Protein Synthesis in the Myocardiopathy and Muscular Dystrophy of the Syrian Hamster

Lochner, Amanda; Brink, A. L.; Brink, A J

doi:10.1042/cs0400089

Cited by 9 publications

(7 citation statements)

References 11 publications

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“…4). These results for soluble protein resemble those for soluble protein and for actomyosin after a short incubation of whole-cell preparations from diaphragm (Lochner et al, 1971) and for total protein of diaphragm (Goldspink & Goldspink, 1977). The labelling pattem of the microsomal protein of the diaphragm resembled that of the soluble protein, except that the labelling was higher than for the soluble protein.…”

Section: Determination Ofprotein and Radioactivitysupporting

confidence: 57%

“…However, certain substances 'such as Ca2 +Mg2+dependent ATPase, calsequestrin and guanylate cyclase do not appear to be changed (Yap & MacLennan, 1976;Blosser & Appel, 1978). Whole cell preparations of dystrophic hamster hindleg muscle, incubated in vitro with labelled amino acids, exhibited an increased labelling of soluble proteins and of actomyosin at both 60 days and 180-240 days of age; similar changes in the heart and diaphragm occurred in the older age group (Lochner et al, 1971). In addition, the total proteins of the hypertrophied diaphragm of dystrophic hamsters, incubated in vitro, exhibited an increase in synthesis and a smaller increase in degradation (Goldspink & Goldspink, 1977).…”

mentioning

confidence: 91%

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Incorporation of amino acids into soluble and membrane protein fractions of dystrophic hamsters

Nicholls¹,

Creasy²,

Chin-See³

et al. 1980

Biochemical Journal

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The incorporation of labelled leucine was measured in protein fractions of muscle in intact control and dystrophic female hamsters and also in cell-free preparations obtained from these animals. The labelling of the soluble sarcoplasmic protein fraction, the microsomal protein fraction and the sarcolemma protein fraction was increased in the dystrophic hindleg muscle. The specific radioactivities of the sarcolemma protein fraction and other fractions were increased markedly relative to that of free leucine in the dystrophic muscle. In cell-free preparations where ribonuclease effects were avoided, the dystrophic muscle exhibited an increased synthesis of peptide bonds.

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Section: Determination Ofprotein and Radioactivitysupporting

confidence: 57%

mentioning

confidence: 91%

Incorporation of amino acids into soluble and membrane protein fractions of dystrophic hamsters

Nicholls¹,

Creasy²,

Chin-See³

et al. 1980

Biochemical Journal

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“…Specifically, since 1963 more than 79,000 articles have been published (PubMed Database) with use of or reference to the hamster. The hamster has been utilized to investigate pathological dysfunction stemming from diabetes mellitus (Sims and Landau 1967), hypoglycemia (Sodoyez et al 1969), muscular dystrophy (Lochner et al 1971), cardiomyopathy (Schwartz et al 1972), hypothermia (Resch and Musacchia 1976), emphysema (Karlinsky and Snider 1978), skeletal muscle transplantation (Faulkner et al 1983), age (Nichols and Borer 1987), chronic wasting infection (Drew et al 1988), skeletal muscle ischemia/reperfusion (Messina 1990), inactivity (Zhan and Sieck 1992), and gene therapy (Xiao et al 2000). Moreover, the hamster has been used to explore the physiological function of the myocardium (Aomine et al 1982), vasculature (Burns and Palade 1968), and skeletal muscle (Lossnitzer and Kelly 1968).…”

mentioning

confidence: 99%

Fiber Composition and Oxidative Capacity of Hamster Skeletal Muscle

Mattson

Miller

Poole

et al. 2002

J Histochem Cytochem.

