Linked Life Data

11495928

Source:http://linkedlifedata.com/resource/pubmed/id/11495928

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
45
pubmed:dateCreated
2001-11-5
pubmed:databankReference
pubmed:abstractText
The 116-kDa a-subunit of the vacuolar proton pump (H(+)-ATPase) exists as several isoforms encoded by different genes and with different patterns of tissue expression. Its function within the multisubunit pump complex has yet to be elucidated. To date, three isoforms have been identified in mouse (designated a1-a3). We now report the cloning and characterization of Atp6n1b, encoding a novel fourth murine isoform (a4). Murine a4 has 833 residues and shows 85% amino acid identity to the human kidney-specific ATP6N1B protein in which loss-of-function alterations cause autosomal recessive distal renal tubular acidosis. The human and murine genes have similar genomic organization; furthermore, Atp6n1b maps to a region of mouse chromosome 6 that is syntenic with the segment of human 7q33-34 containing ATP6N1B. Together these findings establish the two genes as orthologs. The mouse a4 protein is 61, 52, and 47% identical to a1, a2, and a3, respectively. Phylogenetic analysis confirms that among vertebrates there are four a-subunit families, with a4 most resembling a1. Northern blot analysis of Atp6n1b reveals a 3.7-kilobase a4 transcript in kidney but not other major organs, and a reverse transcription polymerase chain reaction in 12 mouse tissues detects expression in kidney alone. Immunofluorescence studies in murine kidney demonstrate high intensity a4 staining at the surface of intercalated cells, with additional expression in the proximal tubule (not previously reported in human kidney). Similar apical a4 immunostaining is also present in male genital tissue. Identification of this novel murine kidney-enriched 116-kDa a-subunit provides a molecular tool for investigation of the currently unknown role of this protein, which is essential for proper function of the apical renal vacuolar H(+)-ATPase in man.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
9
pubmed:volume
276
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
42382-8
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed-meshheading:11495928-Amino Acid Sequence, pubmed-meshheading:11495928-Animals, pubmed-meshheading:11495928-Aquaporin 2, pubmed-meshheading:11495928-Aquaporin 6, pubmed-meshheading:11495928-Aquaporins, pubmed-meshheading:11495928-Chromosome Mapping, pubmed-meshheading:11495928-Cloning, Molecular, pubmed-meshheading:11495928-Mice, pubmed-meshheading:11495928-Molecular Sequence Data, pubmed-meshheading:11495928-Phylogeny, pubmed-meshheading:11495928-Polymorphism, Genetic, pubmed-meshheading:11495928-Pregnancy Proteins, pubmed-meshheading:11495928-Protein Subunits, pubmed-meshheading:11495928-Proton Pumps, pubmed-meshheading:11495928-Proton-Translocating ATPases, pubmed-meshheading:11495928-Reverse Transcriptase Polymerase Chain Reaction, pubmed-meshheading:11495928-Suppressor Factors, Immunologic
pubmed:year
2001
pubmed:articleTitle
Molecular cloning and characterization of Atp6n1b: a novel fourth murine vacuolar H+-ATPase a-subunit gene.
pubmed:affiliation
Department of Medical Genetics, Cambridge Institute for Medical Research, Box 139 Addenbrooke's Hospital, Cambridge CB2 2XY, United Kingdom.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't