| Literature DB >> 10205677 |
S B Ko1, S Uchida, S Naruse, M Kuwahara, K Ishibashi, F Marumo, T Hayakawa, S Sasaki.
Abstract
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.Entities:
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Year: 1999 PMID： 10205677 DOI： 10.1080/15216549900201333
Source DB: PubMed Journal: Biochem Mol Biol Int ISSN： 1039-9712