Il n’y a pas de produits dans votre liste de comparaison.
Votre panier est vide.
Afficher tous les synonymes
Sélectionnez vos espèces d'intérêt
We describe herein eight new pediatric cases of Relapsing Encephalopathy with Cerebellar Ataxia with the causal substitution always located at position 756
the de novo ATP1A3 variant can cause postlingual-onset auditory synaptopathy, making this gene a significant contributor to sporadic progressive ANSD and a biomarker ensuring favorable short-term CI outcomes.
the CAPOS mutation caused a weaker voltage dependence of the pumping rate and a stronger inhibition by cytoplasmic K(+) than the WT enzyme, which together with the reduced Na(+) affinity of the cytoplasmic-facing sites precluded proper pump activation under physiological conditions.
ATP1A3 gene is the main causative gene of AHC. Three hotspot mutations, D801N, E815K and G947R, were found. Hotspot mutation E815K is associated with the most severe phenotype, which presented an earlier age at the time of the first paroxysmal manifestation and first hemiplegic event, severer developmental delay and a greater proportion of epilepsy
Molecular modelling and in vitro electrophysiological studies of the specific CAPOS mutation were performed. Heterologous expression studies of ATP1A3 with the p.Glu818Lys mutation affects sodium binding to, and release from, the sodium-specific site in the pump, the third ion-binding site.
sequencing analysis of ATP1A3 gene was performed, showing a trinucleotide deletion c.2266_2268delGAC p.(D756del) (NM_001256214).
we describe 7 patients with 6 different de novo ATP1A3 mutations...which confirm that ATP1A3-related neurological disorders make up a phenotypic continuum rather than overlapping syndromes
Patients with R756L and R756C protein variants display more prominent ataxia, overlapping with the relapsing encephalopathy with cerebellar ataxia syndrome.
Germline mosaicism for ATP1A3 mutations is a likely explanation for familial recurrence and should be considered during recurrence risk counseling for families of children with ATP1A3-related disorders.
conclude that the de novo G316S mutation in ATP1A3 likely causes or contributes to patient symptoms. More broadly, we conclude that, for conserved genes, it is possible to rapidly and easily model human diseases in C. elegans using CRIPSR/Cas9 genome editing
study confirms that the specific c.2452G>A mutation in the ATP1A3 gene is associated with the CAPOS syndrome in pedigrees of different ethnic backgrounds; also the first report showing the co-occurrence of hemiplegic migraine and CAPOS syndrome in a patient with ATP1A3 mutations
Our results, demonstrate a highly variable clinical phenotype in patients with alternating hemiplegia of childhood that correlates with certain mutations and possibly clusters within the ATPase Na+/K+ transporting subunit alpha 3 gene.
nvestigated a large dystonia family from New Zealand in which only females were affected; found a novel, likely disease-causing, three base-pair deletion (c.443_445delGAG, p.Ser148del) in ATP1A3 in this family by combining genome and exome sequencing
Common variants of ATP1A3 were associated with susceptibility to generalized epilepsy in a Chinese population.
This study further expands the number and spectrum of ATP1A3 mutations associated with Alternating Hemiplegia of Childhood and confirms a more deleterious effect of the E815K mutation on selected neurologic outcomes.
This study demonstrated that the ATP1A3 protein was altered in auditory cortex patient with schizophreia.
interactions of alpha3-NKA with extracellular alpha-syn assemblies reduce its pumping activity as its mutations in RDP/AHC.
Alternating hemiplegia of childhood is a rare disorder caused by de novo mutations in the ATP1A3 gene, expressed in neurons and cardiomyocytes.
The amylospheroids target is neuron-specific Na(+)/K(+)-ATPase alpha3 subunit (NAKalpha3).
Report tumor cell sensitivity to cardiac glycosides depends on pattern of expression of alpha1-, alpha2-, or alpha3-isoforms of Na-K-ATPase.
the neuronal specific alpha3 (alpha3)-subunit of the plasma membrane enzyme Na, K-ATPase (NKA) is a new binding partner of sAPPalpha.
A heterozygous knock-in mouse harboring the D801Y mutation in ATP1A3 was generated. This mice displayed hyperactivity, increased sensitivity to chemically induced epileptic seizures and cognitive deficits. The findings reveal the functional significance of ATP1A3 gene in the control of spatial learning and memory and suggest a link to GABA transmission.
