Metabolic responsiveness to phorbol ester and activity of protein kinase C in isolated hepatocytes from partially hepatectomized rats |
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Authors: | M Houweling W J Vaartjes L M van Golde |
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Affiliation: | Laboratory of Veterinary Biochemistry, State University of Utrecht, The Netherlands. |
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Abstract: | The ability of isolated rat hepatocytes to respond to phorbol-12-myristate-13-acetate (PMA) with acute stimulation of de novo fatty acid synthesis was markedly depressed at 4, 22 and 48 h after partial hepatectomy (PH). This desensitization was not due to surgical stress as shown by comparison with hepatocytes from sham-operated animals. Moreover, the total activity of protein kinase C (PK-C), the principal phorbol ester receptor, was not down-regulated at 22 h after partial hepatectomy. Partial hepatectomy rather caused a small but distinct shift in subcellular PK-C distribution toward the particulate fraction thereby suggesting a modest activation of PK-C. We conclude that the PH-induced desensitization to PMA occurs at a point beyond PK-C activation. |
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