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Plenary Lecture
Peter Agre, 60 views
Found throughout nature, aquaporin water channels confer high water permeability to cell membranes. Discovered in human erythrocytes, AQP1 has been characterized biophysically, and the atomic structure of AQP1 is known. Twelve homologous proteins exist in humans. Some transport only water (aquaporins); others transport water plus glycerol (aquaglyceroporins). These proteins are required for generation of physiological fluids (urine, cerebrospinal fluid, aqueous humor, sweat, saliva, and tears). Involvement of aquaporins in multiple clinical states is becoming recognized—renal concentration, fluid retention, cataract, skin hydration, brain edema, thermal stress, glucose homeostasis, malaria, and even arsenic poisoning. Aquaporins are particularly important in plant biology. This information now provides the challenge of developing new technologies to manipulate aquaporins for clinical or agricultural benefits. Born in 1949 in Minnesota, Peter Agre received his M.D. in 1974 from the Johns Hopkins University School of Medicine. He then served as the Vice Chancellor for science and technology at Duke University. Agre leads the Johns Hopkins Malaria Research Institute (JHMRI). He was elected to the National Academy of Sciences in 2000 and to the American Academy of Arts and Sciences in 2003. He is also a founding member of Scientists and Engineers for America (SEA), and serves on its Board of Advisors. In 2003 he was awarded the Nobel Prize in Chemistry (which he shared with Roderick MacKinnon) for his discovery of aquaporins, water-channel proteins that move water molecules through the cell membrane. In 2009, Peter Agre held the post of 163rd president of the American Association for the Advancement of Science (AAAS).
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