Cloning and characterization of the vasopressin-regulated urea transporter

Guofeng You; Craig P. Smith; Yoshikatsu Kanai; Wen Sen Lee; Matthias Stelzner; Matthias A. Hediger

doi:10.1038/365844a0

Cloning and characterization of the vasopressin-regulated urea transporter

Guofeng You, Craig P. Smith, Yoshikatsu Kanai, Wen Sen Lee, Matthias Stelzner, Matthias A. Hediger

Research output: Contribution to journal › Article › peer-review

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Abstract

UREA is the principal end product of nitrogen metabolism in mammals¹. Movement of urea across cell membranes was originally thought to occur by lipid-phase permeation, but recent studies have revealed the existence of specialized transporters with a low affinity for urea (K_m > 200 mM)². Here we report the isolation of a complementary DNA from rabbit renal medulla that encodes a 397-amino-acid membrane glycoprotein, UT2, with the functional characteristics of the vasopressin-sensitive urea transporter previously described in in vitro-perfused inner medullary collecting ducts^3,4. UT2 is not homologous to any known protein and displays a unique pattern of hydrophobicity. Because of the central role of this transporter in fluid balance^1,3-7 and nitrogen metabolism⁸, the study of this protein will provide important insights into the urinary concentrating mechanism and nitrogen balance.

Original language	English
Pages (from-to)	844-847
Number of pages	4
Journal	Nature
Volume	365
Issue number	6449
DOIs	https://doi.org/10.1038/365844a0
Publication status	Published - 1993
Externally published	Yes

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title = "Cloning and characterization of the vasopressin-regulated urea transporter",

abstract = "UREA is the principal end product of nitrogen metabolism in mammals1. Movement of urea across cell membranes was originally thought to occur by lipid-phase permeation, but recent studies have revealed the existence of specialized transporters with a low affinity for urea (Km > 200 mM)2. Here we report the isolation of a complementary DNA from rabbit renal medulla that encodes a 397-amino-acid membrane glycoprotein, UT2, with the functional characteristics of the vasopressin-sensitive urea transporter previously described in in vitro-perfused inner medullary collecting ducts3,4. UT2 is not homologous to any known protein and displays a unique pattern of hydrophobicity. Because of the central role of this transporter in fluid balance1,3-7 and nitrogen metabolism8, the study of this protein will provide important insights into the urinary concentrating mechanism and nitrogen balance.",

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T1 - Cloning and characterization of the vasopressin-regulated urea transporter

AU - You, Guofeng

AU - Smith, Craig P.

AU - Kanai, Yoshikatsu

AU - Lee, Wen Sen

AU - Stelzner, Matthias

AU - Hediger, Matthias A.

PY - 1993

Y1 - 1993

N2 - UREA is the principal end product of nitrogen metabolism in mammals1. Movement of urea across cell membranes was originally thought to occur by lipid-phase permeation, but recent studies have revealed the existence of specialized transporters with a low affinity for urea (Km > 200 mM)2. Here we report the isolation of a complementary DNA from rabbit renal medulla that encodes a 397-amino-acid membrane glycoprotein, UT2, with the functional characteristics of the vasopressin-sensitive urea transporter previously described in in vitro-perfused inner medullary collecting ducts3,4. UT2 is not homologous to any known protein and displays a unique pattern of hydrophobicity. Because of the central role of this transporter in fluid balance1,3-7 and nitrogen metabolism8, the study of this protein will provide important insights into the urinary concentrating mechanism and nitrogen balance.

AB - UREA is the principal end product of nitrogen metabolism in mammals1. Movement of urea across cell membranes was originally thought to occur by lipid-phase permeation, but recent studies have revealed the existence of specialized transporters with a low affinity for urea (Km > 200 mM)2. Here we report the isolation of a complementary DNA from rabbit renal medulla that encodes a 397-amino-acid membrane glycoprotein, UT2, with the functional characteristics of the vasopressin-sensitive urea transporter previously described in in vitro-perfused inner medullary collecting ducts3,4. UT2 is not homologous to any known protein and displays a unique pattern of hydrophobicity. Because of the central role of this transporter in fluid balance1,3-7 and nitrogen metabolism8, the study of this protein will provide important insights into the urinary concentrating mechanism and nitrogen balance.

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Cloning and characterization of the vasopressin-regulated urea transporter

Abstract

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