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Proc Natl Acad Sci U S A. 1993 Aug 1; 90(15): 7275–7279.
PMCID: PMC47119
PMID: 8346245

Distribution of the aquaporin CHIP in secretory and resorptive epithelia and capillary endothelia.

S Nielsen, B L Smith, E I Christensen, and P Agre
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Abstract

The existence of water-selective channels has been postulated to explain the high water permeability of erythrocytes and certain epithelial cells. The aquaporin CHIP (channel-forming integral membrane protein of 28 kDa), a molecular water channel, is abundant in erythrocytes and water-permeable segments of the nephron. To determine whether CHIP may mediate transmembrane water movement in other water-permeable epithelia, membranes of multiple organs were studied by immunoblotting, immunohistochemistry, and immunoelectron microscopy using affinity-purified anti-CHIP IgG. The apical membrane of the choroid plexus epithelium was densely stained, implying a role for CHIP in the secretion of cerebrospinal fluid. In the eye, CHIP was abundant in apical and basolateral domains of ciliary epithelium, the site of aqueous humor secretion, and also in lens epithelium and corneal endothelium. CHIP was detected in membranes of hepatic bile ducts and water-resorptive epithelium of gall bladder, suggesting a role in bile secretion and concentration. CHIP was not detected in glandular epithelium of mammary, salivary, or lacrimal glands, suggesting the existence of other water-channel isoforms. CHIP was also not detected within the epithelium of the gastrointestinal mucosa. CHIP was abundant in membranes of intestinal lacteals and continuous capillaries in diverse tissues, including cardiac and skeletal muscle, thus providing a molecular explanation for the known water permeability of certain lymphatics and capillary beds. These studies underscore the hypothesis that CHIP plays a major role in transcellular water movement throughout the body.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.
  • Solomon AK, Chasan B, Dix JA, Lukacovic MF, Toon MR, Verkman AS. The aqueous pore in the red cell membrane: band 3 as a channel for anions, cations, nonelectrolytes, and water. Ann N Y Acad Sci. 1983;414:97–124. [PubMed] [Google Scholar]
  • Denker BM, Smith BL, Kuhajda FP, Agre P. Identification, purification, and partial characterization of a novel Mr 28,000 integral membrane protein from erythrocytes and renal tubules. J Biol Chem. 1988 Oct 25;263(30):15634–15642. [PubMed] [Google Scholar]
  • Smith BL, Agre P. Erythrocyte Mr 28,000 transmembrane protein exists as a multisubunit oligomer similar to channel proteins. J Biol Chem. 1991 Apr 5;266(10):6407–6415. [PubMed] [Google Scholar]
  • Preston GM, Agre P. Isolation of the cDNA for erythrocyte integral membrane protein of 28 kilodaltons: member of an ancient channel family. Proc Natl Acad Sci U S A. 1991 Dec 15;88(24):11110–11114. [PMC free article] [PubMed] [Google Scholar]
  • Preston GM, Carroll TP, Guggino WB, Agre P. Appearance of water channels in Xenopus oocytes expressing red cell CHIP28 protein. Science. 1992 Apr 17;256(5055):385–387. [PubMed] [Google Scholar]
  • Zeidel ML, Ambudkar SV, Smith BL, Agre P. Reconstitution of functional water channels in liposomes containing purified red cell CHIP28 protein. Biochemistry. 1992 Aug 25;31(33):7436–7440. [PubMed] [Google Scholar]
  • Preston GM, Jung JS, Guggino WB, Agre P. The mercury-sensitive residue at cysteine 189 in the CHIP28 water channel. J Biol Chem. 1993 Jan 5;268(1):17–20. [PubMed] [Google Scholar]
  • Nielsen S, Smith BL, Christensen EI, Knepper MA, Agre P. CHIP28 water channels are localized in constitutively water-permeable segments of the nephron. J Cell Biol. 1993 Jan;120(2):371–383. [PMC free article] [PubMed] [Google Scholar]
  • van Hoek AN, Verkman AS. Functional reconstitution of the isolated erythrocyte water channel CHIP28. J Biol Chem. 1992 Sep 15;267(26):18267–18269. [PubMed] [Google Scholar]
  • Zhang R, Skach W, Hasegawa H, van Hoek AN, Verkman AS. Cloning, functional analysis and cell localization of a kidney proximal tubule water transporter homologous to CHIP28. J Cell Biol. 1993 Jan;120(2):359–369. [PMC free article] [PubMed] [Google Scholar]
  • Sabolić I, Valenti G, Verbavatz JM, Van Hoek AN, Verkman AS, Ausiello DA, Brown D. Localization of the CHIP28 water channel in rat kidney. Am J Physiol. 1992 Dec;263(6 Pt 1):C1225–C1233. [PubMed] [Google Scholar]
  • Lanahan A, Williams JB, Sanders LK, Nathans D. Growth factor-induced delayed early response genes. Mol Cell Biol. 1992 Sep;12(9):3919–3929. [PMC free article] [PubMed] [Google Scholar]
  • Deen PM, Dempster JA, Wieringa B, Van Os CH. Isolation of a cDNA for rat CHIP28 water channel: high mRNA expression in kidney cortex and inner medulla. Biochem Biophys Res Commun. 1992 Nov 16;188(3):1267–1273. [PubMed] [Google Scholar]
  • Bondy C, Chin E, Smith BL, Preston GM, Agre P. Developmental gene expression and tissue distribution of the CHIP28 water-channel protein. Proc Natl Acad Sci U S A. 1993 May 15;90(10):4500–4504. [PMC free article] [PubMed] [Google Scholar]
  • Ernst SA, Palacios JR, 2nd, Siegel GJ. Immunocytochemical localization of Na+,K+-ATPase catalytic polypeptide in mouse choroid plexus. J Histochem Cytochem. 1986 Feb;34(2):189–195. [PubMed] [Google Scholar]
  • Narula P, Xu M, Kuang KY, Akiyama R, Fischbarg J. Fluid transport across cultured bovine corneal endothelial cell monolayers. Am J Physiol. 1992 Jan;262(1 Pt 1):C98–103. [PubMed] [Google Scholar]
  • van Heeswijk MP, van Os CH. Osmotic water permeabilities of brush border and basolateral membrane vesicles from rat renal cortex and small intestine. J Membr Biol. 1986;92(2):183–193. [PubMed] [Google Scholar]
  • Fushimi K, Uchida S, Hara Y, Hirata Y, Marumo F, Sasaki S. Cloning and expression of apical membrane water channel of rat kidney collecting tubule. Nature. 1993 Feb 11;361(6412):549–552. [PubMed] [Google Scholar]

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