Peter Agre received one of the two 2003 chemistry prizes for clarifying how water is transported into and out of the cells of the body. It was long suspected that cells must contain specifi c water channels, but it was not until 1988 that Agre isolated a membrane protein that, he later realised, was the channel. A decade later, Roderick MacKinnon earned the second of the 2003 awards by using X-ray crystallography to examine the structure of ion (salt) channels and how they work. Agre’s discovery explains, for example, how kidneys recover water from primary urine. It also has implications in animal, bacterial and plant studies.
He was born in Northfi eld, Minnesota, 40 miles south of Minneapolis, in 1949. Like many Minnesotans, he came from ‘viking’ Norwegian stock. His father was a chemistry professor, and double Nobel laureate Linus Pauling was a guest and family hero. Peter attended Theodore Roosevelt high school and was an Eagle Scout but a school camping trip through Russia brought out a teenage rebellious streak and when his chemistry grades slipped to ‘D’ he quit school in 1967 and continued at night school, while learning Russian during the day. Finally, he enrolled at Augsburg where he majored in chemistry. After graduating, he took a year out in 1970 to tour Asia and the Middle East before entering Johns Hopkins medical school. There he became fascinated by biomedical research and met his future wife, Mary Macgill (they married in 1975 and have three daughters and a son).
After gaining his MD in 1974, Agre trained at Case Western Reserve University Hospital, Hospitals of Cleveland, and in 1978 accepted a clinical fellowship in haematology and oncology at the University of North Carolina. In 1981 Agre returned to Johns Hopkins, becoming an assistant professor in 1983. Working on the blood group antigen Rh, Agre’s team isolated two new membrane proteins (approx. 30 kDa) in red cells. After spending 1988–89 on sabbatical to learn DNA technology, Agre decided to explore one protein further. The protein was abundant in kidney tubules and was related to proteins from diverse sources – lens of cow eye, fruit fl y brain, bacteria, and plants. These clues intrigued Agre but it was John Parker, his former professor at UNC, who suggested it might be the long-sought water channel. With Greg Preston, Agre performed a simple test by doctoring six frog eggs with the protein. Immersing six normal eggs in water had no effect, but the doctored eggs “exploded like popcorn”. Presenting their discovery in 1992 the scientists dubbed the protein ‘aquaporin’ or AQP1. At the last count, biochemists in this fi eld had reached AQP12 in humans, but hundreds of aquaporins are now known in plants and micro-organisms.
This text and the picture of the Nobel Laureate were taken from the book: "NOBELS. Nobel Laureates photographed by Peter Badge" (WILEY-VCH, 2008).
Picture: © Peter Badge/ Foundation Lindau Nobelprizewinners Meetings at Lake Constance |