Early detection of inherited muscular dystrophy in chickens

Allen, E. Raworth; Murphy, Bruce J.

doi:10.1007/bf00233561

Cited by 11 publications

(4 citation statements)

References 4 publications

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“…However, it can also be argued that, under relaxing conditions, the thick and thin filaments have separated, but the dystrophic sarcomere resists fragmentation because of a change in the mechanical properties of one of the subcomponents of the sarcomere. In interpreting the results of fragmentation analysis, structural and mechanical features of muscle that may be relevant include (1 ) evidence that the thick6,18 or thin filaments7,18 themselves do not behave as rigid rods but are in fact flexible and elastic, (2) that a separate cytoskeletal scaffold exists into which the Z-disks are integrated,1° (3) that the thin filaments are anchored into the Z-disks, and ( 4 ) that a network of protein known as connectin, with elastic properties, has been postulated to hold the myofilaments and Z-disks together. "alZ Therefore, many different mechanical models can be proposed which can account for the resistance to fragmentation of dystrophic sarcomeres, and further experiments will be required to distinguish among these possibilities.…”

Section: Discussionmentioning

confidence: 99%

Fragmentation analysis of normal and dystrophic avian muscle

et al. 1982

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A difference between normal and dystrophic avian muscle was demonstrated by comparing the patterns of fragmentation of muscle during homogenization. Fragmentation was monitored by morphological methods and by viscometry. This method of fragmentation analysis depends on the principle that the viscosity of a suspension is an exponential function of the partial volume fraction occupied by the suspended particles; the more a tissue is fragmented into smaller pieces, the greater the viscosity of the resulting homogenate. Increasing the duration of homogenization of either fresh muscle in buffer or glycerinated muscle in relaxing solution gradually increased the viscosity of the homogenate of normal muscle, whereas the viscosity of the homogenate of dystrophic muscle remained approximately constant. This difference in viscosity indicated that dystrophic muscle was sheared into larger pieces which were resistant to further fragmentation. Electron microscopic examination showed that the homogenate of dystrophic muscle contained rows of sarcomeres, whereas normal muscle was sheared into amorphous masses of myofilaments.

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Section: Discussionmentioning

confidence: 99%

Fragmentation analysis of normal and dystrophic avian muscle

et al. 1982

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“…As mentioned above, caveolae play a role in buffering mechanical stress at the plasma membrane, since muscle fibers are repeatedly experiencing mechanical stress at the plasma membrane, which must be able to rapidly repair wounds. The failure to repair causes the degenerative changes in Z-band and myofibrils in embryonic pectoralis muscle fibers [91]. McLean et al (1986) also found extensive changes in patterning of sarcolemmal caveolae of chicken dystrophic PLD muscle, but the patterning of normal fibers is arranged in striking bands over the myofibrillar Ibands [89].…”

Section: Caveolin-3: Another Causative Process Of Muscular Dystrophymentioning

confidence: 99%

Caveolin-3: A Causative Process of Chicken Muscular Dystrophy

Kikuchi

2020

Biomolecules

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The etiology of chicken muscular dystrophy is the synthesis of aberrant WW domain containing E3 ubiquitin-protein ligase 1 (WWP1) protein made by a missense mutation of WWP1 gene. The β-dystroglycan that confers stability to sarcolemma was identified as a substrate of WWP protein, which induces the next molecular collapse. The aberrant WWP1 increases the ubiquitin ligase-mediated ubiquitination following severe degradation of sarcolemmal and cytoplasmic β-dystroglycan, and an erased β-dystroglycan in dystrophic αW fibers will lead to molecular imperfection of the dystrophin-glycoprotein complex (DGC). The DGC is a core protein of costamere that is an essential part of force transduction and protects the muscle fibers from contraction-induced damage. Caveolin-3 (Cav-3) and dystrophin bind competitively to the same site of β-dystroglycan, and excessive Cav-3 on sarcolemma will block the interaction of dystrophin with β-dystroglycan, which is another reason for the disruption of the DGC. It is known that fast-twitch glycolytic fibers are more sensitive and vulnerable to contraction-induced small tears than slow-twitch oxidative fibers under a variety of diseased conditions. Accordingly, the fast glycolytic αW fibers must be easy with rapid damage of sarcolemma corruption seen in chicken muscular dystrophy, but the slow oxidative fibers are able to escape from these damages.

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“…eventual destruction of individual myofibers [2][3][4], However, it is unknown whether these findings are attributed to an intrinsic myofiber defect, or are the result of expression of the dystrophic gene in an extramyogenic tis sue.…”

Section: Introductionmentioning

confidence: 99%

Motoneuron Formation in the Brachial Spinal Cord of the Dystrophic Chick Embryo

Bj¹

1982

Pathobiology

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Motor neuroblasts comprising the brachial segments of the lateral motor column in the dystrophic chicken were counted at 6, 7, 9, 12, and 18 days of incubation and at 5 days’ post-hatching. Comparisons with similar counts from normal chick embryos disclosed that there was a significantly greater depletion of motor neurons in normal embryos between days 9 and 12. These findings suggest that nerve-muscle interaction may be altered early in the development of the motor unit in the dystrophic chick embryo.

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Early detection of inherited muscular dystrophy in chickens

Cited by 11 publications

References 4 publications

Fragmentation analysis of normal and dystrophic avian muscle

Fragmentation analysis of normal and dystrophic avian muscle

Caveolin-3: A Causative Process of Chicken Muscular Dystrophy

Motoneuron Formation in the Brachial Spinal Cord of the Dystrophic Chick Embryo

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