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Regulation of protein synthesis in isolated hepatocytes by calcium- mobilizing hormones

CO Brostrom, SB Bocckino, MA Brostrom and EM Galuska

The incorporation of leucine into protein was studied in Ca2+-depleted and Ca2+-restored preparations of normal liver cells isolated from fed, adult male rats. Ca2+-restored cells incorporated amino acid 5-10-fold more rapidly than did Ca2+-depleted cells for incubation periods up to 1 hr. Readdition of Ca2+ at supraphysiologic concentrations (3 mM) to depleted cells restored the rate of incorporation within 8-10 min, whereas lesser concentrations of the cation acted more slowly. Vasopressin and alpha-adrenergic agonists rapidly (in minutes) inhibited amino acid incorporation to variable degrees in liver cells, with pronounced inhibitions (40-75%) occurring at moderate (0.1-1 mM) extracellular Ca2+ concentrations and smaller inhibitions (10-30%) occurring at supraphysiologic concentrations of the cation. Hormonally produced inhibitions were more intense at acid pH than at alkaline pH. The effects of epinephrine were mediated through alpha 1-adrenergic receptors and were not additive with those of vasopressin at saturating concentrations. It is proposed that these hormones, which are known to mobilize sequestered Ca2+ within liver cells, inhibit amino acid incorporation by influencing a Ca2+ requirement associated with protein synthesis.

Volume 29, Issue 1, pp. 104-111, 01/01/1986
Copyright © 1986 by American Society for Pharmacology and Experimental Therapeutics




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B. A. Reilly, M. A. Brostrom, and C. O. Brostrom
Regulation of Protein Synthesis in Ventricular Myocytes by Vasopressin. THE ROLE OF SARCOPLASMIC/ENDOPLASMIC RETICULUM Ca2+ STORES
J. Biol. Chem., February 6, 1998; 273(6): 3747 - 3755.
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