Animal models of muscle diseases Part I: Avian dystrophy

Cosmos, Ethel; Butler, Jane; Mazliah, Jacob; Allard, E. Paul

doi:10.1002/mus.880030312

Cited by 20 publications

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“…The physiologic relevance of the resistance of dystrophic avian muscle Ca2+-ATPase to calmodulin is supported by sensitive studies of muscle strength, based on strain gauge measurements,5 which indicate decreased function in dystrophic muscle by 18 days post-hatch; recent studies in our laboratories have shown that the calmodulin sensitivity of Ca2+-ATPase is decreased and the calmodulin mRNA content of affected muscle significantly increased by 13 days ex ovo (Thacore et al, 1988). These changes occur well in advance of loss of the righting reflex and increases in serum creatine phosphokinase activity which are observed at 30-40 days in dystrophic animals (Cosmos et al, 1980;Hudecki et al, 1984).…”

Section: Discussionmentioning

confidence: 98%

Abnormal response to calmodulin in vitro of dystrophic chicken muscle membrane calcium-ATPase activity

Galindo¹,

Hudecki²,

Davis³

et al. 1988

Biochemistry

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A skeletal muscle membrane fraction enriched in sarcoplasmic reticulum (SR) contained Ca2+-ATPase activity which was stimulated in vitro in normal chickens (line 412) by 6 nM purified bovine calmodulin (33% increase over control, P less than 0.001). In contrast, striated muscle from chickens (line 413) affected with an inherited form of muscular dystrophy, but otherwise genetically similar to line 412, contained SR-enriched Ca2+-ATPase activity which was resistant to stimulation in vitro by calmodulin. Basal levels of Ca2+-ATPase activity (no added calmodulin) were comparable in muscles of unaffected and affected animals, and the Ca2+ optima of the enzymes in normal and dystrophic muscle were identical. Purified SR vesicles, obtained by calcium phosphate loading and sucrose density gradient centrifugation, showed the same resistance of dystrophic Ca2+-ATPase to exogenous calmodulin as the SR-enriched muscle membrane fraction. Dystrophic muscle had increased Ca2+ content compared to that of normal animals (P less than 0.04) and has been previously shown to contain increased levels of immuno- and bioactive calmodulin and of calmodulin mRNA. The calmodulin resistance of the Ca2+-ATPase in dystrophic muscle reflects a defect in regulation of cell Ca2+ metabolism associated with elevated cellular Ca2+ and calmodulin concentrations.

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Section: Discussionmentioning

confidence: 98%

Abnormal response to calmodulin in vitro of dystrophic chicken muscle membrane calcium-ATPase activity

Galindo¹,

Hudecki²,

Davis³

et al. 1988

Biochemistry

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Parenteral branched‐chain amino acid treatment and avian dystrophy

Hudecki¹,

Pollina²,

Heffner³

1982

Muscle and Nerve

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Genetically homozygous line 413 dystrophic chickens were given twice-daily intraperitoneal injections of solutions containing branched-chain amino acids (BCCA-leucine, valine, isoleucine) either alone or in combination; and their alpha-ketoacid analogs (alpha-ketoisocaproic and alpha-ketoisovaleric acids). Another trial consisted of an amino acid mixture containing BCAA. Amino acid supplementation in each case significantly prolonged righting ability measured regularly by a standardized flip-test procedure. Enhanced functional ability was not generally accompanied by a decrease in plasma creatine kinase activity. However, a measurable increase in the affected pectoralis major muscle mass and protein content (female chickens in particular) was found with BCAA therapy. Moreover, the increase in muscle bulk was attended in some cases by a reduction in the relative number of degenerating fibers quantitated microscopically. Contrariwise, the amino acid mixture caused a reduction in pectoralis muscle mass. It is concluded that parenteral BCAA therapy offers limited benefit in retarding dystrophic symptoms in the chickens.

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Clinical trials in chronic neuromuscular diseases: Proceedings of a colloquium at Totts Gap Institute, Bangor, PA, sponsored by The Muscular Dystrophy Association

Wolf¹,

Lewis²

1985

Muscle and Nerve

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Animal models of muscle diseases Part I: Avian dystrophy

Cited by 20 publications

References 0 publications

Abnormal response to calmodulin in vitro of dystrophic chicken muscle membrane calcium-ATPase activity

Abnormal response to calmodulin in vitro of dystrophic chicken muscle membrane calcium-ATPase activity

Parenteral branched‐chain amino acid treatment and avian dystrophy

Clinical trials in chronic neuromuscular diseases: Proceedings of a colloquium at Totts Gap Institute, Bangor, PA, sponsored by The Muscular Dystrophy Association

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