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      The Clinical Outcome Study for dysferlinopathy: An international multicenter study.

      Author(s): 1 , 1 , 1 , 1 , 1 , 1 , 1 , 1 , 1 , 1 , 1 , 1 , 1 , 1 , 1 , 1 , 1 , 1 , 1 , 1 , 1 , 1 , 1 , 1 , 1 , 1 , 1 , 1 , 1 , 1 , 1 , 1 , 1 , 1 , 1
      Publication date (Electronic):
      Journal: Neurology. Genetics
      Publisher: Ovid Technologies (Wolters Kluwer Health)

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          Abstract

          To describe the baseline clinical and functional characteristics of an international cohort of 193 patients with dysferlinopathy.

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          A gene related to Caenorhabditis elegans spermatogenesis factor fer-1 is mutated in limb-girdle muscular dystrophy type 2B.

          L Passos, Ryan Strachan, E Vafiadaki … (1998)
          The limb-girdle muscular dystrophies are a genetically heterogeneous group of inherited progressive muscle disorders that affect mainly the proximal musculature, with evidence for at least three autosomal dominant and eight autosomal recessive loci. The latter mostly involve mutations in genes encoding components of the dystrophin-associated complex; another form is caused by mutations in the gene for the muscle-specific protease calpain 3. Using a positional cloning approach, we have identified the gene for a form of limb-girdle muscular dystrophy that we previously mapped to chromosome 2p13 (LGMD2B). This gene shows no homology to any known mammalian gene, but its predicted product is related to the C. elegans spermatogenesis factor fer-1. We have identified two homozygous frameshift mutations in this gene, resulting in muscular dystrophy of either proximal or distal onset in nine families. The proposed name 'dysferlin' combines the role of the gene in producing muscular dystrophy with its C. elegans homology.
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            Clinical, molecular, and protein correlations in a large sample of genetically diagnosed Italian limb girdle muscular dystrophy patients.

            Sabrina Lucchiari, Marina Mora, Anna Carla Turconi … (2008)
            Limb girdle muscular dystrophies (LGMD) are characterized by genetic and clinical heterogeneity: seven autosomal dominant and 12 autosomal recessive loci have so far been identified. Aims of this study were to evaluate the relative proportion of the different types of LGMD in 181 predominantly Italian LGMD patients (representing 155 independent families), to describe the clinical pattern of the different forms, and to identify possible correlations between genotype, phenotype, and protein expression levels, as prognostic factors. Based on protein data, the majority of probands (n=72) presented calpain-3 deficiency; other defects were as follows: dysferlin (n=31), sarcoglycans (n=32), alpha-dystroglycan (n=4), and caveolin-3 (n=2). Genetic analysis identified 111 different mutations, including 47 novel ones. LGMD relative frequency was as follows: LGMD1C (caveolin-3) 1.3%; LGMD2A (calpain-3) 28.4%; LGMD2B (dysferlin) 18.7%; LGMD2C (gamma-sarcoglycan) 4.5%; LGMD2D (alpha-sarcoglycan) 8.4%; LGMD2E (beta-sarcoglycan) 4.5%; LGMD2F (delta-sarcoglycan) 0.7%; LGMD2I (Fukutin-related protein) 6.4%; and undetermined 27.1%. Compared to Northern European populations, Italian patients are less likely to be affected with LGMD2I. The order of decreasing clinical severity was: sarcoglycanopathy, calpainopathy, dysferlinopathy, and caveolinopathy. LGMD2I patients showed both infantile noncongenital and mild late-onset presentations. Age at disease onset correlated with variability of genotype and protein levels in LGMD2B. Truncating mutations determined earlier onset than missense substitutions (20+/-5.1 years vs. 36.7+/-11.1 years; P=0.0037). Similarly, dysferlin absence was associated with an earlier onset when compared to partial deficiency (20.2+/-standard deviation [SD] 5.2 years vs. 28.4+/-SD 11.2 years; P=0.014). (c) 2007 Wiley-Liss, Inc.
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              Dysferlin is a plasma membrane protein and is expressed early in human development.

