Aberrant glycosylation of α‐dystroglycan causes defective binding of laminin in the muscle of chicken muscular dystrophy

Saito, Fumiaki; Blank, Martina; Schröder, Jörn E.; Manya, Hiroshi; Shimizu, Teruo; Campbell, Kevin P.; Endo, Tamao; Mizutani, Makoto; Kröger, Stephan; Matsumura, Kiichiro

doi:10.1016/j.febslet.2005.03.033

Cited by 30 publications

(26 citation statements)

References 25 publications

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“…Though much remains unclear about WWP1Õs substrates, it has been demonstrated that WWP1 could interact with bdystroglycan, an important muscle protein consisting of membrane [30]. Abnormal glycosylation of a-dystroglycan in chicken muscular dystrophy was also reported [31]. Some E3s are known to recognize sugar chain [32][33][34], leading to the hypothesis that WWP1 might be able to recognize the sugar chain of a-dystroglycan and regulate the glycosylated molecules, and that insufficiently glycosylated a-dystroglycan, which originally requires degradation, accumulates and causes the disease because altered WWP1 can not recognize and degrade it.…”

Section: Discussionmentioning

confidence: 99%

The ubiquitin ligase gene (WWP1) is responsible for the chicken muscular dystrophy

et al. 2008

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Chicken muscular dystrophy with abnormal muscle (AM) has been studied for more than 50 years, but the gene responsible for it remains unclear. Our previous studies narrowed down the AM candidate region to approximately 1 Mbp of chicken chromosome 2q containing seven genes. In this study, we performed sequence comparison and gene expression analysis to elucidate the responsible gene. One missense mutation was detected in AM candidate genes, while no remarkable alteration of expression patterns was observed. The mutation was identified in WWP1, detected only in dystrophic chickens within several tetrapods. These results suggested WWP1 is responsible for chicken muscular dystrophy.

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Section: Discussionmentioning

confidence: 99%

The ubiquitin ligase gene (WWP1) is responsible for the chicken muscular dystrophy

et al. 2008

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“…In addition, several human congenital muscular dystrophies are caused by mutations in glycosyltransferases that modify the unusual O-linked carbohydrate moieties that are found on DG (Cohn, 2005;Schachter et al, 2004). The loss of these carbohydrate modifications has been shown to disrupt DG binding to several ligands, including laminins (Kanagawa et al, 2005;Kim et al, 2004;Patnaik and Stanley, 2005;Saito et al, 2005). Like laminin deficiencies that cause MCD1A, these dystrophies also cause developmental brain abnormalities, including MDC1C (myd in mice), Fukuyama's muscular dystrophy (FCMD), muscle-eye-brain disease (MEB) and Walker-Warburg syndrome (WWS).…”

Section: Discussionmentioning

confidence: 99%

Identification of dystroglycan as a second laminin receptor in oligodendrocytes, with a role in myelination

et al. 2007

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2Developmental abnormalities of myelination are observed in the brains of laminin-deficient humans and mice. The mechanisms by which these defects occur remain unknown. It has been proposed that, given their central role in mediating extracellular matrix (ECM) interactions, integrin receptors are likely to be involved. However, it is a non-integrin ECM receptor, dystroglycan, that provides the key linkage between the dystrophin-glycoprotein complex (DGC) and laminin in skeletal muscle basal lamina, such that disruption of this bridge results in muscular dystrophy. In addition, the loss of dystroglycan from Schwann cells causes myelin instability and disorganization of the nodes of Ranvier. To date, it is unknown whether dystroglycan plays a role during central nervous system (CNS) myelination. Here, we report that the myelinating glia of the CNS, oligodendrocytes, express and use dystroglycan receptors to regulate myelin formation. In the absence of normal dystroglycan expression, primary oligodendrocytes showed substantial deficits in their ability to differentiate and to produce normal levels of myelin-specific proteins. After blocking the function of dystroglycan receptors, oligodendrocytes failed both to produce complex myelin membrane sheets and to initiate myelinating segments when co-cultured with dorsal root ganglion neurons. By contrast, enhanced oligodendrocyte survival in response to the ECM, in conjunction with growth factors, was dependent on interactions with beta-1 integrins and did not require dystroglycan. Together, these results indicate that laminins are likely to regulate CNS myelination by interacting with both integrin receptors and dystroglycan receptors, and that oligodendrocyte dystroglycan receptors may have a specific role in regulating terminal stages of myelination, such as myelin membrane production, growth, or stability.

