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Nobelist Agre To Give NIH Director's Lecture

As is often the case in science, serendipity played a role in the discovery. While studying the Rh blood group antigen in red blood cells, Dr. Peter Agre came across a highly abundant protein contaminant. "We basically discovered a new protein and didn't have a clue what it did," he said. Further study hinted that it might be the long-sought channel that regulates water movement into and out of cells. "A couple of generations of physiologists have argued about whether water crosses cell membranes by diffusion or whether it travels by special pathways," he said. "And it turns out there are special pathways, and that's what we discovered." He dubbed the protein "aquaporin" (water pore).

Agre won the 2003 Nobel Prize in Chemistry for his discovery, an honor he shared with Dr. Roderick MacKinnon, who discovered how ions move through cell membranes. "So the humble truth is, this brilliant discovery began as an accidental observation," Agre said laughing.

Nobel laureate Dr. Peter Agre

A professor of biological chemistry and professor of medicine at Johns Hopkins University School of Medicine, Agre will deliver the NIH Director's Lecture on "Aquaporin Water Channels: From Atomic Structure to Clinical Medicine," on Wednesday, Feb. 23 at 3 p.m. The lecture will take place in Masur Auditorium, Bldg. 10.

More than 10 aquaporins have now been identified in humans and the clinical implications are enormous, Agre said. Several labs are using the newfound information on aquaporins to try to develop treatments for various diseases and conditions. "Any fluid transport problem will almost certainly involve aquaporins," Agre noted. "One such problem is the swelling that results after a stroke or accidental head injury. Swelling that occurs in one structure of the brain does so at the expense of compression in another," he said. "It would be fantastic if more research on aquaporins could lead to a new treatment for this condition."

There are now many other examples of clinical syndromes linked to poorly functioning water channels, he continued. In the kidney, faulty aquaporin regulation can lead to a condition in which the kidneys cannot concentrate urine and patients become dehydrated. Or, conversely, an overabundance of aquaporins may lead to fluid retention in congestive heart failure and in pregnancy. An abnormal distribution of aquaporins in salivary gland cells might contribute to salivary gland dysfunction. In a disorder called Sjogren's syndrome, for example, saliva production may be so limited that people lack enough of it to properly chew, swallow or speak.

These previously unknown water channels have been discovered in animals, plants and lower organisms. "In our lab, we're currently looking at the role of aquaporins in microorganisms, because each microorganism has at least a few of these," Agre said. "We're wondering if these are potential drug targets in the treatment of tuberculosis or malaria."

Agre's work on aquaporins began with support from NHLBI. "The NIH has made all the difference; it was the NIH funding, and scientific help from our colleagues at Hopkins, that got us started on this," he said. "In fact, it's really the taxpayers who get credit for this research, because they funded it." Agre currently has grants from NEI as well as NHLBI.

A native of Minnesota, he received a bachelor's degree in chemistry from Augsburg College in Minneapolis and earned an M.D. from Johns Hopkins. He completed a residency in internal medicine at Case Western Reserve University Hospitals then held a clinical fellowship in hematology/oncology at the University of North Carolina at Chapel Hill. He joined the faculty at Hopkins in 1984 and rose through the ranks to his current position. He also has served as director of the Johns Hopkins Graduate Program in Cellular and Molecular Medicine, the first NIH-funded program in molecular medicine in the U.S.

For more information and reasonable accommodation, contact Hilda Madine at (301) 594-5595 or hmadine@cc.nih.gov.


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