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anti-Mouse (Murine) ATP1A2 Antikörper:
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proof of concept study demonstrates that reduced expression of the alpha2 isoform in the spinal cord is protective following spinal cord injury
Atp1a2 does contribute to alcohol-related behaviors, but the effect is modest with a clear dependence on sex.
Atp1alpha2 is preferentially expressed with Atp1beta2 in T-tubules of cardiac myocytes, forming alpha2beta2 heterodimers.
study provides evidence that muscle beta-catenin is crucial for maintenance of resting membrane potential(RMP)of skeletal muscle cells; muscle cells lacking beta-catenin show decreased expression of alpha2 subunit of Na,K-ATPase, a probable mechanism by which beta-catenin regulates RMP and affects normal function of skeletal muscle
Heart expression of alpha2 does not play a role in the regulation of basal cardiovascular function or blood pressure; however, heart expression of alpha2 plays a role in the hypertrophic response to pressure overload.
Atp1a2 has a more prominent role (vs. Atp1a1) in modulating cardiac myocyte sarcoplasmic reticulum Ca(2+) release.
The ouabain-binding site of either the alpha1 or alpha2 Na,K-ATPase subunit does not play an essential role in the development of DOCA-salt hypertension in a mouse model
Central sodium chloride causes hypertension in mice. The blood pressure response is mediated by the ouabain-like substance in the brain, specifically by its binding to the alpha(2)-isoform of the Na,K-ATPase.
Atp1a2 expression in heart and vascular smooth muscle is not essential for regulation of basal systolic blood pressure.
Ion channel NKCC1 and alpha2 Na, K-ATPase played important roles in the inner ear potassium recycling.
Both protein and mRNA expression of alpha1 and alpha2 isoforms of Na,K-ATPase and NKCC1 in the lateral wall were dramatically reduced following a long-term deafening
The cardiotonic steroid-binding site of the alpha2 Na,K-ATPase plays a role in maintaining normal SBP during pregnancy
The Na,K-ATPase alpha(2) subunit is expressed during development when the t-tubules form. These results suggest that the alpha(2) isoform may serve, in part, a physiological role in the muscle t-tubules.
Na,K-ATPase alpha2 isoform could be important in the modulation of neuronal activity in the neonate
Ca2+ signaling is regulated by the expression of this protein as studied in knockout mice
Heterozygote Atp1a2 mutant adult mice showed increased fear/anxiety behavior and enhanced neuronal activity in the amygdala and piriform cortex after conditioned fear stimuli; homozygotes died just post-birth and showed neuronal apoptosis in these regions
the alpha2 Na,K-ATPase isozyme mediates ouabain-induced cardiac contractility in mice
individual alpha-isoforms of the Na(+)/K(+)-ATPase differ functionally and that the alpha(2)-isoform couples more strongly to activation-relaxation pathways in vascular smooth muscle
the alpha2-isoform of Na-K-ATPase mediates the ouabain-induced increase in vascular contractility and could play a role in the development and maintenance of ouabain-induced hypertension.
We propose a model for functional coupling between the Na+, K+-ATPase alpha2 subunit and KCC2, which excludes Cl- from the cytosol in respiratory center neurons.
Data implicate ATP1A2 as a new hypokalaemic periodic paralysis gene and leak currents as a common pathomechanism of hypokalaemic periodic paralysis.
The sporadic hemiplegic migraine is caused mutation of ATP1A2 gene.
A novel p.Arg348Pro ATP1A2 mutation was found in 14 family members: 12 with clinical familial hemiplegic migraine (FHM), one with psychomotor retardation and possible FHM, and one without FHM features
On the other hand, the presence of KCNK18 mutation indicated another FHM subtype.
A missense variant of the ATP1A2 gene is associated with a novel phenotype of progressive sensorineural hearing loss associated with migraine
Report tumor cell sensitivity to cardiac glycosides depends on pattern of expression of alpha1-, alpha2-, or alpha3-isoforms of Na-K-ATPase.
Data indicate that a second-site mutation distant from Na+ site III increases Na+ affinity, Na(+),K(+)-ATPase activity, and cellular K+ uptake in mutants with the replacement of the aspartate.
genome-wide linkage analysis of the migraine phenotype in 38 families with Rolandic epilepsy; evidence found of linkage to migraine at chromosome 17q12-22 and suggestive evidence at 1q23.1-23.2, centering over the FHM2 locus
Three patients with a proven mutation in the ATP1A2 gene clinically presented without hemiparesis.
mutations in the ATP1A2 gene might contribute to pulmonary arterial remodelling and pulmonary arterial hypertension
Identification of a novel heterozygous mutation in the ATP1A2 gene (c.1766T>C, Ile589Thr) causing atypical alternating hemiplegia of childhood in a Saudi consanguineous family
In this family, benign familial infantile seizures (BFIS) are caused by a PRRT2 mutation and hemiplegic migraine by p.Arg689Gln ATPase ATP1A2 mutation.
