Proteolytic Activity During Growth of Hypertrophic and Atrophic Muscles of Genetically Dystrophic Chickens

Peterson, D. W.; Lilyblade, A. L.; Bond, D. C.

doi:10.3181/00379727-141-36932

Cited by 14 publications

(3 citation statements)

References 12 publications

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“…Associated with the increased rates of protein degradation in dystrophic muscle is the elevation in activity of lysosomal cathepsins A, B, C and D (Iodice et al, 1972;Peterson et al, 1972). During early development of normal breast muscle after hatching, cathepsin activity is initially high and gradually declines as growth slows, whereas in hypertrophied dystrophic pectoral muscle, cathepsin activity remains elevated.…”

Section: Discussionmentioning

confidence: 99%

“…Lysosomal cathepsin activity has also been shown to hereditary muscular dystrophy in the chicken is be markedly increased in dystrophic muscle, inferaccelerated muscle protein turnover. Protein syn-ring elevated protein catabolism in this tissue (lodice thesis has been reported to be elevated 2-fold Peterson et al, 1972). By using isotopic dystrophic pectoral muscle (Weinstock et al, 1969).…”

Section: One Of the Many Abnormalities That Characterizesmentioning

confidence: 96%

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Myofibrillar protein degradation in the chicken 3-Methylhistidine release in vivo and in vitro in normal and genetically muscular-dystrophic chickens

Hillgartner

Williams

Flanders

et al. 1981

Biochemical Journal

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Myofibrillar protein degradation was measured in 4-week-old normal (line 412) and genetically muscular-dystrophic (line 413) New Hampshire chickens by monitoring the rates of 3-methylhistidine excretion in vivo and in vitro. A method of perfusing breast and wing muscles was developed and the rate of 3-methylhistidine release in vitro was measured between 30 and 90min of perfusion. During this perfusion period, 3-methylhistidine release from the muscle preparation was linear, indicating that changes in 3-methylhistidine concentration of the perfusate were the result of myofibrillar protein degradation. Furthermore, the viability of the perfused muscle was maintained during this interval. After 60min of perfusion, ATP, ADP and creatine phosphate concentrations in pectoral muscle were similar to muscle freeze-clamped in vivo. Rates of glucose uptake and lactate production were constant during the perfusion. In dystrophic-muscle preparations, the rate of 3-methylhistidine release in vitro (nmol/h per g of dried muscle) was elevated 2-fold when compared with that in normal muscle. From these data the fractional degradation rates of myofibrillar protein in normal and dystrophic pectoral muscle were calculated to be 12 and 24% respectively. Daily 3-methylhistidine excretion (nmol/day per g body wt.) in vivo was elevated 1.35-fold in dystrophic chickens. Additional studies revealed that the anti-dystrophic drugs diphenylhydantoin and methylsergide, which improve righting ability of dystrophic chickens, did not alter 3-methylhistidine release in vitro. This result implies that changes in myofibrillar protein turnover are not the primary lesion in avian muscular dystrophy. From tissue amino acid analysis, the myofibrillar 3-methylhistidine content per g dry weight of muscle was similar in normal and dystrophic pectoral muscle. More than 96% of the 3-methylhistidine present in pectoral muscle was associated with the myofibrillar fraction. Dystrophic myofibrillar protein contained significantly less 3-methylhistidine (nmol/g of myofibrillar protein) than protein from normal muscle. This observation supports the hypothesis that there may be a block in the biochemical maturation and development of dystrophic muscle after hatching. Free 3-methylhistidine (nmol/g wet wt.) was elevated in dystrophic muscle, whereas blood 3-methylhistidine concentrations were similar in both lines. In summary, the increased myofibrillar protein catabolism demonstrated in dystrophic pectoral muscle correlates with the increased lysosomal cathepsin activity in this tissue as reported by others.

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Section: Discussionmentioning

confidence: 99%

Section: One Of the Many Abnormalities That Characterizesmentioning

confidence: 96%

Myofibrillar protein degradation in the chicken 3-Methylhistidine release in vivo and in vitro in normal and genetically muscular-dystrophic chickens

Hillgartner

Williams

Flanders

et al. 1981

Biochemical Journal

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“…Indirect evidence of the importance of protein degradation in muscular dystrophy has come from measurements of proteinase activity in dystrophic muscle and from studies of the effect of antiproteinases on degenerative changes in dystrophic muscle. Elevated amounts of proteinases have been found in dystrophic mouse (Weinstock et al, 1958;McCaman, 1963;Tappel et al, 1962;Pennington, 1963), chicken (Tappel et al, 1962;lodice et al, 1966;Peterson et al, 1972) and human (Kar & Pearson, 1978) muscle. In 1976 reported that degenerative changes in dystrophic chick (Connecticut strain) muscle cultures could be prevented by antiproteinases such as leupeptin and pepstatin, and these inhibitors have also been shown to inhibit protein degradation in other systems (Iodice, 1976;Libby & Goldberg, 1978).…”

mentioning

confidence: 99%

Protein degradation in skin fibroblasts from patients with Duchenne muscular dystrophy

Statham¹,

Witkowski²,

Dubowitz³

1980

Biochemical Journal

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The rates of degradation of [3H]leucine-labelled proteins have been measured in cultures of skin fibroblasts obtained from normal controls (five subjects) and patients with Duchenne muscular dystrophy (six subjects). Cultures were incubated with [3H]leucine (10 microCi/ml) for 60 min to label "short-lived" proteins, and with [3H]leucine (5 microCi/ml) for 60 h to label "long-lived" proteins. Optimal wash procedures were devised for removal of [3H]leucine from the extracellular space and from cell pools before beginning degradation measurements. Re-utilization of [3H]leucine released from degraded labelled proteins was prevented by supplementing the medium with 4mM-leucine. Rates of degradation did not depend on the growth state of the cells or on cell age over the range used (passages eight-20). Degradation of long-lived proteins was approximately linear over a 24h period, at a rate of 1.0% per h. 30% of short-lived protein was degraded within 6h. No differences were observed between protein degradation in normal fibroblasts and in those from patients with Duchenne muscular dystrophy.

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Therapeutic Trials in Muscular Dystrophy

Enomoto

Bradley

1977

Arch Neurol

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Proteolytic Activity During Growth of Hypertrophic and Atrophic Muscles of Genetically Dystrophic Chickens

Cited by 14 publications

References 12 publications

Myofibrillar protein degradation in the chicken 3-Methylhistidine release in vivo and in vitro in normal and genetically muscular-dystrophic chickens

Myofibrillar protein degradation in the chicken 3-Methylhistidine release in vivo and in vitro in normal and genetically muscular-dystrophic chickens

Protein degradation in skin fibroblasts from patients with Duchenne muscular dystrophy

Therapeutic Trials in Muscular Dystrophy

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