Initiation Factors in Protein Synthesis of Liver and Skeletal Muscle of Rats Force-Fed a Threonine-Devoid Diet

Murty, Challakonda N.; Verney, Ethel; Sidransky, Herschel

doi:10.3181/00379727-145-37751

Cited by 7 publications

(3 citation statements)

References 8 publications

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“…Subsequently, a number of investigators have reported that the active components of the ribosomal wash in liver are protein factors that are required for the initiation of mRNA translation in eukaryotes (Grummt & Bielka, 1971;Murty et al, 1971;Lynn etal., 1973;Picciano etal., 1973;Schreier & Staehelin, 1973). In a number of reports (Lynn et al, 1973;Lanclos & Bresnick, 1972;Murty et al, 1974a), alterations in the hepatic activity of initiation factors have been observed under certain experimental conditions. Also, the activity of initiation factors of transplantable hepatoma H5123 appeared to be different from that of host liver (Murty et al, 1974b).…”

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Initiation factors in protein synthesis by free and membrane-bound polyribosomes of liver and hepatoma

Murty

Verney

Sidransky

1975

Biochemical Journal

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The activity of initiation factors obtained from free and membrane-bound polyribosomes of liver and of transplantable H5123 hepatoma of rats was investigated by using an assay of protein synthesis in vitro in which poly(U)-directed polyphenylalanine synthesis was measured. Initiation factors of membrane-bound polyribosomes prepared by using the anionic detergent deoxycholate exhibited less activity in incorporating [14C]phenylalanyltRNA into polypeptides than did initiation factors of free polyribosomes. However, when membrane-bound polyribosomes were prepared after using the non-ionic detergent Triton X-100, no significant differences in activities in polyphenylalanine synthesis were observed between the initiation factors of free and membrane-bound polyribosomes. These results suggest that Triton X-100 is preferable to deoxycholate in the isolation of initiation factors from polyribosomes. Initiation factors, prepared by using Triton X-100, of free polyribosomes of hepatoma exhibited greater activity in the stimulation of polyphenylalanine synthesis than did the initiation factors of free or membrane-bound polyribosomes of host livers or of membrane-bound polyribosomes of hepatomas.

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Initiation factors in protein synthesis by free and membrane-bound polyribosomes of liver and hepatoma

Murty

Verney

Sidransky

1975

Biochemical Journal

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“…There is also evidence which shows that the initiation factors associated with ribosome preparations may in part regulate protein synthesis (9,15). Furthermore, under several experimental conditions, the alterations in the rate of protein synthesis have been related to changes in the activity of initiation factors (11,14,20). We have now observed that in well-fed adrenalectomized rats administration of tryptophan enhances the capacity of initiation factors to support protein synthesis.…”

Section: Discussionmentioning

confidence: 99%

“…There is now evidence which shows that the activities of soluble com ponents of protein synthesis in the cytosol-as well as ribosome-associated initia tion factors are greatly influenced by altered nutritional conditions (1,11). The present experiment was, therefore, designed to study the changes in the activity of hepatic soluble and initiation factors in the well-fed adrenalectomized rats following a single tube-feeding of tryptophan.…”

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Bilateral Adrenalectomy: Factors Affecting Hepatic Protein Synthesis following a Single Tube-Feeding of Tryptophan

Nakhla¹

1978

Ann Nutr Metab

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Effect of tryptophan force-feeding to well-fed adrenalectomized rats on the ability of liver cell sap and initiation factors to support protein synthesis in vitro was investigated. 5 h after tryptophan force-feeding, the capacity of liver cell sap, pH 5 enzyme and pH 5 supernatant to support protein synthesis was greatly increased. The capacity of cell sap to support charging of tRNA with either (¹⁴C)-leucine or (¹⁴C)-phenylalanine was increased following a dose of tryptophan. Initiation factors prepared from tryptophan-fed adrenalectomized rats stimulated polyuridylic-acid-directed polyphenylalanine synthesis to a greater extent than those from livers of water-fed adrenalectomized controls.

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Altered Protein Synthesis

Sidransky

1977

Comprehensive Physiology

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The sections in this article are: Inhibition of Protein Synthesis Puromycin Ethionine Sparsomycin Hypertonicity of Portal Blood Enhancement of Protein Synthesis Alterations or Imbalances in Nutrition Hormones, Toxins, Physical Agents, Chemicals Altered Metabolic States Induced Synthesis of Specific Proteins Correlation Between Structural and Functional Changes Discussion

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Initiation Factors in Protein Synthesis of Liver and Skeletal Muscle of Rats Force-Fed a Threonine-Devoid Diet

Cited by 7 publications

References 8 publications

Initiation factors in protein synthesis by free and membrane-bound polyribosomes of liver and hepatoma

Initiation factors in protein synthesis by free and membrane-bound polyribosomes of liver and hepatoma

Bilateral Adrenalectomy: Factors Affecting Hepatic Protein Synthesis following a Single Tube-Feeding of Tryptophan

Altered Protein Synthesis

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