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      Aquaporin water channels: unanswered questions and unresolved controversies

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          Abstract

          The long-standing biophysical question of how water crosses plasma membranes has been answered by the recent discovery of the aquaporins. Identification of this large family of membrane water-transport proteins has generated new questions about the physiological functions, tissue distributions, and regulatory mechanisms of individual aquaporins. The fast pace of developments in this field has also resulted in major discrepancies in published reports which warrant resolution.

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          Appearance of water channels in Xenopus oocytes expressing red cell CHIP28 protein.

          G. M. Preston, T. P. Carroll, W Guggino … (1992)
          Water rapidly crosses the plasma membrane of red blood cells (RBCs) and renal tubules through specialized channels. Although selective for water, the molecular structure of these channels is unknown. The CHIP28 protein is an abundant integral membrane protein in mammalian RBCs and renal proximal tubules and belongs to a family of membrane proteins with unknown functions. Oocytes from Xenopus laevis microinjected with in vitro-transcribed CHIP28 RNA exhibited increased osmotic water permeability; this was reversibly inhibited by mercuric chloride, a known inhibitor of water channels. Therefore it is likely that CHIP28 is a functional unit of membrane water channels.
          Article 0 comments Cited 136 times – based on 0 reviews     Review now
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            Cloning and expression of apical membrane water channel of rat kidney collecting tubule.

            Y Hirata, Masao Sasaki, S. Uchida … (1993)
            Concentrating urine is mandatory for most mammals to prevent water loss from the body. Concentrated urine is produced in response to vasopressin by the transepithelial recovery of water from the lumen of the kidney collecting tubule through highly water-permeable membranes. In this nephron segment, vasopressin regulates water permeability by endo- and exocytosis of water channels from or to the apical membrane. CHIP28 is a water channel in red blood cells and the kidney proximal tubule, but it is not expressed in the collecting tubule. Here we report the cloning of the complementary DNA for WCH-CD, a water channel of the apical membrane of the kidney collecting tubule. WCH-CD is 42% identical in amino-acid sequence to CHIP28. WCH-CD transcripts are detected only in the collecting tubule of the kidney. Immunohistochemically, WCH-CD is localized to the apical region of the kidney collecting tubule cells. Expression of WCH-CD in Xenopus oocytes markedly increases osmotic water permeability. The functional expression and the limited localization of WCH-CD to the apical region of the kidney collecting tubule suggest that WCH-CD is the vasopressin-regulated water channel.
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              Requirement of human renal water channel aquaporin-2 for vasopressin-dependent concentration of urine.

              P Deen, M A Verdijk, N. Knoers … (1994)
              Concentration of urine in mammals is regulated by the antidiuretic hormone vasopressin. Binding of vasopressin to its V2 receptor leads to the insertion of water channels in apical membranes of principal cells in collecting ducts. In nephrogenic diabetes insipidus (NDI), the kidney fails to concentrate urine in response to vasopressin. A male patient with an autosomal recessive form of NDI was found to be a compound heterozygote for two mutations in the gene encoding aquaporin-2, a water channel. Functional expression studies in Xenopus oocytes revealed that each mutation resulted in nonfunctional water channel proteins. Thus, aquaporin-2 is essential for vasopressin-dependent concentration of urine.
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                Author and article information

                Journal
                Journal ID (nlm-ta): Curr Opin Cell Biol
                Journal ID (iso-abbrev): Curr. Opin. Cell Biol
                Title: Current Opinion in Cell Biology
                Publisher: Published by Elsevier Ltd.
                ISSN (Print): 0955-0674
                ISSN (Electronic): 1879-0410
                Publication date PMC-release: 11 February 2002
                Publication date (Print): 1995
                Publication date (Electronic): 11 February 2002
                Volume: 7
                Issue: 4
                Pages: 472-483
                Affiliations
                [a ]Department of Biological Chemistry, Physiology Building Room 420, Johns Hopkins University School of Medicine, 725 North Wolfe Street, Baltimore, MD 21205-2185, USA.
                [b ]Renal Unit, Massachusetts General Hospital-East, 149 13th Street, Charlestown, MA 02129, USA.
                [c ]Department of Cell Biology, Institute of Anatomy, University of Aarhus, DK-8000 Aarhus C, Denmark.
                Author notes
                [* ]Author for correspondence: P Agre.
                Article
                Publisher ID: 0955-0674(95)80003-4
                DOI: 10.1016/0955-0674(95)80003-4
                PMC ID: 7135066
                PubMed ID: 7495566
                SO-VID: 53502206-040d-4580-bbf8-76b86c178594
                Copyright © Copyright © 1995 Published by Elsevier Ltd.
                License:

                Since January 2020 Elsevier has created a COVID-19 resource centre with free information in English and Mandarin on the novel coronavirus COVID-19. The COVID-19 resource centre is hosted on Elsevier Connect, the company's public news and information website. Elsevier hereby grants permission to make all its COVID-19-related research that is available on the COVID-19 resource centre - including this research content - immediately available in PubMed Central and other publicly funded repositories, such as the WHO COVID database with rights for unrestricted research re-use and analyses in any form or by any means with acknowledgement of the original source. These permissions are granted for free by Elsevier for as long as the COVID-19 resource centre remains active.

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                Subject: Article

                ScienceOpen disciplines: Cell biology
                Keywords: aqp—aquaporin,crna—complementary rna,mip—major intrinsinc protein of lens,pcr—polymerase chain reaction
                Data availability:
                ScienceOpen disciplines: Cell biology
                Keywords: aqp—aquaporin, crna—complementary rna, mip—major intrinsinc protein of lens, pcr—polymerase chain reaction

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