Cloning and functional expression of rAQP9L a new member of aquaporin family from rat liver

Shigeru B.H. Ko, Shinichi Uchida, Satoru Naruse, Michio Kuwahara, Kenichi Ishibashi, Fumiaki Marumo, Tetsuo Hayakawa, Sei Sasaki

Research output: Contribution to journalArticlepeer-review

58 Citations (Scopus)


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.

Original languageEnglish
Pages (from-to)309-318
Number of pages10
JournalBiochemistry and Molecular Biology International
Issue number2
Publication statusPublished - 1999 Feb
Externally publishedYes


  • Aquaporin
  • Glycerol
  • Rat liver
  • Urea

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Genetics


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