The 2003 Nobel Prize in Chemistry was awarded to American Physiological Society member Peter C. Agre from Johns Hopkins School of Medicine for being the first to identify and characterize water channels (photo courtesy of Hans Mehlin, Nobel e-Museum). This pivotal work of Dr. Agre and collaborators began in the search for the red cell protein responsible for Rh immunoreactivity. In these studies, a protein contaminant was found that was isolated and purified and then cloned and characterized (1, 4, 5). These studies demonstrated that this protein is highly expressed not only in red cells but also in the renal proximal tubule and the descending limb of the loop of Henle and that it mediates the transport of water (1, 5). We now refer to this protein as aquaporin-1. Agre and collaborators went on to demonstrate that humans with mutations in aquaporin-1 cannot concentrate their urine fully (2). Since then, an entire family of water channels have been identified, cloned, and characterized. These seminal studies of Agre and collaborators have thus resulted in an explosion of knowledge regarding water movement across cell membranes and, in particular, how water channels contribute to urinary concentration. The extensive contributions of the Agre laboratory have been reviewed in greater detail elsewhere (3).



View larger version (110K):
[in this window]
[in a new window]
 
 
REFERENCES

  1. Denker BM, Smith BL, Kuhajda FP, and Agre P. Identification, purification, and partial characterization of a novel Mr 28,000 integral membrane protein from erythrocytes and renal tubules. J Biol Chem 263: 15634–15642, 1988.[Abstract/Free Full Text]
  2. King LS, Choi M, Fernandez PC, Cartron JP, and Agre P. Defective urinary concentrating ability due to a complete deficiency of aquaporin-1. N Engl J Med. 345: 175–179, 2001.[Free Full Text]
  3. Knepper MA and Nielsen S. Peter Agre, 2003 Nobel Prize winner in chemistry. J Am Soc Nephrol 15: 1093–1095, 2004.[Abstract/Free Full Text]
  4. Preston GM and Agre P. Isolation of the cDNA for erythrocyte integral membrane protein of 28 kilodaltons: member of an ancient channel family. Proc Natl Acad Sci USA 88: 11110–11114, 1991.[Abstract]
  5. Preston GM, Carroll TP, Guggino WB, and Agre P. Appearance of water channels in xenopus oocytes expressing red cell CHIP28 protein. Science 256: 385387, 1992.




This Article
Full Text (PDF)
Alert me when this article is cited
Alert me if a correction is posted
Services
Email this article to a friend
Similar articles in this journal
Similar articles in PubMed
Alert me to new issues of the journal
Download to citation manager
Articles citing this Article
PubMed
PubMed Citation


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
Visit Other APS Journals Online
Copyright © 2004 by the American Physiological Society.