rdf:type |
|
lifeskim:mentions |
|
pubmed:issue |
2
|
pubmed:dateCreated |
1999-6-7
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pubmed:databankReference |
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pubmed:abstractText |
A new aquaporin was isolated from rat liver based on homology to known aquaporins. A 1408 bp cDNA was sequenced (designated rAQP9L) with a 885 bp open reading frame encoding a 295 amino acid hydrophobic protein. rAQP9L has the greatest amino-acid sequence identity with human AQP9 (75%) and a less homology with AQP3 (49%) and AQP7 (47%). Northern blot analysis indicated a 1.4-kb transcript expressed strongly in liver > testis > brain = lung. Expression of rAQP9L cRNA in Xenopus oocytes increased osmotic water permeability by 6-folds which was inhibited by 0.3 mM mercury chloride by 42%. rAQP9L also facilitated glycerol and urea transport by 2- and 5-folds, respectively. The large discrepancy of tissue distribution between hAQP9 and rAQP9L suggest that rAQP9L is a new aquaporin, which is involved in transport of urea as well as water in liver.
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pubmed:language |
eng
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pubmed:journal |
|
pubmed:citationSubset |
IM
|
pubmed:chemical |
|
pubmed:status |
MEDLINE
|
pubmed:month |
Feb
|
pubmed:issn |
1039-9712
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pubmed:author |
|
pubmed:issnType |
Print
|
pubmed:volume |
47
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
309-18
|
pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:10205677-Amino Acid Sequence,
pubmed-meshheading:10205677-Animals,
pubmed-meshheading:10205677-Aquaporins,
pubmed-meshheading:10205677-Base Sequence,
pubmed-meshheading:10205677-Biological Transport,
pubmed-meshheading:10205677-Cloning, Molecular,
pubmed-meshheading:10205677-Liver,
pubmed-meshheading:10205677-Mercuric Chloride,
pubmed-meshheading:10205677-Molecular Sequence Data,
pubmed-meshheading:10205677-Oocytes,
pubmed-meshheading:10205677-RNA, Messenger,
pubmed-meshheading:10205677-Rats,
pubmed-meshheading:10205677-Sequence Alignment,
pubmed-meshheading:10205677-Urea,
pubmed-meshheading:10205677-Water,
pubmed-meshheading:10205677-Xenopus
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pubmed:year |
1999
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pubmed:articleTitle |
Cloning and functional expression of rAOP9L a new member of aquaporin family from rat liver.
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pubmed:affiliation |
International Medicine II, Nagoya University School of Medicine, Japan.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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