic reticulum membranes. The half-maximal effect was obtained at 0.3 mM oleate. The redistribution of this enzyme induced by oleate was also obtained with purified protein kinase C and hepatic microsomal membranes. This effect seems to be mediated by long-chain fatty acids since translocation was not obtained with esterified derivatives.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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1-(5-Isoquinolinesulfonyl)-2-Methylpiperazine
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Animals
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Arachidonic Acid
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Arachidonic Acids / pharmacology
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Biological Transport / drug effects
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Brain / enzymology
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Calcium / pharmacology
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Fatty Acids / pharmacology
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Intracellular Membranes / enzymology
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Isoenzymes / metabolism
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Isoquinolines / pharmacology
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Leupeptins / pharmacology
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Microsomes, Liver / enzymology*
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Oleic Acid
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Oleic Acids / pharmacology*
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Phorbol 12,13-Dibutyrate / pharmacology
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Phosphatidate Phosphatase / metabolism
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Piperazines / pharmacology
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Protein Kinase C / metabolism*
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Rats
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Spermine / pharmacology
Substances
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Arachidonic Acids
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Fatty Acids
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Isoenzymes
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Isoquinolines
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Leupeptins
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Oleic Acids
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Piperazines
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Arachidonic Acid
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Spermine
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Oleic Acid
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Phorbol 12,13-Dibutyrate
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1-(5-Isoquinolinesulfonyl)-2-Methylpiperazine
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Protein Kinase C
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Phosphatidate Phosphatase
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leupeptin
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Calcium