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Kansas (DCP)S U M M A R Y The hamster is a valuable biological model for physiological investigation. Despite the obvious importance of the integration of cardiorespiratory and muscular system function, little information is available regarding hamster muscle fiber type and oxidative capacity, both of which are key determinants of muscle function. The purpose of this investigation was to measure immunohistochemically the relative composition and size of muscle fibers composed of types I, IIA, IIX, and IIB fibers in hamster skeletal muscle. The oxidative capacity of each muscle was also assessed by measuring citrate synthase activity. Twenty-eight hindlimb, respiratory, and facial muscles or muscle parts from adult (144-147 g bw) male Syrian golden hamsters ( n ϭ 3) were dissected bilaterally, weighed, and frozen for immunohistochemical and biochemical analysis. Combining data from all 28 muscles analyzed, type I fibers made up 5% of the muscle mass, type IIA fibers 16%, type IIX fibers 39%, and type IIB fibers 40%. Mean fiber cross-sectional area across muscles was 1665 Ϯ 328 m 2 for type I fibers, 1900 Ϯ 417 m 2 for type IIA fibers, 3230 Ϯ 784 m 2 for type IIX fibers, and 4171 Ϯ 864 m 2 for type IIB fibers. Citrate synthase activity was most closely related to the population of type IIA fibers ( r ϭ 0.68, p Ͻ 0.0001) and was in the rank order of type IIA Ͼ I Ͼ IIX Ͼ IIB. These data demonstrate that hamster skeletal muscle is predominantly composed of type IIB and IIX fibers.

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“…Studies of creatine kinase in mouse muscular dystrophy have revealed the presence of an abnormal enzyme molecule lacking one of the two essential thiol groups of the normal dimeric enzyme (Hooton & Watts, 1966). Defects in sarcosomal oxidative phosphorylation have been detected at late stages of polymyopathy in the same Syrian hamster strain we have used for our studies (Lochner & Brink, 1967;Lochner et al, 1968;Schwartz et al, 1968). An abnormal foetal-type metmyoglobin has been detected in the muscles ofpatients with progressive muscular dystrophy (Whorton et al, 1961).…”

Section: Discussionmentioning

confidence: 89%

Cell-free protein synthesis in heart and skeletal muscles from polymyopathic hamsters

Bester

Gevers

1973

Biochemical Journal

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1. Cell-free protein synthesis was studied in striated and smooth muscles in an attempt to elucidate the primary genetic defect in polymyopathic hamsters. 2. When washed membrane-free polyribosomes from myopathic and control heart muscle were individually recombined with pH5 enzymes from both types of animals, the pH5 enzymes from myopathic muscle were less active in polypeptide synthesis than those from controls, irrespective of the source of polyribosomes. 3. The same defect was present in skeletal-muscle preparations. 4. Both the initial rate and the maximum extent of incorporation were affected in the defective preparations from myopathic muscle. 5. Concentration differences, with respect to total protein and RNA, were not responsible. 6. Preincubation of the pH5 enzymes resulted in a greater degree of inhibition. 7. The defect in the pH5 enzymes from myopathic muscle was also expressed in poly(U)-directed polyphenylalanine synthesis. 8. Acid proteinase activity in extracts of control and myopathic muscle was the same but general ribonuclease activity in the latter extracts was higher. 9. The defect was also present when both types of pH5 enzymes were prepared in the presence of the ribonuclease-asborbent bentonite. 10. pH5 enzymes from uterine smooth muscle, brains and livers of myopathic animals were similarly affected in homologous and heterologous combinations. 11. It is concluded that the general tissue defect is both qualitative and quantitative in nature, implying that there is a shortage of some essential soluble component in the pH5 fraction which is accompanied by the presence of an altered substituent. This prevents the attainment of extents of polypeptide synthesis in vitro obtained in control extracts from unaffected animals.

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Protein Synthesis in the Myocardiopathy and Muscular Dystrophy of the Syrian Hamster

Cited by 9 publications

References 11 publications

Incorporation of amino acids into soluble and membrane protein fractions of dystrophic hamsters

Incorporation of amino acids into soluble and membrane protein fractions of dystrophic hamsters

Fiber Composition and Oxidative Capacity of Hamster Skeletal Muscle

Cell-free protein synthesis in heart and skeletal muscles from polymyopathic hamsters

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