The Influence of Starvation on Rat Liver Polysomes

Arora, D. J. S.; Lamirande, Gaston de

doi:10.1139/o71-165

Cited by 10 publications

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“…Starvation in the rat is accompanied by loss in liver weight (Schultz, 1949;Thomson et al, 1953), de-granulation of endoplasmic reticulum (Henshaw et al, 1963), fragmentation of polyribosomes (Wittman et al, 1969;Richardson et al, 1971; Arora & De Lamirande, 1971) and a decreased rate of protein biosynthesis (Wagle, 1963;Sox & Hoagland, 1966;Richardson et al, 1971). In contrast, phenobarbitone, a potent inducer of many liver microsomal enzyme systems (Conney & Burns, 1962;Gillette, 1963), increases the amount of the smooth endoplasmic reticulum (Orrenius et al, 1965) and the rate of protein synthesis in rat liver both in vivo (Kato et al, 1965a;Jick & Shuster, 1966;Glazer & Sartorelli, 1972) and in vitro (Gelboin & Sokoloff, 1961;Kato et al, 1965bKato et al, , 1966.…”

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The effect of phenobarbitone on protein synthesis by liver polyribosomes in fed and starved rats

Ragnotti

Aletti

1975

Biochemical Journal

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1. The effect of phenobarbitone on the rate of protein synthesis and on the sedimentation patterns of various liver subcellular fractions containing ribosomes was studied in rats. 2. Phenobarbitone treatment increased the incorporation of [14C]leucine into protein by all preparations, provided they had not been subjected to preliminary treatment with Sephadex G-25. The phenobarbitone-induced effect on incorporation was associated with a gain in liver weight and a higher degree of polyribosomal aggregation. 3. Preparations that were treated with Sephadex G-25 incorporated more radioactivity into protein, but did not show the response to phenobarbitone treatment. 4. When the influence of starvation and phenobarbitone was studied separately on membrane-bound and membrane-free polyribosomes, it was shown that whereas both classes of polyribosomes were affected by starvation, apparently only the former class was susceptible to phenobarbitone stimulation of protein synthesis. 5. The decreased capacity for protein synthesis of polyribosomes from starved rats was independent of their association with the membranes of the endoplasmic reticulum, but resulted from polyribosomal disaggregation, from an intrinsic defect of the polyribosomes themselves and from changes in composition of the cell sap. 6. The results are discussed in relation to the problem ofthe control ofprotein biosynthesis and of the functional separation of membrane-bound and membrane-free polyribosomes.

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