NDLI: Cholangiocytes express the aquaporin CHIP and transport water via a channel-mediated mechanism.

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Cholangiocytes express the aquaporin CHIP and transport water via a channel-mediated mechanism.

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Cholangiocytes express the aquaporin CHIP and transport water via a channel-mediated mechanism.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Agre, P. Yano, M. Ueno, Y. Larusso, N. F. Pham, L. Roberts, S. K. Alpini, G.
Description	Author Affiliation: Roberts SK ( Department of Internal Medicine, Mayo Clinic, Rochester, MN 55905.);
Abstract	Cholangiocytes line the intrahepatic bile ducts and regulate salt and water secretion during bile formation, but the mechanism(s) regulating ductal water movement remains obscure. A water-selective channel, the aquaporin CHIP, was recently described in several epithelia, so we tested the hypothesis that osmotic water movement by cholangiocytes is mediated by CHIP. Isolated rodent cholangiocytes showed a rapid increase in volume in the presence of hypotonic extracellular buffers; the ratio of osmotic to diffusional permeability coefficients was > 10. The osmotically induced increase in cholangiocyte volume was inversely proportional to buffer osmolality, independent of temperature, and reversibly blocked by HgCl2. Also, the luminal area of isolated, enclosed bile duct units increased after exposure to hypotonic buffer and was reversibly inhibited by HgCl2. RNase protection assays, anti-CHIP immunoblots, and immunocytochemistry confirmed that CHIP transcript and protein were present in isolated cholangiocytes but not in hepatocytes. These results demonstrate that (i) isolated cholangiocytes and intact, polarized bile duct units manifest rapid, mercury-sensitive increases in cell size and luminal area, respectively, in response to osmotic gradients and (ii) isolated cholangiocytes express aquaporin CHIP at both the mRNA and the protein level. The data implicate aquaporin water channels in the transcellular movement of water across cholangiocytes lining intrahepatic bile ducts and provide a plausible molecular explanation for ductal water secretion.
ISSN	00278424
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	26
Volume Number	91
Language	English
Publisher	National Academy of Sciences
Publisher Date	1994-01-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Aquaporins Bile Ducts Cytology Ion Channels Metabolism Water-Electrolyte Balance Animals Aquaporin 1 Biological Transport Drug Effects Gene Expression Immunoenzyme Techniques Genetics Mercuric Chloride Pharmacology RNA, Messenger Temperature Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S. Multidisciplinary
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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