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a novel heterozygous intronic mutation (c.639 + 1G>A) in the ATP6V0A4 gene was identified along with a heterozygous nonsense variant (c.580C>T, p.Arg194*).
The p. P137S and p. R302W mutations in ATP6V1B1 and p. S473F and p. R807X in ATP6V0A4, were novel disease-causing mutations of distal renal tubular acidosis.
Distal renal acidosis patient carries two novel mutations, one in each of the genes ATP6V0A4 and ATP6V1B1.
The aim of this work was to analyze the prevalence of genetic defects in SLC4A1, ATP6V0A4, 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.
ITM2A expression is positively regulated by PKA-CREB signaling and ITM2A expression interferes with autophagic flux by interacting with vacuolar ATPase.
e have described patients with severe distal renal tubular acidosis and a novel splicing mutation in the ATP6V0A4 gene in a family originating from the Siliana region in northwestern Tunisia
Functional analysis of selected regulated proteins revealed that knockdown of HNRPD, PHB2 and UB2V2 can increase HCMV replication, while knockdown of A4 and KSRP resulted in decreased HCMV replication.
For the remaining patients, two mutations in the ATP6V0A4 gene, one of them being novel, were found in three Tunisian cases.
Two from different families carrying ATP6V0A4 mutations manifested early onset moderate mixed HL and moderate SNHL
Mutations of the ATP6V0A4 gene is associated with primary distal renal tubular acidosis.
Case Report: novel ATP6V0A4 gene mutation confirmed autosomal recessive distal renal tubular acidosis with normal hearing.
The function of vacuolar ATPase (V-ATPase) a subunit isoforms in invasiveness of MCF10a and MCF10CA1a human breast cancer cells.
Four mutations in the ATP6V0A4 gene were obesrved one single nucleotide deletion in exon 13, the nonsensein exon 3, and the missense changes in exon 17 and in exon 19.
This study demonistrated that expression identifies subtypes of oligodendrogliomas, pilocytic astrocytomas and gangliogliomas and may contribute to refine characterization of these tumors.
There is the first evidence presented with progressive hearing loss associated with ATP6VOA4 mutation in a chinese patient.
Novel compound heterozygous ATP6V0A4 mutations in an infant with distal renal tubular acidosis.
stability and function of the metabolon composed of H+ATPase and glycolytic components can be compromised by either loss of required PFK-1 binding (G820R) or loss of pump protein (R807Q)
the a4 isoform may be responsible for targeting V-ATPases to the plasma membrane of MB231 cells and that cell surface V-ATPases play a significant role in breast cancer invasion
Mutations in ATP6V0A4 present enlarged vestibular aqueduct and early onset sensorial hearing loss.
The identification of novel locations for the a4 subunit and other tissue-restricted subunits increases the range of unique subunit combinations making up the proton pump.
The first detailed analysis of the structure and function of the auditory system in Atp6v0a4(-/-) knockout mice, is reported.
V-ATPase a4 knockout mice suffer not only from severe acidosis but also from proximal tubule dysfunction with defective endocytic trafficking, proteinuria, phosphaturia and accumulation of lysosomal material.
Atp6v0a4 knockout mouse is a model of distal renal tubular acidosis with hearing loss, with additional extrarenal phenotype
Immunolocalization demonstrated expression of all 'a' subunits in the proximal tubule and in the intercalated cells of the collecting system. PCR detected mRNAs encoding all four 'a' isoforms with a relative abundance in the following order: a4>a2=a1>a3.
Data suggestthat Foxi1 is necessary for expression of at least four subunits in three different epithelia and most likely is a major determinant for proper assembly of a functional vacuolar H(+)-ATPase complex at these locations.
This gene encodes a component of vacuolar ATPase (V-ATPase), a multisubunit enzyme that mediates acidification of intracellular compartments of eukaryotic cells. V-ATPase dependent 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. This gene is one of four genes in man and mouse that encode different isoforms of the a subunit. Alternatively spliced transcript variants encoding the same protein have been described. Mutations in this gene are associated with renal tubular acidosis associated with preserved hearing.
ATPase, H+ transporting, lysosomal (vacuolar proton pump) non-catalytic accessory protein 1B
, ATPase, H+ transporting, lysosomal (vacuolar proton pump) non-catalytic accessory protein 2 (38kD)
, H(+)-transporting two-sector ATPase, noncatalytic accessory protein 1B
, V-ATPase 116 kDa
, V-type proton ATPase 116 kDa subunit a
, V-type proton ATPase 116 kDa subunit a isoform 4
, vacuolar proton pump 116 kDa accessory subunit
, vacuolar proton pump, subunit 2
, vacuolar proton translocating ATPase 116 kDa subunit a kidney isoform
, ATPase, H+ transporting, lysosomal (vacuolar proton pump) noncatalytic accessory protein 1B
, V-ATPase alpha 4
, vacuolar proton translocating ATPase 100 kDa a4 subunit