Calcium-dependent Inhibition of Protein Synthesis in Rat Parotid Gland

Overview

Journal Biochem J

Specialty Biochemistry

Date 1978 Oct 15

PMID 215129

Citations 5

Authors

P Kanagasuntheram

S C Lim

Affiliations

Soon will be listed here.

Abstract

1. Protein synthesis in the rat parotid gland in vitro was studied by measuring the incorporation of [3H]phenylalanine into trichloroacetic acid-insoluble proteins. In the unstimulated gland, the rate of incorporation was dependent on the phenylalanine concentration in the medium and proceeded linearly for up to 3h. 2. Adrenaline, carbamoylcholine, phenylephrine and ionophore A23187 inhibited the incorporation of [3H]phenylalanine into acid-insoluble protein; isoprenaline, dibutyryl cyclic AMP and 8-bromo-cyclic GMP were inactive. 3. Inhibition by adrenaline and carbamoylcholine but not by ionophore A23187 required extracellular Ca2+. 4. Both adrenaline and carbamoylcholine increased the magnitude of the acid-soluble [3H]phenylalanine pool at 10 micrometer extracellular phenylalanine, but had no effect if the phenylalanine concentration was increased to 200 micrometer. 5. There was no correlation between cellular ATP content and the observed inhibition of protein synthesis. 6. Our results suggest that both alpha-adrenergic and cholinergic receptors may play a role in the regulation of protein synthesis in the rat parotid gland, and that their effects are mediated by a rise in intracellular free Ca2+.

Citing Articles

Cholinergic regulation of amylase gene expression in the rat parotid gland. Inhibition by two distinct post-transcriptional mechanisms.

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The effects of calcium on protein turnover in skeletal muscles of the rat.

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A Ca2+-linked increase in coupled cAMP synthesis and hydrolysis is an early event in cholinergic and beta-adrenergic stimulation of parotid secretion.

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Mechanism of action of extracellular calcium on isoprenaline-evoked amylase secretion from isolated rat parotid glands.

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Phosphorylation of elongation factor 2 during Ca(2+)-mediated secretion from rat parotid acini.

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