A role for collagen in the pathogenesis of muscular dystrophy?

Duance, Victor Colin; Stephens, H. Brodie; Dünn, Michael J.; Bailey, Allen J.; Dubowitz, Victor

doi:10.1038/284470a0

Cited by 125 publications

(54 citation statements)

References 17 publications

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“…The phenomenon may be viewed irreversible derangement of muscle tissue organization (2,5,12). Fibrosis hinders nutritional support of myofibers, particularly in the advanced stages when they become physically isolated from blood supply (2).…”

Section: Discussionmentioning

confidence: 99%

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Expression of transforming growth factor-beta 1 in dystrophic patient muscles correlates with fibrosis. Pathogenetic role of a fibrogenic cytokine.

Bernasconi¹,

Torchiana²,

et al. 1995

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Section: Discussionmentioning

confidence: 99%

“…Myofiber degeneration is followed by muscle fibrosis, predominantly composed of type HI collagen and involving the endomysium and perimysium (12). Fibrosis may be evident at the early stage and progresses with the disease.…”

Section: Introductionmentioning

confidence: 99%

Expression of transforming growth factor-beta 1 in dystrophic patient muscles correlates with fibrosis. Pathogenetic role of a fibrogenic cytokine.

Bernasconi¹,

Torchiana²,

et al. 1995

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“…4a, lane t), a doublet of relatively well-resolved bands with apparent molecular weights of 130,000 and 140,000 were precipitated together with another polypeptide with an apparent molecular weight of 255,000. Because its distribution in frozen-sectioned muscle was similar to that described for type III collagen by Duance et al (12), further experiments were undertaken to determine whether or not antigen-39 might also be collagenous. Conditioned medium, containing either [35S]methionine-or [3H]proline-and [3H]glycine-labeled secreted products, was treated with purified bacterial collagenase before immunoprecipitation.…”

Section: Antigen-31--lamininmentioning

confidence: 99%

Extracellular matrix organization in developing muscle: correlation with acetylcholine receptor aggregates.

Bayne¹,

Anderson²,

Fambrough³

1984

The Journal of Cell Biology

177

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Monoclonal antibodies recognizing laminin, heparan sulfate proteoglycan, fibronectin, and two apparently novel connective tissue components have been used to examine the organization of extracellular matrix of skeletal muscle in vivo and in vitro. Four of the five monoclonal antibodies are described for the first time here.Immunocytochemical experiments with frozen-sectioned muscle demonstrated that both the heparan sulfate proteoglycan and laminin exhibited staining patterns identical to that expected for components of the basal lamina. In contrast, the remaining matrix constituents were detected in all regions of muscle connective tissue: the endomysium, perimysium, and epimysium.Embryonic muscle cells developing in culture elaborated an extracellular matrix, each antigen exhibiting a unique distribution. Of particular interest was the organization of extracellular matrix on myotubes: the build-up of matrix components was most apparent in plaques overlying clusters of an integral membrane protein, the acetylcholine receptor (AChR). The heparan sulfate proteoglycan was concentrated at virtually all AChR clusters and showed a remarkable level of congruence with receptor organization; laminin was detected at 70-95% of AChR clusters but often was not completely co-distributed with AChR within the cluster; fibronectin and the two other extracellular matrix antigens occurred at ~20, 8, and 2% of the AChR clusters, respectively, and showed little or no congruence with AChR. From observations on the distribution of extracellular matrix components in tissue cultured fibroblasts and myogenic cells, several ideas about the organization of extracellular matrix are suggested. (a) Congruence between AChR clusters and heparan sulfate proteoglycan suggests the existence of some linkage between the two molecules, possibly important for regulation of AChR distribution within the muscle membrane. (b) The qualitatively different patterns of extracellular matrix organization over myotubes and fibroblasts suggest that each of these cell types uses somewhat different means to regulate the assembly of extracellular matrix components within its domain. (c) The limited co-distribution of different components within the extracellular matrix in vitro and the selective immune precipitation of each antigen from conditioned medium suggest that each extracellular matrix component is secreted in a form that is not complexed with other matrix constituents.The surface of adult vertebrate skeletal muscle fibers is regionally specialized, both at tendon-attachment sites and at the neuromuscular junction. While the mechanisms that control the formation and maintenance of such specialized regions are still not clearly understood, attention has been focused recently on the possible influence of extracellular matrix on muscle surface organization. The extracellular matrix surrounding each muscle fiber can be divided into two obvious morphological layers (see reference 40). Most proximal to the sarcolemma is a felt-like band, -10-15-nm thick,

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“…A Cinemetria é um ramo da biomecânica que busca medir os parâmetros cinemáticos do movimento, ou seja, investigar a posição, deslocamento, velocidade e aceleração de um ou diferentes segmentos de interesse (AMADIO et al, 1999 Estudos sobre a presença e proporção das fibras colágenas nas distrofias musculares têm encontrado variações nestes dois aspectos, em relação aos tipos I, III e IV (DUANCE et al, 1980;STEPHENS et al, 1982;RAMPOLDI et al, 1986;HANTAI et al, 1995;PASSERINI et al, 2002). Ainda que os achados de cada autor, em relação ao tipo de colágeno alterado na DMD sejam variáveis, existe um consenso de que os tipos I, III e IV, dentre todos os outros já descritos merecem atenção no estudo da fibrose e adaptação tecidual.…”

Section: Avaliação Biomecânicaunclassified

“…A fim de melhor entender a localização da fibrose no músculo distrófico e as adaptações teciduais na presença da fisioterapia, utilizamos a análise imuno-histoquímica dos colágenos do tipo I, III e IV, uma vez que são apontados por diferentes estudos como quantitativamente aumentados na DMD (DUANCE et al, 1980;HANTAI et al, 1995;HUEBNER et al, 2008).…”

Section: Força De Reação Do Solo X Velocidadeunclassified

Golden Retriever Muscular Dystrophy (GRMD) como modelo morfofuncional da reparação tecidual na Distrofia Muscular de Duchenne

Machado¹

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A role for collagen in the pathogenesis of muscular dystrophy?

Cited by 125 publications

References 17 publications

Expression of transforming growth factor-beta 1 in dystrophic patient muscles correlates with fibrosis. Pathogenetic role of a fibrogenic cytokine.

Expression of transforming growth factor-beta 1 in dystrophic patient muscles correlates with fibrosis. Pathogenetic role of a fibrogenic cytokine.

Extracellular matrix organization in developing muscle: correlation with acetylcholine receptor aggregates.

Golden Retriever Muscular Dystrophy (GRMD) como modelo morfofuncional da reparação tecidual na Distrofia Muscular de Duchenne

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