Amino Acid Incorporation into Protein by Cell-free Preparations from Rat Skeletal Muscle. II. Preparation and Properties of Muscle Ribosomes and Polyribosomes<sup>*</sup>

Breuer, Charles B.; Davies, M.C.; Florini, James R.

doi:10.1021/bi00899a020

Cited by 57 publications

(32 citation statements)

References 30 publications

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“…12 5 109.77 + 6.88c,d 3.73 + 0.11 18 8 97.77 + 4.68c,d 3.82 + 0.17 24 4 71.62 + 4. 13 3.58 + 0.21 30 3 58.08 ± 5.61…”

Section: Resultsmentioning

confidence: 98%

Age-related Changes in the Cellular Level of Amylase and Protein Synthesis in the Rat Parotid Gland

Kim

1981

J Dent Res

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Age-related changes in the cellular content of secretory proteins and protein synthesis were studied in parotid glands of rats of various ages. The secretory protein content (determined by measuring the level of alpha-amylase activity) and the synthesis of proteins (assayed by the rate of incorporation of 3H-leucine into acid-insoluble proteins) decline with increasing age. Morphological and radioautographic studies of the gland indicate that the decline in protein synthesis is due to the reduction in the ability of secretory cells to synthesize proteins.

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“…12 5 109.77 + 6.88c,d 3.73 + 0.11 18 8 97.77 + 4.68c,d 3.82 + 0.17 24 4 71.62 + 4. 13 3.58 + 0.21 30 3 58.08 ± 5.61…”

Section: Resultsmentioning

confidence: 98%

Age-related Changes in the Cellular Level of Amylase and Protein Synthesis in the Rat Parotid Gland

Kim

1981

J Dent Res

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“…The groups of 50-65 ribosomes isolated from chick muscle are much more active than single ribosomes in incorporating radioactive amino acids into protein. Two of the products have been characterized as the large and small sub-units of myosin (Heywood et al, 1967;Sarkar & Cooke, 1970; Rourke & Heywood, 1972) and ribosomal aggregates from rat muscle also synthesize protein relatively actively (Breuer et al, 1964;Wool et al, 1968;von der Decken & Omstedt, 1970).…”

Section: Polyribosomes In Musclementioning

confidence: 99%

“…However, ribonuclease releases myosin or actomyosin from muscle ribosomes (Heywood et al, 1967;Allen & Terrence, 1968) and it removes nascent catalase from liver ribosomes (Uenoyama & Ono, 1972). Admittedly, under the authors' experimental conditions, presumptive polyribosomes from skeletal muscle are stable to treatment with enzymes which catalyse the hydrolysis of protein (Breuer et al, 1964;Heywood et al, 1967;. However, such enzymes disaggregate ribosomal aggregates obtained from cardiac muscle and from cells which form collagen (Rabinowitz et aE., 1964;Fernhndez-Madrid, 1967).…”

Section: Polyribosomes In Musclementioning

confidence: 99%

On the Cellular Regulation of Growth and Development in Skeletal Muscle

Burleigh

1974

Biological Reviews

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Summary 1. Fibres of skeletal muscle in different mammalian species vary more in number and in their rates of growth than in their ultimate breadth, and they grow more slowly in cattle and man than in rats and mice. Cells of large mammalian species probably divide comparatively slowly in pre‐natal life but do so for longer, and thus they attain greater numbers than do their counterparts in smaller mammals. Such cells include the precursors of muscle, and common mechanisms may therefore limit rates of growth before and after muscles form. If some metabolic processes are slower in mammals destined to be large, corresponding trends in age‐related cellular changes which ultimately suppress mitotic activity may cause differences between species in the overall size of muscles and in that of other tissues. This is probably an oversimplification. 2. It is difficult to decide how far the rate of growth and the final diameters of muscle fibres reflect the number of myoblasts which initially fuse into myotubes and the number of myoblasts which are subsequently incorporated into individual fibres. New nuclei are probably added with age along the length of a fibre, but it is uncertain whether they then synthesize ribosomes which produce contractile protein. It seems likely that fibres elongate to different extents by adding myoblasts terminally. 3. There is some evidence that myofibrils grow throughout the depth of a fibre by adding new myofilaments to their surface, but there is none that is convincing to the effect that myofibrils form de novo at a fibre's periphery. Ribosome‐like structures distributed in the sarcoplasm between myofibrils have been described, and their numbers decline in comparison with those of the myofibrils during growth. Thus, fibres possibly attain their maximum breadth when the loss of superficial filaments from myofibrils exceeds the capacity of ribosomes to replace them. The evidence is inconclusive as to whether myofitrillar protein is broken down and replaced at rates which vary within a muscle or between muscles differing in physiological properties. Sarcoplasmic proteins appear to be replaced more rapidly than those in myofibrils. It is also speculated that muscle proteins are synthesized and degraded more slowly in species which take longer to develop. 4. Observations, with the microscope suggest that new ribosomes appear in cells which are becoming myoblasts. Whether the ribosomes subsequently break down is not established. The evidence that I‐somes occur in muscle is inconclusive, as is that for the existence of messenger RNA and its selective synthesis when muscle is forming in the embryo. 5. A decline in the synthesis of RNA occurs as myotubes appear and contractile protein begins to accumulate. The significance of this phenomenon is not known, and in more mature muscle some RNA also appears to fluctuate in a fashion which is unrelated to rates of controlling protein synthesis. Such RNA may occur at the periphery of fibres or in satellite cells. In some instances it may be formed by cells ...

