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Human Polyclonal SNTA1 Primary Antibody for ELISA, WB - ABIN250089
Fernández-Larrea, Merlos-Suárez, Ureña, Baselga, Arribas: A role for a PDZ protein in the early secretory pathway for the targeting of proTGF-alpha to the cell surface. in Molecular cell 1999
Ordered disorder of the astrocytic dystrophin-associated protein complex in the norm and pathology.
High expression of Snta1 is associated with adipocyte hypertrophy and ectopic triglyceride deposition in obesity.
SNTA deficient mice are protected from fat loss and non-alcoholic steatohepatitis in the experimental methionine-choline-deficient model.
Data indicate that alpha-syntrophin plays an important role in the regulation of oxidative stress from endogenously generated reactive oxygen species (ROS) during myoblast differentiation by modulating the protein stability of catalase.
the function of SNTA has been analyzed in 3T3-L1 cells.
alpha-syntrophin plays a pivotal role in the survival pathway triggered by menadione-induced oxidative stress in cultured myoblasts.
Alpha-syntrophin deficiency markedly reduces astrocyte swelling during severe hypoosmotic stress/brain edema.
Isolated muscle bundles from SNTA1 mutant mice showed reduced force production after hypo-osmotic shock. In addition, the mutant muscle bundles showed delayed recovery of specific gravity after being exposed to hypo-osmotic conditions.
alpha-Syntrophin, which resides in nuclei of myocytes, functions as the upstream mediator of nuclear nNOS translocation and nNOS-dependent mitochondrial biogenesis.
the removal of the perivascular pool of AQP4 due to alpha-syntrophin deletion reduces edema formation, especially under pathological conditions and during states associated with elevated K+.
Scaffold proteins alpha-syntrophin and dystrophin exhibit lower densities in retinal microglia compared with brain astrocytes.
The interaction between the conserved COOH-terminal 125-amino acid domain (which is located in the light chains of MAP1A, MAP1B, and MAP1S) and alpha1-syntrophin is direct and occurs through the pleckstrin homology domain 2 (PH2).
Data show that in Dp71-null mice, the levels of beta-dystroglycan (beta-DG) and alpha1-syntrophin (alpha1-Syn) were lower and utrophin expression did not change, and the neuronal nitric oxide synthase (nNOS) expression and activity were increased.
We identified alpha1-syntrophin, a component of the dystrophin-associated protein complex (DAPC), as a myocilin-binding candidate.
Migration of myoblasts from alpha-syntrophin knockout mice could not be stimulated by HGF.
These results demonstrate that alpha-syn is required for the maturation and stability of the postsynaptic apparatus and suggest that alpha-syn may act via alpha-dbn1.
alpha-syntrophin plays an important role in regulating myogenesis by modulating myogenin expression
the first pleckstrin homology and PDZ domains of alpha-syntrophin work in concert to facilitate the localization of AChRs and nNOS at the neuromuscular junction
Alpha1-syntrophin knockout mice have skeletal muscle hypertrophy and aberrant formation of neuromuscular junctions during muscle regeneration
Aquaporin 4 and alpha1-syntrophin colocalized frequently at the astrocyte membrane, especially at the perivascular astrocyte endfoot processes
not associated with sudden infant death syndrome
Low SNTA expression is associated with non-alcoholic steatohepatitis but is unchanged in hepatocellular carcinoma.
A novel SNTA1 variant is likely causative for drug induced long-QT syndrome by augmenting the late sodium current.
In a nonreferred nationwide Danish cohort of SIDS cases, up to 5/66 (7.5%) of SIDS cases can be explained by genetic variants in the sodium channel complex genes.
our results present a possible mechanism of Rac1 activation involving SNTA1 and emphasise its role in ROS generation, cell migration, and acquisition of malignancy.
Calcium homeostasis mishandling in Duchenne muscular dystrophy myotubes depends on store operated calcium entry under the influence alpha1-syntrophin regulation as well as TRPV2-dependant cation influx.
The combined mutations of A261V-SNTA1 plus R800L-SCN5A increase the INa current late/peak ratio and time constants of current decay.
In contrast to stomach, lung, colon and rectal cancers, SNTA1 protein was found to be downregulated in esophageal cancers and upregulated in breast cancer.
alpha1D-adrenergic receptors are regulated by syntrophins through a PDZ domain-mediated interaction
These results establish an SNTA1-based nNOS complex attached to SCN5A as a key regulator of sodium current and suggest that SNTA1 be considered a rare long QT syndrome-susceptibility gene.
SNTA1 is a new susceptibility gene for LQTS. A257G-SNTA1 can cause gain-of-function of Na(v)1.5 similar to the LQT3.
Alpha1-syntrophin mutations identified in sudden infant death syndrome cause an increase in late cardiac sodium current.
Syntrophins are cytoplasmic peripheral membrane scaffold proteins that are components of the dystrophin-associated protein complex. This gene is a member of the syntrophin gene family and encodes the most common syntrophin isoform found in cardiac tissues. The N-terminal PDZ domain of this syntrophin protein interacts with the C-terminus of the pore-forming alpha subunit (SCN5A) of the cardiac sodium channel Nav1.5. This protein also associates cardiac sodium channels with the nitric oxide synthase-PMCA4b (plasma membrane Ca-ATPase subtype 4b) complex in cardiomyocytes. This gene is a susceptibility locus for Long-QT syndrome (LQT) - an inherited disorder associated with sudden cardiac death from arrhythmia - and sudden infant death syndrome (SIDS). This protein also associates with dystrophin and dystrophin-related proteins at the neuromuscular junction and alters intracellular calcium ion levels in muscle tissue.
syntrophin, alpha 1 (dystrophin-associated protein A1, 59kDa, acidic component)
, 59 kDa dystrophin-associated protein A1 acidic component 1
, acidic alpha 1 syntrophin
, dystrophin-associated protein A1, 59kDa, acidic component
, pro-TGF-alpha cytoplasmic domain-interacting protein 1
, syntrophin, acidic 1
, 59-1 DAP