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GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 19 Dec 2016.

Dysferlin, limb girdle muscular dystrophy 2B

dysferlin, DYSF, LGMD2B
The protein encoded by this gene belongs to the ferlin family and is a skeletal muscle protein found associated with the sarcolemma. It is involved in muscle contraction and contains C2 domains that play a role in calcium-mediated membrane fusion events, suggesting that it may be involved in membrane regeneration and repair. In addition, the protein encoded by this gene binds caveolin-3, a skeletal muscle membrane protein which is important in the formation of caveolae. Specific mutations in this gene have been shown to cause autosomal recessive limb girdle muscular dystrophy type 2B (LGMD2B) as well as Miyoshi myopathy. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Aug 2008] (from NCBI)
Top mentioned proteins: CAN, HAD, AGE, caveolin-1, Calpain
Papers using dysferlin antibodies
mdx(cv) mice manifest more severe muscle dysfunction and diaphragm force deficits than do mdx Mice.
McNeil Paul, In PLoS ONE, 2010
... The dysferlin expression cassettes was cloned between AAV2 ITRs using flanking Xba I restriction enzyme sites in a plasmid derived from pCMVβ (Clontech).
Papers on dysferlin
Ferlins show tissue-specific expression and segregate as plasma membrane/late endosomal or trans-Golgi/recycling ferlins.
Cooper et al., Sydney, Australia. In Traffic, Jan 2016
In humans, dysferlin mutations cause limb-girdle muscular dystrophy (LGMD2B) due to defective Ca(2+) -dependent, vesicle-mediated membrane repair and otoferlin mutations cause non-syndromic deafness due to defective Ca(2+) -triggered auditory neurotransmission.
Dysferlinopathy in Iran: Clinical and genetic report.
Attarian et al., Tehrān, Iran. In J Neurol Sci, Jan 2016
METHODS: Genomic DNA was extracted from peripheral blood and 55 exons and flanking intronic boundaries of the dysferlin gene (DYSF; NM_003494.2) were screened for mutations and analyzed.
Membrane Injury and Repair in the Muscular Dystrophies.
Head et al., Sydney, Australia. In Neuroscientist, Dec 2015
We review the different mechanisms by which muscle fibers in patients with muscular dystrophy are rendered more susceptible to injury, and we summarize the latest developments in our understanding of how the muscular dystrophy protein dysferlin mediates satellite-cell independent membrane repair.
Plasma Membrane Repair in Health and Disease.
McNally et al., Chicago, United States. In Curr Top Membr, Dec 2015
Dysferlin is a membrane-associated protein implicated in sarcolemmal repair and also linked to other membrane functions including the maintenance of transverse tubules in muscle.
Full-length Dysferlin Transfer by the Hyperactive Sleeping Beauty Transposase Restores Dysferlin-deficient Muscle.
Izsvák et al., Berlin, Germany. In Mol Ther Nucleic Acids, Dec 2015
We constructed an SB transposon-based vector to deliver full-length human DYSF cDNA into dysferlin-deficient H2K A/J myoblasts.
Genome-wide expression analysis comparing hypertrophic changes in normal and dysferlinopathy mice.
Lee et al., Baltimore, United States. In Genom Data, Dec 2015
Our study shows that blocking this pathway in dysferlin deficient mice results in early improvement in histopathology but ultimately accelerates muscle degeneration.
Calcium signaling in membrane repair.
Xu et al., Ann Arbor, United States. In Semin Cell Dev Biol, Sep 2015
Multiple calcium sensors, including synaptotagmin (Syt) VII, dysferlin, and apoptosis-linked gene-2 (ALG-2), are involved in PM resealing, suggesting that Ca(2+) may regulate multiple steps of the repair process.
Dysferlinopathy Fibroblasts Are Defective in Plasma Membrane Repair.
Hayashi et al., Tsukuba, Japan. In Plos Curr, 2014
BACKGROUND: Dysferlin is a sarcolemmal protein that is defective in Miyoshi myopathy and limb-girdle muscular dystrophy type 2B, and is involved in sarcolemmal repair.
Genetic basis of limb-girdle muscular dystrophies: the 2014 update.