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“…The observed level of heterogeneity in the satellite cell population may relate to differences in experimental design, the timing Laminin is one of the external matrix proteins that is complexed with the dystrophin-associated proteins that are either internal, transmembrane or linked with proteins inside the sarcolemma in normal muscle (Crawford et al, 2000;Ervasti and Campbell, 1993;Ferletta et al, 2003). In muscles affected by mutations in proteins of the dystrophin-associated protein complex, the expression of laminin is reduced; this is also noted in dystrophin-deficient muscle (Ferletta et al, 2003;Kanagawa et al, 2005;Kikkawa et al, 2004;Kim et al, 2004;Saito et al, 2005). Treatment with glucocorticoids increases the expression of laminin in mdx mouse skeletal muscle (Anderson et al, 2000).…”

Section: Satellite Cells In Muscle Plasticitymentioning

confidence: 99%

The satellite cell as a companion in skeletal muscle plasticity:currency, conveyance, clue, connector and colander

Anderson

2006

Journal of Experimental Biology

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THE JOURNAL OF EXPERIMENTAL BIOLOGY 2277 Satellite cells in muscle plasticity formed cells fusing to form myoblasts and finally multinucleated muscle fibres.'That conference was a landmark in studies of the satellite cell and muscle regeneration, and was attended by many of the notable and pioneering contributors to the field of muscle development and muscle regeneration. Muir summarized the debate on a working definition of the satellite cell, as follows (Muir, 1970):'The satellite cell of striated muscle can be defined as a mononucleated cell, whose cytoplasm does not contain myofilaments, and which is enclosed by or lies within the basement membrane component of the sarcolemma of the striated muscle fibre. This definition does not exclude cells which are partially or completely separated from the muscle fibre plasma membrane by extensions of the basement membrane, providing that the basement membrane forms a complete investment of their outer surfaces. ' Although there were presentations detailing the observed uptake of 3 H-thymidine into nuclei of satellite cells (Hay, 1970), the role of satellite cells as precursors was not fully established in 1969. In fact there was still very strong debate that a muscle fibre could fragment into blastema cells that led to new formation of muscle. Even at this time, there was more than one paper on the appearance of osteogenic and chondrogenic tissues from minces of muscle replaced under the skin, and a report of muscle fibre nuclei contributed by a labelled connective tissue grafted into a salamander limb during regeneration (Steen, 1970).It wasn't until two seminal reports from the laboratory of Dr Charles Leblond at McGill University (Moss and Leblond, 1970;Moss and Leblond, 1971) that skeletal muscle satellite cells were convincingly identified as the source of precursor cells that proliferate and fuse to form new skeletal muscle fibres. Time-course studies of labelled nuclei in growing muscle showed that satellite cells were the only muscle cells that had incorporated 3 H-thymidine. The report followed work on colchicine-treated rats (MacConnachie et al., 1964) that showed mitotic figures only in the peripheral 'satellite' position on muscle fibres. The idea that muscle fibre nuclei give rise to the increasing number of myonuclei during the growth was convincingly ruled out (Enesco and Puddy, 1964). The notion that satellite cells contribute these domains to a growing or regenerating fibre, one at a time, is daunting in light of the expenditure of proliferative energy and fusion events. However, it speaks strongly to one of the major roles of satellite cells as a currency of muscle (see below). Satellite cells were also observed on intrafusal fibres (Katz, 1961). Two types of satellite cells were identified on these socalled muscle spindle fibres and were distinguished from those on extrafusal fibres (Maynard and Cooper, 1973), although at least one would now be called a myoblast.Although typically quiescent in normal adult muscle, satellite cells are generally con...

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Aberrant glycosylation of α‐dystroglycan causes defective binding of laminin in the muscle of chicken muscular dystrophy

Cited by 30 publications

References 25 publications

The ubiquitin ligase gene (WWP1) is responsible for the chicken muscular dystrophy

The ubiquitin ligase gene (WWP1) is responsible for the chicken muscular dystrophy

Identification of dystroglycan as a second laminin receptor in oligodendrocytes, with a role in myelination

The satellite cell as a companion in skeletal muscle plasticity:currency, conveyance, clue, connector and colander

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