              K Bushby, I Mahjneh, Melissa L. Anderson … (1999)
              Recently, a single gene, DYSF, has been identified which is mutated in patients with limb-girdle muscular dystrophy type 2B (LGMD2B) and with Miyoshi myopathy (MM). This is of interest because these diseases have been considered as two distinct clinical conditions since different muscle groups are the initial targets. Dysferlin, the protein product of the gene, is a novel molecule without homology to any known mammalian protein. We have now raised a monoclonal antibody to dysferlin and report on the expression of this new protein: immunolabelling with the antibody (designated NCL-hamlet) demonstrated a polypeptide of approximately 230 kDa on western blots of skeletal muscle, with localization to the muscle fibre membrane by microscopy at both the light and electron microscopic level. A specific loss of dysferlin labelling was observed in patients with mutations in the LGMD2B/MM gene. Furthermore, patients with two different frameshifting mutations demonstrated very low levels of immunoreactive protein in a manner reminiscent of the dystrophin expressed in many Duchenne patients. Analysis of human fetal tissue showed that dysferlin was expressed at the earliest stages of development examined, at Carnegie stage 15 or 16 (embryonic age 5-6 weeks). Dysferlin is present, therefore, at a time when the limbs start to show regional differentiation. Lack of dysferlin at this critical time may contribute to the pattern of muscle involvement that develops later, with the onset of a muscular dystrophy primarily affecting proximal or distal muscles.
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                Author and article information

                Journal
                Journal ID (iso-abbrev): Neurol Genet
                Title: Neurology. Genetics
                Publisher: Ovid Technologies (Wolters Kluwer Health)
                ISSN (Print): 2376-7839
                Publication date (Electronic): Aug 2016
                Volume: 2
                Issue: 4
                Affiliations
                [1 ] The John Walton Muscular Dystrophy Research Centre (E.H., C.L.B., A.M., M.J., K. Bettinson, U.M., M.E., H.L., V.S., K. Bushby), Institute of Genetic Medicine, Newcastle upon Tyne, UK; Magnetic Resonance Centre (F.E.S., A.M.B.), Institute for Cellular Medicine, Newcastle University, UK; Jain Foundation, Inc. (L.R.), Seattle, WA; Division of Biostatistics and Study Methodology (A.C.), Center for Translational Science, Children's National Health System, Washington, DC; Department of Pediatrics, Epidemiology and Biostatistics (A.C.), George Washington University; Department of Neurology (D.X.B.-G.), Children's National Health System, Washington, DC; National Institutes of Health (NINDS) (D.X.B.-G.), Bethesda, MD; Carolinas Healthcare System Neurosciences Institute (E.B.), Charlotte; AIM & CEA NMR Laboratory (P.G.C.), Institute of Myology, Pitié-Salpêtrière University Hospital, Paris, France; Stanford University School of Medicine (J.W.D., C.T.R.), CA; Neuromuscular Disorders Unit (J.D.-M.), Department of Neurology, Hospital de la Santa Creu i Sant Pau, Barcelona, Spain; Centro de Investigación Biomédica en Red en Enfermedades Raras (CIBERER) (J.D.-M.), Barcelona, Spain; Muscle Research Unit (U.G., S.S.), Experimental and Clinical Research Center, A Joint Cooperation of the Charité Medical Faculty and the Max Delbrück Center for Molecular Medicine, Berlin, Germany; Washington University (M.H., A.P.), St. Louis, MO; Institute for Neuroscience and Muscle Research (K.J.J.), Children's Hospital at Westmead, University of Sydney, Australia; Nationwide Children's Hospital (J.R.M.), Columbus, OH; Department of Neurology (M.M.-Y., S.T.), National Center Hospital, National Center of Neurology and Psychiatry, Tokyo, Japan; Neuromuscular Unit, Department of Neurology (C.P.), Hospital U. Virgen del Rocío, Instituto de Biomedicina de Sevilla, Spain; Department of Neuroscience (E.P., C.S.), University of Padova, Italy; Neuromuscular and ALS Center (E.S.-C.), La Timone Hospital
                Article
                Publisher Item ID: NG2016002162
                DOI: 10.1212/NXG.0000000000000089
                PMC ID: 4994875
                PubMed ID: 27602406
                SO-VID: ae00f8f1-249d-44f1-a526-e0b9edf64820
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