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Human Caveolin 3 Protein expressed in Wheat germ - ABIN1348152
Sawada, Ishikawa, Tanji, Nakachi, Senba, Okudaira, Uchihara, Taira, Ohshiro, Yamada, Tanaka, Uezato, Ohshima, Sasai, Burgering, Duc Dodon, Fujii, Sunakawa, Mori: Overexpression of caveolin-1 in adult T-cell leukemia. in Blood 2010
Cav3 is involved in muscle development and is required for correct intracellular organization and myoblast fusion.
Data (including data from studies using recombinant proteins that lack typical in-vivo post-translational modifications such as palmitoylation) suggest Cav3 exhibits little tendency to partition into liquid-ordered domains of unilamellar vesicles.
MURC/cavin-4 (show MURC Proteins), especially in combination with Cav-3, may play a consistent role in the differentiation process of rhabdomyosarcoma.
This study demonstrated that cav3 mutation in stinct disorders including limb-girdle muscular dystrophy 1C, rippling muscle disease, and isolated creatine kinase elevation in Greece.
In a nonreferred nationwide Danish cohort of SIDS (show IDS Proteins) cases, up to 5/66 (7.5%) of SIDS (show IDS Proteins) cases can be explained by genetic variants in the sodium channel complex genes.
our results indicate that inhibition of Cav3 currents by 5,6-epoxyeicosatrienoic acid is an important mechanism controlling the vascular tone.
detrimental effect of Cav-3 V82I variant on cell viability may participate in determining the susceptibility to cardiac death.
The caveolin-3:p.T78M did not exhibit a long-QT syndrome phenotype.
Cav3 is an important negative regulator for cardiac late sodium cutrrent via nNOS (show NOS1 Proteins) dependent direct S-nitrosylation of SCN5A (show SCN5A Proteins).
data show a developmental change in HCN4 (show HCN4 Proteins)-Cav3 association in human embryonic stem cell-derived cardiomyocytes. Cav3 expression and its association with ionic channels likely represent a crucial step of cardiac maturation
A very high prevalence of previously SIDS (show IDS Proteins)-associated variants was identified in exome data from population studies.
Cav-3 overexpressing mice have changes in ECG intervals, heart rates, and cardiac ion channel expression
Loss of CAV3 interferes with downstream insulin (show INS Proteins) signaling and lipid uptake and increases susceptibility to palmitate-induced insulin (show INS Proteins) resistance.
eNOS (show NOS3 Proteins), caveolin-3, and connexin-43 (show GJA1 Proteins) were detected in subsarcolemmal mitochondria
Data show increased expression of T-type Ca(2 (show CA2 Proteins)+) current and association of protein kinase C alpha (PKCalpha (show PKCa Proteins)) with caveolin-3 (Cav-3)was disrupted in the hypertrophic ventricular myocyte.
Cardioprotection in myocardial infarction is abolished in caveolin-3 knockout mice.
The lithogenic diet was associated with significantly lower CAV3 in the liver and lower CAV3 and CCKAR in the gallbladder compared with the control mice.
Cav-3 may be a novel participant in B-cell expression, T-cell cytokine production and activation of inflammation
Cav3 protein can modify integrin function and mechanotransduction in the cardiomyocyte and intact heart
Deinactivation of Cav3 channels increases T-type Ca(2 (show CA2 Proteins)+) influx and increases feedback inhibition in olfactory bulb.
The Cav-1 (show CAV1 Proteins) and Cav-3 knockout mice exhibited enhanced lesion volume and cytokine/chemokine (show CCL1 Proteins) production after Traumatic brain injury.
cloned and characterized caveolin-3 from porcine muscle; caveolin-3 was expressed specifically in skeletal muscle & heart; first evidence that caveolin-3 has a certain regulated expression pattern during the prenatal period of skeletal muscle development
This gene encodes a caveolin family member, which functions as a component of the caveolae plasma membranes found in most cell types. Caveolin proteins are proposed to be scaffolding proteins for organizing and concentrating certain caveolin-interacting molecules. Mutations identified in this gene lead to interference with protein oligomerization or intra-cellular routing, disrupting caveolae formation and resulting in Limb-Girdle muscular dystrophy type-1C (LGMD-1C), hyperCKemia or rippling muscle disease (RMD). Alternative splicing has been identified for this locus, with inclusion or exclusion of a differentially spliced intron. In addition, transcripts utilize multiple polyA sites and contain two potential translation initiation sites.
, calveolin 3
, caveolin 3