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SGCA encodes a component of the dystrophin-glycoprotein complex (DGC), which is critical to the stability of muscle fiber membranes and to the linking of the actin cytoskeleton to the extracellular matrix. Additionally we are shipping SGCA Antibodies (57) and and many more products for this protein.
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Pathogenic mutations were found in SGCA from Egyptian families with limb-girdle muscular dystrophy.
IN TMD (show TTN Proteins) patients, a locus near the sarcoglycan (show SGCD Proteins) alpha ( SGCA), rs4794106, was suggestive in the discovery analysis ( P = 2.6 x 10(6)) and replicated (i.e., 1-tailed P = 0.016) in the Brazilian cohort.
The results suggest that the carrier rate of c.101G>T in SGCA may be high in Taiwan, especially in the aboriginal population regardless of the tribes.
Results show that HRD1 (show SYVN1 Proteins) and RFP2 (show TRIM13 Proteins) contributes are required for the disposal of V247M alpha-sarcoglycan mutant.
2 members of a Spanish family with muscular dystrophy had a new missense mutation c409G>A, p.Glu137Lys in exon 5 of the alpha-sarcoglycan gene, as well as a paternal c739G>A, p.Val24Met mutation inexon 6.
DNA analysis demonstrated homozygosity for a point mutation (574C>T) in the alpha-sarcoglycan gene.
E-cadherin,alpha-dystroglycan and beta-dystroglycan levels were decreased in the oesophageal primary tumour samples, despite the presence of normal levels of dystroglycan mRNA.
This study reported recessive founder LGMD2D for the Magdalen Islands, an archipelago (show FBXW7 Proteins) settled in the XIXth century, largely by Acadian immigrants.
Peptide sequences in alpha-DG are substrates for protein-O-mannose N-acetylglucosaminyltransferase (show GCNT2 Proteins) 1 (POMGnT1 (show POMGNT1 Proteins)), demonstrated when a library of mannopeptides is generated which corresponds to sequences of the mucin (show SLC13A2 Proteins)-like stem region of alpha-DG.
Long-term, sustainable gene expression of alpha-sarcoglycan was observed following gene transfer mediated by AAV.
The differential expression of two alpha-SG mRNAs during mouse embryonic development may be a consequence of the differential regulation of both promoters by myogenic and cardiogenic factors.
Loss of sarcoglycan (show SGCD Proteins) is associated with loss of miRNA669a and myopathy.
Sgca-;Sgce-null mouse shows a complete loss of residual sarcoglycans and a strong reduction in both dystrophin and dystroglycan.
Impaired proliferation of Sgca-null myogenic precursors was confirmed by single fiber analysis and this difference correlated with Sgca expression during myogenic progenitor cell proliferation.
Absence of members of the dystrophin (show DMD Proteins)-associated glycoprotein complex constitutes a permissive environment for spontaneous development of embryonal rhabdomyosarcoma associated with mutation of p53 (show TP53 Proteins) and mutation or altered splicing of Mdm2 (show MDM2 Proteins).
These findings suggest that the sarcoglycan (show SGCD Proteins) complex serves a mechanical function in the diaphragm by contributing to muscle passive stiffness and to the modulation of the contractile properties of the muscle.
Muscle masses were 40-100% larger for Sgca-null compared with age- and gender-matched wild-type mice, with the majority of the increased muscle mass for Sgca-null mice attributable to greater connective tissue and water contents
Diaphragm from Sgca-null mouse presents a clear dystrophic phenotype, with necrosis, regeneration, fibre hypertrophy and splitting, excess of collagen and fatty infiltration.
Deficiency of Sgca differently affects fast- and slow-twitch skeletal muscles.
The alpha-SG promoter is activated by MyoD (show MYOD1 Proteins), which interacts with TFIID (show TBP Proteins) and TFIIB (show GTF2B Proteins) in a protein complex differentially located at the distal promoter and around the proximal promoter during myogenic cell differentiation.
This gene encodes a component of the dystrophin-glycoprotein complex (DGC), which is critical to the stability of muscle fiber membranes and to the linking of the actin cytoskeleton to the extracellular matrix. Its expression is thought to be restricted to striated muscle. Mutations in this gene result in type 2D autosomal recessive limb-girdle muscular dystrophy. Multiple transcript variants encoding different isoforms have been found for this gene.
50 kDa dystrophin-associated glycoprotein
, 50kD DAG
, sarcoglycan, alpha (50kDa dystrophin-associated glycoprotein)