Savarese et al., Napoli, Italy. In Acta Myol, 2014
The autosomal recessive forms (LGMD2) are: LGMD2A (calpain 3), LGMD2B (dysferlin), LGMD2C (γ sarcoglycan), LGMD2D (α sarcoglycan), LGMD2E (β sarcoglycan), LGMD2F (δ sarcoglycan), LGMD2G (telethonin), LGMD2H (TRIM32), LGMD2I (FKRP), LGMD2J (titin), LGMD2K (POMT1), LGMD2L (anoctamin 5), LGMD2M (fukutin), LGMD2N (POMT2), LGMD2O (POMTnG1), LGMD2P (dystroglycan), LGMD2Q (plectin), LGMD2R (desmin), LGMD2S (TRAPPC11), LGMD2T (GMPPB), LGMD2U (ISPD), LGMD2V (Glucosidase, alpha ), LGMD2W (PINCH2).
Antisense therapy in neurology.
Yokota et al., Edmonton, Canada. In J Pers Med, 2012
Spinal muscular atrophy (SMA), Huntington's disease (HD), amyotrophic lateral sclerosis (ALS), Duchenne muscular dystrophy (DMD), Fukuyama congenital muscular dystrophy (FCMD), dysferlinopathy (including limb-girdle muscular dystrophy 2B; LGMD2B, Miyoshi myopathy; MM, and distal myopathy with anterior tibial onset; DMAT), and myotonic dystrophy (DM) are all reported to be promising targets for antisense therapy.
Modular dispensability of dysferlin C2 domains reveals rational design for mini-dysferlin molecules.
Sinnreich et al., Basel, Switzerland. In J Biol Chem, 2012
Modular dispensability of dysferlin C2 domains reveals rational design for mini-dysferlin molecules.
Myogenesis in dysferlin-deficient myoblasts is inhibited by an intrinsic inflammatory response.
Partridge et al., Washington, D.C., United States. In Neuromuscul Disord, 2012
The results suggest that decreased myotube fusion in dysferlin deficiency is attributable to intrinsic inflammatory activation and can be improved using anti-inflammatory mediators.
Dystrophin and dysferlin double mutant mice: a novel model for rhabdomyosarcoma.
Shultz et al., Bar Harbor, United States. In Cancer Genet, 2012
Mice with dystrophin and dysferlin double mutations develop mixed sarcomas with variable penetrance and latency.
Proteasomal inhibition restores biological function of mis-sense mutated dysferlin in patient-derived muscle cells.
Sinnreich et al., Basel, Switzerland. In J Biol Chem, 2012
Inhibition of the proteasome by lactacystin or Velcade increases the levels of R555W mis-sense mutated dysferlin.
Lysosome fusion to the cell membrane is mediated by the dysferlin C2A domain in coronary arterial endothelial cells.
Li et al., Richmond, United States. In J Cell Sci, 2012
dysferlin mediates lysosome fusion to the plasma membrane and thereby leads to ASMase translocation, membrane raft clustering and NADPH oxidase activation in coronary arterial endothelial cells, which consequently results in endothelial dysfunction
Defective membrane repair in dysferlin-deficient muscular dystrophy.
Campbell et al., Iowa City, United States. In Nature, 2003
Dysferlin-null mice maintain a functional dystrophin-glycoprotein complex but nevertheless develop a progressive muscular dystrophy
Limb-girdle muscular dystrophy type 2G is caused by mutations in the gene encoding the sarcomeric protein telethonin.
Jenne et al., São Paulo, Brazil. In Nat Genet, 2000
11) and dysferlin, respectively, and are usually associated with a mild phenotype.
A gene related to Caenorhabditis elegans spermatogenesis factor fer-1 is mutated in limb-girdle muscular dystrophy type 2B.
Bushby et al., Newcastle upon Tyne, United Kingdom. In Nat Genet, 1998
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).
Dysferlin, a novel skeletal muscle gene, is mutated in Miyoshi myopathy and limb girdle muscular dystrophy.
Brown et al., United States. In Nat Genet, 1998
We describe nine mutations in the dysferlin gene in nine families; five are predicted to prevent dysferlin expression.
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