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“…A simpler method for the preparation of muscle ribosomes than the one reported by Breuer, Davies & Florini (1964) was devised. The characteristics of the amino acid-incorporating activity of these ribosomes with regard to cell sap, energy and incubation times have been reported (White, 1967).…”

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confidence: 99%

The effects of catabolic and anabolic steroids on amino acid incorporation by skeletal-muscle ribosomes

Bullock¹,

White²,

Worthington³

1968

Biochemical Journal

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1. A method is described for the routine isolation of ribosomes from small quantities of skeletal muscle that have been homogenized with the Ultra-Turrax tissue disintegrator. 2. Ribosomes prepared by this method from rats receiving triamcinolone acetonide or rabbits receiving cortisone acetate show a marked fall in their ability to incorporate amino acids when compared with ribosomes from control animals. 3. This fall in activity can be partially prevented in rats by pretreating the animals with an anabolic steroid, steroid 36644-Ba. 4. Testosterone (5mg./kg.) administered to rabbits in conjunction with cortisone acetate is not effective in maintaining ribosomal activity. However, steroid 36644-Ba at onetenth of an equiandrogenic dose (0-05mg./kg.) is extremely effective. 5. The results with ribosomes isolated from rabbits support the concept that steroid 36644-Ba and possibly all anabolic steroids have an ability to counteract the catabolic action of corticosteroids that is greater than their androgenic activity would suggest.It has been known for some years that androgens (anabolic steroids) are clinically useful for counteracting and controlling the undesirable effects of chronic corticosteroid therapy. The subject has been reviewed by Reifenstein (1956 WVhite (1967) that the amino acid-incorporating ability of ribosomes (called in the present paper P ribosomes) isolated from the psoas muscle of rats fell after Al-9oc-fluorohydrocortisone 16ac,17c-acetonide (triamcinolone acetonide) had been given in vivo, and that pretreatment of the animals with the anabolic compound 17fl-hydroxy-170c-methylandrosta-1,4-dien-3-one (methandionone or methandrostenolone) enabled full ribosomal activity to be retained. In the present paper these results have been extended by the examination of another anabolic steroid (steroid 36644-Ba) composed of 14 17, -hydroxy -7oc,17c -dimethyl -A -nor -B homooestrane-3,6-dione (I) in equilibrium with its enol form (II).One of the most important questions in the clinical use of anabolic steroids is whether their ability to antagonize the catabolic effects of glucocorticoids is due solely to their androgenicity. On the basis of the levator ani assay (Hershberger, Shipley & Meyer, 1953), which uses the castrated male rat, steroid 36644-Ba, administered subcutaneously, was 150-500 times more efficient than methyltestosterone in restoring the weight of the levator ani muscle to normal, but only 2-5-10 times more potent than methyltestosterone in restoring the weight of the seminal vesicles and ventral prostate (Desaulles & Schar, 1967). Thus the compound can be said to have an anabolic to androgenic ratio between 15 and 200.To see whether steroid 36644-Ba has an anticatabolic to androgenic ratio in a similar range, experiments were carried out with ribosomes from rabbits that had been pretreated with cortisone acetate. A regimen for drug administration was used (Little, 1966) in which cortisone acetate was administered to rabbits for 2 weeks followed by a 2-week period in which the animals...

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Amino Acid Incorporation into Protein by Cell-free Preparations from Rat Skeletal Muscle. II. Preparation and Properties of Muscle Ribosomes and Polyribosomes^*

Cited by 57 publications

References 30 publications

Age-related Changes in the Cellular Level of Amylase and Protein Synthesis in the Rat Parotid Gland

Age-related Changes in the Cellular Level of Amylase and Protein Synthesis in the Rat Parotid Gland

On the Cellular Regulation of Growth and Development in Skeletal Muscle

The effects of catabolic and anabolic steroids on amino acid incorporation by skeletal-muscle ribosomes

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Amino Acid Incorporation into Protein by Cell-free Preparations from Rat Skeletal Muscle. II. Preparation and Properties of Muscle Ribosomes and Polyribosomes*

Cited by 57 publications

References 30 publications

Age-related Changes in the Cellular Level of Amylase and Protein Synthesis in the Rat Parotid Gland

Age-related Changes in the Cellular Level of Amylase and Protein Synthesis in the Rat Parotid Gland

On the Cellular Regulation of Growth and Development in Skeletal Muscle

The effects of catabolic and anabolic steroids on amino acid incorporation by skeletal-muscle ribosomes

Contact Info

Product

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Amino Acid Incorporation into Protein by Cell-free Preparations from Rat Skeletal Muscle. II. Preparation and Properties of Muscle Ribosomes and Polyribosomes^*