Knockout of sodium pump alpha3 subunit gene (Atp1a3(-/-)) results in perinatal seizure and defective respiratory rhythm generation
Mice harboring a heterozygous hot spot disease mutation, D801Y suffer abrupt hypothermia-induced dystonia. D-to-Y mutation abolished pump-mediated Na+/K+ exchange.
Study identified the Na+/K+-ATPase alpha 1 and 3 subunits as receptors for the extracellular fragment of GPNMB that mediates activation of cellular signaling pathways and subsequent neuroprotective effects.
Myshkin mice carrying a wild-type Atp1a3 transgene that confers a 16 % increase in brain-specific total Na(+),K(+)-ATPase activity show significant phenotypic improvements compared with non-transgenic Myshkin mice.
Heterozygous Myshkin mice have an amino acid change (I810N) in Na+,K+-ATPase alpha3 and deficits in learning and memory consistent with the cognitive impairment of the vast majority of Alternating Hemiplegia of Childhood patients
findings show Atp1a3-deficient heterozygotes exhibited shorter stride length at 4 weeks of age without stress and at later stages under chronic restraint stress; Atp1a3 was widely expressed in the brain and spinal cord of young mice; expression pattern was compatible with movement abnormalities under lack of one of alleles
These results shed light on the role of Atp1a3 in the inhibitory synapse, and potential involvement of inhibitory synaptic dysfunction for the pathophysiology of dystonia.
The results reveled that the NKAalpha3 subunit is found within gamma-motoneurons of spinal cord.
Increased Atp1a3 protein levels in the hippocampus provide evidence for its possible role in mechanisms that parallel memory training.
We found that a mutation that decreases neuronal Na(+) ,K(+) -ATPase activity interacts with stress to exacerbate depression.
Retinoschisin, the protein involved in the pathogenesis of X-linked juvenile retinoschisis, membrane association is severely impaired in the absence of ATP1A3 and ATP1B2.
Stress induced deficits in motor coordination and balance in female Atp1a3 mutant (Het) mice. These mice also exhibited decreased thermal sensitivity, as well as altered circling patterns and monoamine systems.
Data show that ATP1alpha(3) is widely expressed in neuronal populations but mainly in GABAergic neurons in areas and nuclei related to movement control, in agreement with rapid-onset of dystonia parkinsonism symptoms.
These data demonstrate that, through its interaction with the alpha3 sodium-potassium ATPase, agrin regulates activity-dependent processes in neurons, providing a molecular framework for agrin action in the CNS.
Learning and memory deficits observed in Na,K-ATPase alpha2 and alpha3 mice reveal Na,K-ATPase to be an important factor in the functioning of pathways associated with spatial learning.
while ATP1A3-isoforms regulate sodium and potassium homeostasis in subicular interneurones, ATP1A1-isoforms assume this function in pyramidal cells
studies of the behavioral aspects of alpha1, alpha2, and alpha 3 deficient mice show that haploinsufficiency of both alpha2 and alpha 3 isoforms result in behavioral defects.
the basal frequency of myocyte contraction depends on endogenous agrin-alpha3 Na,K-ATPase interaction
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.
Molecular cloning and sequence of the porcine ATP1A3 promoter.
preparations of Na+,K(+)-ATPase isozymes from calf brain that contain catalytic subunits of three types (alpha 1, alpha 2, and alpha 3) were obtained.The real isozyme composition of the Na+ pump from the grey matter and the brain stem was determined.
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 3 subunit. Alternatively spliced transcript variants encoding different isoforms have been found for this gene.
Na(+)/K(+) ATPase alpha(III) subunit
, Na(+)/K(+) ATPase alpha-3 subunit
, Na+/K+ ATPase 3
, sodium pump subunit alpha-3
, sodium-potassium ATPase catalytic subunit alpha-3
, sodium-potassium-ATPase, alpha 3 polypeptide
, sodium/potassium-transporting ATPase alpha-3 chain
, sodium/potassium-transporting ATPase subunit alpha-3
, ATPase, Na+K+ transporting, alpha 3 subunit
, Na+/K+ -ATPase alpha 3 subunit
, Na /K transporting alpha 3 polypeptide
, ATPase, Na+/K+ transporting, alpha 3 polypeptide