Literature DB >> 9193450

The aquaporin family of water channel proteins in clinical medicine.

M D Lee1, L S King, P Agre.   

Abstract

The aquaporins are a family of membrane channel proteins that serve as selective pores through which water crosses the plasma membranes of many human tissues and cell types. The sites where aquaporins are expressed implicate these proteins in renal water reabsorption, cerebrospinal fluid secretion and reabsorption, generation of pulmonary secretions, aqueous humor secretion and reabsorption, lacrimation, and multiple other physiologic processes. Determination of the aquaporin gene sequences and their chromosomal locations has provided insight into the structure and pathophysiologic roles of these proteins, and primary and secondary involvement of aquaporins is becoming apparent in diverse clinical disorders. Aquaporin-1 (AQP1) is expressed in multiple tissues including red blood cells, and the Colton blood group antigens represent a polymorphism on the AQP1 protein. AQP2 is restricted to renal collecting ducts and has been linked to congenital nephrogenic diabetes insipidus in humans and to lithium-induced nephrogenic diabetes insipidus and fluid retention from congestive heart failure in rat models. Congenital cataracts result from mutations in the mouse gene encoding the lens homolog Aqp0 (Mip). The present understanding of aquaporin physiology is still incomplete; identification of additional members of the aquaporin family will affect future studies of multiple disorders of water distribution throughout the body. In some tissues, the aquaporins may participate in the transepithelial movement of fluid without being rate limiting, so aquaporins may be involved in clinical disorders without being causative. As outlined in this review, our challenge is to identify disease states in which aquaporins are involved, to define the aquaporins' roles mechanistically, and to search for ways to exploit this information therapeutically.

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Year:  1997        PMID: 9193450     DOI: 10.1097/00005792-199705000-00001

Source DB:  PubMed          Journal:  Medicine (Baltimore)        ISSN: 0025-7974            Impact factor:   1.889


  20 in total

1.  Neonatal and adult rabbit renal brush border membrane vesicle solute reflection coefficients.

Authors:  R Quigley; M Flynn; M Baum
Journal:  Biol Neonate       Date:  1999-08

Review 2.  The choroid plexuses and the barriers between the blood and the cerebrospinal fluid.

Authors:  M B Segal
Journal:  Cell Mol Neurobiol       Date:  2000-04       Impact factor: 5.046

Review 3.  Molecular insights into the physiology of the 'thin film' of airway surface liquid.

Authors:  R C Boucher
Journal:  J Physiol       Date:  1999-05-01       Impact factor: 5.182

4.  Congenital progressive polymorphic cataract caused by a mutation in the major intrinsic protein of the lens, MIP (AQP0).

Authors:  P Francis; V Berry; S Bhattacharya; A Moore
Journal:  Br J Ophthalmol       Date:  2000-12       Impact factor: 4.638

5.  cAMP regulated membrane diffusion of a green fluorescent protein-aquaporin 2 chimera.

Authors:  F Umenishi; J M Verbavatz; A S Verkman
Journal:  Biophys J       Date:  2000-02       Impact factor: 4.033

6.  High microvascular endothelial water permeability in mouse lung measured by a pleural surface fluorescence method.

Authors:  E P Carter; B P Olveczky; M A Matthay; A S Verkman
Journal:  Biophys J       Date:  1998-04       Impact factor: 4.033

7.  Water permeability in human airway epithelium.

Authors:  Peter Steen Pedersen; Kristina Procida; Per Leganger Larsen; Niels-Henrik Holstein-Rathlou; Ole Frederiksen
Journal:  Pflugers Arch       Date:  2005-09-17       Impact factor: 3.657

8.  Distinct biochemical and topological properties of the 31- and 27-kilodalton plasma membrane intrinsic protein subgroups from red beet.

Authors:  L M Barone; H H Mu; C J Shih; K B Kashlan; B P Wasserman
Journal:  Plant Physiol       Date:  1998-09       Impact factor: 8.340

9.  Roles of AQP5/AQP5-G103D in carbamylcholine-induced volume decrease and in reduction of the activation energy for water transport by rat parotid acinar cells.

Authors:  Keitaro Satoh; Yoshiteru Seo; Shinsuke Matsuo; Mileva Ratko Karabasil; Miwako Matsuki-Fukushima; Takashi Nakahari; Kazuo Hosoi
Journal:  Pflugers Arch       Date:  2012-08-19       Impact factor: 3.657

Review 10.  Ontogeny of water transport in the rabbit proximal tubule.

Authors:  Raymond Quigley; Jaap Mulder; Michel Baum
Journal:  Pediatr Nephrol       Date:  2003-09-05       Impact factor: 3.714

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