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

doi:10.1080/15216549900201333

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 journal › Article › peer-review

16 Citations (Scopus)

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.

Original language	English
Pages (from-to)	309-318
Number of pages	10
Journal	Biochemistry and Molecular Biology International
Volume	47
Issue number	2
DOIs	https://doi.org/10.1080/15216549900201333
Publication status	Published - 1999 Feb
Externally published	Yes

Keywords

Aquaporin
Glycerol
Rat liver
Urea

ASJC Scopus subject areas

Biochemistry
Molecular Biology
Genetics

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10.1080/15216549900201333

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title = "Cloning and functional expression of rAQP9L a new member of aquaporin family from rat liver",

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.",

keywords = "Aquaporin, Glycerol, Rat liver, Urea",

author = "Ko, {Shigeru B.H.} and Shinichi Uchida and Satoru Naruse and Michio Kuwahara and Kenichi Ishibashi and Fumiaki Marumo and Tetsuo Hayakawa and Sei Sasaki",

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AU - Ko, Shigeru B.H.

AU - Uchida, Shinichi

AU - Naruse, Satoru

AU - Kuwahara, Michio

AU - Ishibashi, Kenichi

AU - Marumo, Fumiaki

AU - Hayakawa, Tetsuo

AU - Sasaki, Sei

PY - 1999/2

Y1 - 1999/2

N2 - 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.

AB - 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.

KW - Aquaporin

KW - Glycerol

KW - Rat liver

KW - Urea

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

Abstract

Keywords

ASJC Scopus subject areas

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