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subcellular localization of dScgbeta dramatically changes during mitosis through possible association with tubulin (show TUBB Proteins); these observations point to a complex role of sarcoglycans in non-muscle tissues.
Clinical severity of limb-girdle muscular dystrophy type 2Emay be predicted by SGCB gene mutation and sarcoglycan (show SGCD Proteins) protein expression.
Defective assembly of sarcoglycan (show SGCD Proteins) complex in patients with beta-sarcoglycan gene mutations
beta-sarcoglycan and SPATA18 (show SPATA18 Proteins) may have a role in limb-girdle muscular dystrophy type 2E
While the quantity of beta-sarcoglycan was nearly normal in the limb girdle muscular dystrophy (LGMD)2E carrier, the levels of dysferlin protein were reduced to 50% of controls in the carriers of LGMD2B.
These data suggest that formation of the beta-delta-core may promote the export and deposition of sarcoglycan (show SGCD Proteins) subcomplexes at the plasma membrane, and therefore identifies a mechanism for sarcoglycan (show SGCD Proteins) transport.
The limb-girdle muscular dystrophy patients with beta-sarcoglycan deficient LGMD2E do not enable an accurate prediction of the genotype.
this study shows that the serglycin (show SRGN Proteins)-deficient mice are more susceptible to Trichinella spiralis infection and display an unbalanced immune response
beta-Sarcoglycan deficiency reduces atherosclerotic plaque formation in ApoE (show APOE Proteins)-knockout mouse model.
Data suggest that serglycin (show SRGN Proteins) proteoglycans play a role in extravasation as well as colonization and growth of metastatic cells.
serglycin (show SRGN Proteins) deficient mice exhibited elevated concentrations of serum LDL after feeding high-fat diet for 20 weeks.
serglycin (show SRGN Proteins) plays a critical role in the maturation of dense-core cytotoxic granules in cytotoxic lymphocytes and the trafficking and storage of perforin (show PRF1 Proteins) and granzyme B, whereas granzyme A (show GZMA Proteins) is unaffected
In Sgcb-null mice, severe morphological disruption was present from 4 weeks in both quadriceps and diaphragm, and included conspicuous deposition of extracellular matrix components.
Wild-type mast cells efficiently degraded exogenous or endogenously produced IL-13 (show IL13 Proteins) upon degranulation,whereas serglycin (show SRGN Proteins) -/- mast cells completely lacked this ability.
Dopamine storage increased during mast cell maturation from bone marrow precursors, and was dependent on the presence of serglycin (show SRGN Proteins).
Cells lacking mouse mast cell protease 6 exhibited similar defects in apoptosis as observed in serglycin (show SRGN Proteins)(-/-) cells, indicating that the pro-apoptotic function of serglycin (show SRGN Proteins) is due to downstream effects of proteases that are complex-bound to serglycin (show SRGN Proteins)
The PRG-1 (show PTGR1 Proteins) transcription is initiated at multiple transcription start site and no influence on expression in vivo by Nex1 (show NEUROD6 Proteins) deficiency.
This gene encodes a member of the sarcoglycan family. Sarcoglycans are transmembrane components in the dystrophin-glycoprotein complex which help stabilize the muscle fiber membranes and link the muscle cytoskeleton to the extracellular matrix. Mutations in this gene have been associated with limb-girdle muscular dystrophy.
, SarcoGlycaN family member (sgn-1)
, Guanylate cyclase soluble alpha 1 (GTP pyrophosphate - lyase)
, Guanylate cyclase, soluble, alpha 1 (GTP pyrophosphate - lyase)
, guanylate cyclase soluble subunit alpha-3
, soluble guanylate cyclase large subunit
, 43 kDa dystrophin-associated glycoprotein
, beta-sarcoglycan(43kD dystrophin-associated glycoprotein)
, limb girdle muscular dystrophy 2E (non-linked families)
, sarcoglycan, beta (43kD dystrophin-associated glycoprotein)
, mastocytoma proteoglycan core protein
, proteoglycan 1, secretory granule
, proteoglycan, secretory granule
, secretory granule proteoglycan core protein