The present study provides further evidence on the involvement of ATP1A2 mutations in both migraine and epilepsy, underlying the relevance of genetic analysis in families with a comorbidity of both disorders.
We describe a four-generation Italian family with familial hemiplegic migraine (FHM) and epilepsy due to a novel ATP1A2 missense mutation
Relationship between intracellular Na+ concentration and reduced Na+ affinity in Na+,K+-ATPase mutants causing neurological disease
genetic testing showed a mutation in the ATP1A2 gene OF two patients suffering from migraine with aura since youth
ATP1A2 missense mutations are associated with familial hemiplegic migraine.
Data indicate that (4-Chloro-2-(piperidin-1-yl)thiazol-5-yl)(phenyl)methanone and (4-bromo-2-(piperidin-1-yl)thiazol-5-yl)(phenyl)methanone inhibited cell growth through inhibition of both alpha-1 Na(+)/K(+)-ATPase (NAK) and Ras oncogene activity.
examined a family with a FHM phenotype due to a M731T mutation in ATP1A2. A 10-year follow-up allowed us to observe complex auras, including psychotic symptoms in two siblings
Skeletal muscle in elderly individuals was characterized by decreased NKA alpha(2) protein abundance, but unchanged [(3)H]ouabain binding.
biochemical and biophysical characteristics of the alpha(2)beta(1) isozyme of Na(+)/K(+)-ATPase from caveolae vesicles of pulmonary smooth muscle plasma membrane were studied during solubilization and purification
Na,K-ATPase alpha2 and Ncx4a regulate left-right patterning by modulating intracellular calcium levels in Kupffer's vesicle and by influencing cilia function
This observation is consistent with a major role of alpha2 in aqueous humor production and suggests that, potentially, alpha2-selective digoxin derivatives could be of interest as novel drugs for control of intraocular pressure.
Study reports the cloning and expression of Na, K-ATPase alpha2 (atp1a2) and alpha3 (atp1a3) subunits during Xenopus development and compare the expression patterns of each subunit.
The protein encoded by this gene belongs to the family of P-type cation transport ATPases, and to the subfamily of Na+/K+ -ATPases. Na+/K+ -ATPase is an integral membrane protein responsible for establishing and maintaining the electrochemical gradients of Na and K ions across the plasma membrane. These gradients are essential for osmoregulation, for sodium-coupled transport of a variety of organic and inorganic molecules, and for electrical excitability of nerve and muscle. This enzyme is composed of two subunits, a large catalytic subunit (alpha) and a smaller glycoprotein subunit (beta). The catalytic subunit of Na+/K+ -ATPase is encoded by multiple genes. This gene encodes an alpha 2 subunit. Mutations in this gene result in familial basilar or hemiplegic migraines, and in a rare syndrome known as alternating hemiplegia of childhood.
Na(+)/K(+) ATPase alpha(+) subunit
, Na(+)/K(+) ATPase alpha-2 subunit
, sodium pump subunit alpha-2
, sodium/potassium-transporting ATPase subunit alpha-2
, ATPase, Na+K+ transporting, alpha 2
, Na+/K+ -ATPase alpha 2 subunit
, Na+/K+ ATPase, alpha-A(+) catalytic polypeptide
, Na+/K+ ATPase, alpha-B polypeptide
, sodium-potassium ATPase catalytic subunit alpha-2
, sodium/potassium-transporting ATPase alpha-2 chain
, ATPase, Na+/K+ transporting, alpha 2 (+) polypeptide
, Na,K-ATPase alpha-2-subunit
, Na+/K+ transporting alpha 2 polypeptide
, Na,K-ATPase alpha 2 subunit
, Sodium pump subunit alpha-2
, ATPase, Na+/K+ transporting, alpha 2 polypeptide
, LOW QUALITY PROTEIN: sodium/potassium-transporting ATPase subunit alpha-2
, Na/K ATPase alpha 2 subunit
, ATPase, Na+/K+ transporting, alpha 2 polypeptide L homeolog
, ATPase, Na+/K+ transporting, alpha 2 polypeptide S homeolog
, ATPase Na+/K+ transporting subunit alpha 4
, sodium/potassium-transporting ATPase subunit alpha-4