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J Biol Chem, Vol. 273, Issue 6, 3747-3755, February 6, 1998

Regulation of Protein Synthesis in Ventricular Myocytes by Vasopressin
THE ROLE OF SARCOPLASMIC/ENDOPLASMIC RETICULUM Ca²⁺ STORES

From the Department of Pharmacology, Robert Wood Johnson Medical School, Piscataway, New Jersey 08854

Protein synthesis in H9c2 ventricular myocytes was subject to rapid inhibition by agents that release Ca²⁺ from the sarcoplasmic/endoplasmic reticulum, including thapsigargin, ionomycin, caffeine, and arginine vasopressin. Inhibitions were attributable to the suppression of translational initiation and were coupled to the mobilization of cell-associated Ca²⁺ and the phosphorylation of eIF2. Ionomycin and thapsigargin produced relatively stringent degrees of Ca²⁺ mobilization that produced an endoplasmic reticulum (ER) stress response. Translational recovery was associated with the induction of ER chaperones and resistance to translational inhibition by Ca²⁺-mobilizing agents. Vasopressin at physiologic concentrations mobilized 60% of cell-associated Ca²⁺ and decreased protein synthesis by 50% within 20-30 min. The inhibition of protein synthesis was exerted through an interaction at the V1 vascular receptor, was imposed at physiologic extracellular Ca²⁺ concentrations, and became refractory to hormonal washout within 10 min of treatment. Inhibition was found to attenuate after 30 min, with full recovery occurring in 2 h. Translational recovery did not involve an ER stress response but rather was derived from the partial repletion of intracellular Ca²⁺ stores. Longer exposures to vasopressin were invariably accompanied by increased rates of protein synthesis. Translational inhibition by vasopressin, but not by Ca²⁺-mobilizing drugs, was both preventable and reversible by treatment with phorbol ester, which reduced the extent of Ca²⁺ mobilization occurring in response to the hormone. Larger and more prolonged translational inhibitions occurred after down-regulation of protein kinase C. This report provides the first compelling evidence that hormonally induced mobilization of sarcoplasmic/endoplasmic reticulum Ca²⁺ stores is regulatory upon mRNA translation.

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