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Distal renal acidosis patient carries two novel mutations, one in each of the genes ATP6V0A4 (show ATP6V0A4 Proteins) and ATP6V1B1.
A novel c.1169dupC frameshift mutation of ATP6V1B1 gene was identified in one family and the c.1155dupC North African mutation in 2 other families. Both mutations are located in exon 12 of ATP6V1B1 gene in Moroccan patients with recessive form of distal renal tubular acidosis associated with precocious hearing loss.
The aim of this work was to analyze the prevalence of genetic defects in SLC4A1 (show SLC4A1 Proteins), ATP6V0A4 (show ATP6V0A4 Proteins), and ATP6V1B1 genes and to assess the clinical phenotype of distal renal tubular acidosis patients that are eventually typical of the different genetic forms of the disease.
Our data indicate that recurrent stone formers with the vacuolar H(+)-ATPase (show ATP6V1B2 Proteins) B1 subunit p.E161K SNP exhibit a urinary acidification deficit with an increased prevalence of calcium phosphate-containing kidney stones
ATP6V1B1 genetic mutations were detected in more than half of the families studied. Mutations in this gene therefore seem to be the most common causative factors in hearing loss associated with distal renal tubular acidosis in these families.
Two founder mutations in the ATP6V1B1 gene were found in 16/27 dRTA cases.
Two probands from different kindreds with mutations in ATP6V1B1 presented early onset profound sensorineural hearing loss
Rare and family-specific variants in ATP6V1B1 are responsible for distal renal tubular acidosis and sensorineural hearing loss syndrome in Turkey.
Mutations of the ATP6V1B1 gene is associated with primary distal renal tubular acidosis.
Three ATP6V1B1 mutations were observed: one frameshift mutation in exon 12; a G to C single nucleotide substitution, on the acceptor splicing site in intron 2, and one novel missense mutation in exon 11.
vH(+)-ATPase has been detected in the cell membrane and in intracellular pools in bovine rumen epithelium.
1) Atp6v1b1+/- mice developed a mild incomplete dRTA. dRTA is partly compensated by respiration. 2) Compensatory mechanisms for the absence of B1 take place only in the collecting duct of Atp6v1b1-/- kidneys.
Because MRL-Atp6v1b1vxt/vtx mice do not recapitulate the metabolic acidosis of dRTA patients, they provide a new genetic model for nonsyndromic deafness with enlarged vestibular aqueduct (EVA (show MPZL2 Proteins); OMIM #600791).
Dot1l (show DOT1L Proteins) is a new epigenetic regulator of principal cells and intercalated cell differentiation and Atp6v1b1 is a new transcriptional target of Dot1l (show DOT1L Proteins).
Aldosterone increases V-ATPase-dependent proton secretion in clear cells in the caput epididymis via MR/NR3C2 and PKC activation.
Data conclude that V-ATPase (show ATP6V1H Proteins)-mediated H(+) secretion in the olfactory epithelium is required for optimal olfactory function.
Provide comprehensive protein expression profiles of specialized V-ATPase-B1-expressing cells in the kidney and epididymis.
Redistribution of Atp6v1b2 (show ATP6V1B2 Proteins) occurs from intracellular compartments into the apical membrane of epididymal clear cells from Atp6v1b1(-/-) mice.
In mice that lack a functional B1 subunit of the V-ATPase (show ATP6V1H Proteins), sAC (show ADCY10 Proteins) was colocalized apically in A-IC along with V-ATPase (show ATP6V1H Proteins) containing the alternative B2 subunit isoform.
Gene ablation abolished the enhanced urinary acidification stimulated by exposure of dissected outer medullary collecting ducts to high (5.0 mM) extracellular Ca(2 (show CA2 Proteins)+).
This gene encodes a component of vacuolar ATPase (V-ATPase), a multisubunit enzyme that mediates acidification of eukaryotic intracellular organelles. V-ATPase dependent organelle acidification is necessary for such intracellular processes as protein sorting, zymogen activation, receptor-mediated endocytosis, and synaptic vesicle proton gradient generation. V-ATPase is composed of a cytosolic V1 domain and a transmembrane V0 domain. The V1 domain consists of three A and three B subunits, two G subunits plus the C, D, E, F, and H subunits. The V1 domain contains the ATP catalytic site. The V0 domain consists of five different subunits: a, c, c', c'', and d. Additional isoforms of many of the V1 and V0 subunit proteins are encoded by multiple genes or alternatively spliced transcript variants. This encoded protein is one of two V1 domain B subunit isoforms and is found in the kidney. Mutations in this gene cause distal renal tubular acidosis associated with sensorineural deafness.
H(+)-transporting two-sector ATPase, 58kD subunit
, H+-ATPase beta 1 subunit
, V-ATPase B1 subunit
, V-ATPase subunit B 1
, V-type proton ATPase subunit B, kidney isoform
, endomembrane proton pump 58 kDa subunit
, vacuolar proton pump 3
, vacuolar proton pump subunit B 1
, vacuolar proton pump, subunit 3
, ATPase, H+ transporting, V1 subunit B1
, ATPase, H+ transporting, lysosomal 56/58kDa, V1 subunit B1 (Renal tubular acidosis with deafness)
, vacuolar H+-ATPase
, ATPase, H+ transporting, V1 subunit B
, ATPase, H+ transporting, lysosomal (vacuolar proton pump), beta 56/58 kDa
, ATPase, H+ transporting, lysosomal 56/58kDa, V1 subunit B
, lysosomal 56/58kDa