[This corrects the article DOI: 10.1371/journal.pone.0214908.].
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| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC10202262 | PMC |
| http://journals.plos.org/plosone/article?id=10.1371/journal.pone.0286286 | PLOS |
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Objective: Dysferlin is a large transmembrane protein that functions in critical processes of membrane repair and vesicle fusion. Dysferlin-deficiency due to mutations in the dysferlin gene leads to muscular dystrophy (Miyoshi myopathy (MM), limb girdle muscular dystrophy type 2B (LGMD2B), distal myopathy with anterior tibial onset (DMAT)), typically with early adult onset. At least 416 pathogenic dysferlin mutations are known, but for approximately 17% of patients, one or both of their pathogenic variants remain undefined following standard exon sequencing methods that interrogate exons and nearby flanking intronic regions but not the majority of intronic regions.
View Article and Find Full Text PDFLack of MG53 in human heart precludes utility as a biomarker of myocardial injury or endogenous cardioprotective factor.
Cardiovasc Res
May 2016
Institute for Neuroscience and Muscle Research, Kids Research Institute, The Children's Hospital at Westmead, Locked Bag 4001, Westmead 2145, Australia Discipline of Paediatrics and Child Health, University of Sydney, Children's Hospital at Westmead Clinical School, Westmead 2145, Australia.
Aims: Mitsugumin-53 (MG53/TRIM72) is an E3-ubiquitin ligase that rapidly accumulates at sites of membrane injury and plays an important role in membrane repair of skeletal and cardiac muscle. MG53 has been implicated in cardiac ischaemia-reperfusion injury, and serum MG53 provides a biomarker of skeletal muscle injury in the mdx mouse model of Duchenne muscular dystrophy. We evaluated the clinical utility of MG53 as a biomarker of myocardial injury.
View Article and Find Full Text PDFHomologous recombination mediates functional recovery of dysferlin deficiency following AAV5 gene transfer.
PLoS One
December 2012
Department of Pediatrics, The Ohio State University, Columbus, Ohio, United States of America.
The dysferlinopathies comprise a group of untreatable muscle disorders including limb girdle muscular dystrophy type 2B, Miyoshi myopathy, distal anterior compartment syndrome, and rigid spine syndrome. As with other forms of muscular dystrophy, adeno-associated virus (AAV) gene transfer is a particularly auspicious treatment strategy, however the size of the DYSF cDNA (6.5 kb) negates packaging into traditional AAV serotypes known to express well in muscle (i.
View Article and Find Full Text PDFLack of correlation between outcomes of membrane repair assay and correction of dystrophic changes in experimental therapeutic strategy in dysferlinopathy.
PLoS One
October 2012
Généthon, CNRS UMR8587, Evry, France.
Mutations in the dysferlin gene are the cause of Limb-girdle Muscular Dystrophy type 2B and Miyoshi Myopathy. The dysferlin protein has been implicated in sarcolemmal resealing, leading to the idea that the pathophysiology of dysferlin deficiencies is due to a deficit in membrane repair. Here, we show using two different approaches that fulfilling membrane repair as asseyed by laser wounding assay is not sufficient for alleviating the dysferlin deficient pathology.
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