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Open AccessJournal ArticleDOI

Aquaporin water channels in gastrointestinal physiology

Tonghui Ma, +1 more
- 01 Jun 1999 - 
- Vol. 517, Iss: 2, pp 317-326
TLDR
Evidence that aquaporin‐type water channels are involved in GI fluid transport is evaluated and preliminary evaluation of GI function suggests a role for AQP1 in dietary fat processing and AQP4 in colonic fluid absorption.
Abstract
Fluid transport is a major function of the gastrointestinal (GI) tract with more than 9 litres of fluid being absorbed or secreted across epithelia in human salivary gland, stomach, the hepatobiliary tract, pancreas, small intestine and colon. This review evaluates the evidence that aquaporin-type water channels are involved in GI fluid transport. The aquaporins are a family of small (≈30 kDa) integral membrane proteins that function as water channels. At least seven aquaporins are expressed in various tissues in the GI tract: AQP1 in intrahepatic cholangiocytes, AQP4 in gastric parietal cells, AQP3 and AQP4 in colonic surface epithelium, AQP5 in salivary gland, AQP7 in small intestine, AQP8 in liver, pancreas and colon, and AQP9 in liver. There are functional data suggesting that some GI cell types expressing aquaporins have high or regulated water permeability; however, there has been no direct evidence for a role of aquaporins in GI physiology. Recently, transgenic mice have been generated with selective deletions of various aquaporins. Preliminary evaluation of GI function suggests a role for AQP1 in dietary fat processing and AQP4 in colonic fluid absorption. Further study of aquaporin function in the GI tract should provide new insights into normal GI physiology and disease mechanisms, and may yield novel therapies to regulate fluid movement in GI diseases.

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Citations
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References
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Journal ArticleDOI

Vasopressin increases water permeability of kidney collecting duct by inducing translocation of aquaporin-CD water channels to plasma membrane

TL;DR: It is concluded that vasopressin increases the water permeability of collecting duct cells by inducing a reversible translocation of AQP-CD water channels from IVs to the APM.
Journal ArticleDOI

Requirement of human renal water channel aquaporin-2 for vasopressin-dependent concentration of urine.

TL;DR: 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, which is essential for vasopressin-dependent concentration of urine.
Journal ArticleDOI

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

TL;DR: 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 as mentioned in this paper.
Journal ArticleDOI

Reconstitution of functional water channels in liposomes containing purified red cell CHIP28 protein.

TL;DR: Results demonstrate that CHIP28 protein functions as a molecular water channel and also indicate thatCHIP28 is responsible for most transmembrane water movement in RBCs.
Journal ArticleDOI

Severely Impaired Urinary Concentrating Ability in Transgenic Mice Lacking Aquaporin-1 Water Channels

TL;DR: The results suggest that AQP1 knockout mice are unable to create a hypertonic medullary interstitium by countercurrent multiplication, and AQP 1 is thus required for the formation of a concentrated urine by the kidney.
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