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The protein encoded by DYSF belongs to the ferlin family and is a skeletal muscle protein found associated with the sarcolemma.
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zebrafish dysferlin expression is involved in stabilizing muscle structures and its downregulation causes muscle disorganization.
Our data suggest that dysferlin modulates SR Ca(2 (show CA2 ELISA Kits)+) release in skeletal muscle, and that in its absence osmotic shock injury causes increased RyR1 (show RYR1 ELISA Kits)-mediated Ca(2 (show CA2 ELISA Kits)+) leak from the SR into the cytoplasm.
dysferlin has membrane tubulating capacity and that it shapes the T-tubule system.
These results provide one mechanism by which the C57BL/6J background intensifies dysferlinopathy, giving rise to a more severe form of muscular dystrophy in the Dysf(B6) mouse model through increased membrane leak and inflammation.
dysferlin-deficient cardiomyocytes showed slower Ca2 (show CA2 ELISA Kits)+ re-sequestration. Dysferlin deficiency blunted the beta-adrenergic effect on relaxation and pumping function of ex vivo working hearts.
Using both naturally occurring and genetically engineered dysferlin-deficient mice, the authors demonstrated that loss of dysferlin confers increased susceptibility to coxsackievirus infection and myocardial damage.
By targeting DYSF premRNA introns harbouring differentially defined 3' splice sites (3' SS), we found that target introns encoding weakly defined 3' SSs were trans-spliced successfully in vitro in human myoblasts also in vivo in skeletal muscle of mice.
Dysferlin does not regulate cardiac voltage-dependent ion channels in cardiomyocytes.
results show that dysferlin exerts protective effects on the fukutin (show FKTN ELISA Kits)(Hp/-) FCMD (show FKTN ELISA Kits) mouse model, and the (dysferlin(sjl/sjl): fukutin (show FKTN ELISA Kits)(Hp/-)) mice will be useful as a novel model for a recently proposed antisense oligonucleotide therapy for FCMD (show FKTN ELISA Kits)
results provide the mechanism for dysferlin-mediated repair of skeletal muscle sarcolemma and identify ASM (show SMPD1 ELISA Kits) as a potential therapy for dysferlinopathy
These novel observations of conspicuous intermyofibrillar lipid and progressive adipocyte replacement in dysferlin-deficient muscles.
This review detailed the different partners and function of dysferlin and positions the sarcolemma repair in normal and pathological conditions. [Review]
Immunofluorescence demonstrated that the percentage of complex I- and complex IV-deficient fibres was higher in patients with DYSF mutations than in age-matched controls. No clonally expanded mtDNA deletions were detected using long-range PCR in any of the analysed muscle fibres. Complex I and complex IV deficiency is higher in patients than age matched controls but patients do not have rearrangements of the mtDNA.
Data suggest that dysferlin exhibits modular architecture of 4 tertiary domains: 1) C2A, readily removed as solo domain; 2) midregion C2B-C2C-Fer (show FER ELISA Kits)-DysF, excised as intact module with several dynamic folding options; 3) C-terminal four-C2 domain module; 4) calpain-2 (show CAPN2 ELISA Kits)-cleaved mini-dysferlinC72, particularly resistant to proteolysis. Missense variant L344P in muscular dystrophy patient largely escapes proteasomal surveillance.
Human deltoid muscle biopsies of 5 Chilean dysferlinopathy patients exhibited the presence of muscular connexins (Cx40.1, Cx43 and Cx45).
This review suggested that the functions of dysferlin in vesicle trafficking and membrane remodeling in skeletal muscle.
DYSF expression is significantly upregulated in human masticatory mucosa during wound healing
DYSF mutations in Chinese patients clustered in the N-terminal region of the gene. Exonic rearrangements were found in 23% of patients with only one pathogenic mutation identified by Sanger sequencing or NGS. The novel mutations found in this study greatly expanded the mutational spectrum of dysferlinopathy.
This study showed that 4 patients with Inflammatory Myopathy associated with DYSF mutation.
results support a function for dysferlin as a calcium-sensing SNARE (show NAPA ELISA Kits) effector for membrane fusion events
C2 domains mediate high affinity self-association of dysferlin in a parallel homodimer
dysferlin mediates lysosome fusion to the plasma membrane and thereby leads to ASMase (show SMPD1 ELISA Kits) translocation, membrane raft clustering and NADPH oxidase (show NOX1 ELISA Kits) activation in coronary arterial endothelial cells, which consequently results in endothelial dysfunction
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.
dysferlin, limb girdle muscular dystrophy 2B (autosomal recessive)
, dysferlin variant a
, dystrophy-associated fer-1-like protein
, fer-1-like protein 1
, dystrophy-associated fer-1-like 1
, Dystrophy-associated fer-1-like protein
, Fer-1-like protein 1