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Aquaporin Water Channels: Atomic Structure to Clinical Medicine

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Air date: Wednesday, February 23, 2005, 3:00:00 PM
Time displayed is Eastern Time, Washington DC Local
Views: Total views: 99 * This only includes stats from October 2011 and forward.
Category: WALS - Wednesday Afternoon Lectures
Runtime: 01:01:27
Description: The high water permeability of certain biological membranes is due to the presence of aquaporin water channel proteins. AQP1 was discovered in human red cells. AQP1 has been thoroughly characterized biophysically, and the atomic structure of AQP1 has been elucidated. Ten homologs have been identified in humans. These are selectively permeated by water (aquaporins) or water plus glycerol (aquaglyceroporins). The sites of expression predict the clinical phenotypes in humans. Individuals lacking Colton blood group antigens have mutations in the AQP1 gene. When deprived of water, AQP1-null individuals exhibit a defect in urine concentration and a marked reduction in fluid exchange between capillary and interstitium in lung.

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NIH Director's Wednesday Afternoon Lecture Series
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Author: Peter Agre, Ph.D., Johns Hopkins University School of Medicine
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CIT Live ID: 3443
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