Abstract: Series 105, Lecture 5
The Harvey Lectures Series 105 (2009—2010)
previous lecture | next lecture
Lecture #5: Thursday, March 18, 2010 — Time and Location
Aquaporin Water Channels: From Atomic Structure to Malaria
Peter Agre, MD
University Professor and Director
Johns Hopkins Malaria Research Institute
Bloomberg School of Public Health
Baltimore, Maryland
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.