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In summary, the APA (zeige ENPEP ELISA Kits)-associated ATP2B3(Leu425_Val426del) mutant promotes aldosterone production by at least 2 different mechanisms: 1) a reduced Ca(2 (zeige CA2 ELISA Kits)+) export due to the loss of the physiological pump function; and 2) an increased Ca(2 (zeige CA2 ELISA Kits)+) influx due to opening of depolarization-activated Ca(2 (zeige CA2 ELISA Kits)+) channels as well as a possible Ca(2 (zeige CA2 ELISA Kits)+) leak through the mutated pump.
Mutations in ATP2B3 gene is associated with aldosterone-producing adenomas.
Different mutations (KCNJ5 (zeige KCNJ5 ELISA Kits), ATP1A1 (zeige ATP1A1 ELISA Kits), ATP2B3, and CACNA1D (zeige CACNA1D ELISA Kits)) are found in different aldosterone-producing nodules from the same adrenal, suggesting that somatic mutations are independent events triggered by mechanisms that remain to be identified.
Novel PMCA3 missense mutation co-occurring with a heterozygous mutation in LAMA1 impaired cellular Ca2+ homeostasis in patients with Cerebellar Ataxia.
Somatic mutations found in KCNJ5 (zeige KCNJ5 ELISA Kits), ATP1A1 (zeige ATP1A1 ELISA Kits), and ATP2B3 appear to be the driving forces for a higher aldosterone production and proliferations of glomerulosa cells.
ATP2B3 mutations are present in aldosterone-producineg adenomas that result in an increase in CYP11B2 (zeige CYP11B2 ELISA Kits) gene expression and may account for the dysregulated aldosterone production in a subset of patients with sporadic primary aldosteronism.
Somatic mutations in ATP2B3 gene leads to aldosterone-producing adenomas and secondary hypertension.
Mutation of plasma membrane Ca2+ ATPase isoform 3 in a family with X-linked congenital cerebellar ataxia impairs Ca2 (zeige CA2 ELISA Kits)+ homeostasis.
role in the intracellular Ca(2 (zeige CA2 ELISA Kits)+) extrusion of syncytiotrophoblast-like structure originating from the differentiation of cultured trophoblast cells isolated from human term placenta
Expression of the placental calcium transporter PMCA3 mRNA predicts neonatal whole body bone mineral content
The protein encoded by this gene belongs to the family of P-type primary ion transport ATPases characterized by the formation of an aspartyl phosphate intermediate during the reaction cycle. These enzymes remove bivalent calcium ions from eukaryotic cells against very large concentration gradients and play a critical role in intracellular calcium homeostasis. The mammalian plasma membrane calcium ATPase isoforms are encoded by at least four separate genes and the diversity of these enzymes is further increased by alternative splicing of transcripts. The expression of different isoforms and splice variants is regulated in a developmental, tissue- and cell type-specific manner, suggesting that these pumps are functionally adapted to the physiological needs of particular cells and tissues. This gene encodes the plasma membrane calcium ATPase isoform 3. Alternatively spliced transcript variants encoding different isoforms have been identified.
ATPase, Ca++ transporting, plasma membrane 3
, plasma membrane calcium ATPase-like
, plasma membrane calcium ATPase
, plasma membrane calcium pump
, plasma membrane calcium-transporting ATPase 3
, plasma membrane calcium ATPase 3
, plasma membrane calcium ATPase 3a