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rdf:type |
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lifeskim:mentions |
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pubmed:dateCreated |
2003-10-30
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pubmed:abstractText |
The multisubunit vacuolar-type proton-translocating ATPases (H(+)-ATPases) mediate the acidification of various intracellular organelles. In a subset of tissues, they also mediate H(+) secretion at the plasma membrane. Two isoforms of the H(+)-ATPase B-subunit exist in humans; we have shown that mutations in ATP6V1B1, encoding the B1-isoform, cause the clinical condition distal renal tubular acidosis. Here we report the cloning and characterization of murine Atp6v1b1, which encodes a 513-amino acid (aa) protein with 93% identity to human ATP6V1B1. Genomic organization is conserved between the murine and human H(+)-ATPase B1-subunits, and Atp6v1b1 maps to a region of mouse chromosome 6 syntenic to human 2p13, the location of ATP6V1B1. Northern blotting detects a 2.2-kb Atp6v1b1 transcript in the kidney and testis, but not other major organs. In mouse kidney, the B1-subunit localizes to intercalated cells of the cortical and medullary collecting duct. B1 protein levels were not increased in either mouse renal cortex or medulla after either 2 or 7 days of oral acid loading. These results demonstrate that Atp6v1b1 encodes the murine ortholog of human ATP6V1B1 and provides a tool for future development of animal models based on manipulation of the Atp6v1b1 genomic locus.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Oct
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pubmed:issn |
0378-1119
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
30
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pubmed:volume |
318
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
25-34
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:14585495-5' Flanking Region,
pubmed-meshheading:14585495-Amino Acid Sequence,
pubmed-meshheading:14585495-Animals,
pubmed-meshheading:14585495-Antibody Specificity,
pubmed-meshheading:14585495-Base Sequence,
pubmed-meshheading:14585495-Cloning, Molecular,
pubmed-meshheading:14585495-DNA,
pubmed-meshheading:14585495-DNA, Complementary,
pubmed-meshheading:14585495-Epididymis,
pubmed-meshheading:14585495-Gene Expression Regulation, Enzymologic,
pubmed-meshheading:14585495-Humans,
pubmed-meshheading:14585495-Immune Sera,
pubmed-meshheading:14585495-Immunohistochemistry,
pubmed-meshheading:14585495-Isoenzymes,
pubmed-meshheading:14585495-Kidney,
pubmed-meshheading:14585495-Male,
pubmed-meshheading:14585495-Mice,
pubmed-meshheading:14585495-Mice, Inbred Strains,
pubmed-meshheading:14585495-Molecular Sequence Data,
pubmed-meshheading:14585495-Phylogeny,
pubmed-meshheading:14585495-Protein Subunits,
pubmed-meshheading:14585495-RNA, Messenger,
pubmed-meshheading:14585495-Sequence Alignment,
pubmed-meshheading:14585495-Sequence Analysis, DNA,
pubmed-meshheading:14585495-Sequence Homology, Amino Acid,
pubmed-meshheading:14585495-Sequence Homology, Nucleic Acid,
pubmed-meshheading:14585495-Vacuolar Proton-Translocating ATPases
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pubmed:year |
2003
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pubmed:articleTitle |
Molecular cloning and characterization of Atp6v1b1, the murine vacuolar H+ -ATPase B1-subunit.
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pubmed:affiliation |
Department of Genetics, Yale University School of Medicine, New Haven, CT 06520-8005, USA.
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pubmed:publicationType |
Journal Article,
Comparative Study
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