October 8, 2003
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Audio of Press Briefing
Peter Agre, M.D., 54, professor
of biological chemistry at the Johns Hopkins University School of
Medicine, today was awarded the 2003 Nobel Prize in Chemistry by the Royal
Swedish Academy of Sciences. The Academy recognized him for his
laboratory's 1991 discovery of the long-sought "channels" that regulate
and facilitate water molecule transport through cell membranes, a process
essential to all living organisms.
Agre (pronounced AHG-ray) shares this
year's prize with Roderick MacKinnon, a Rockefeller University scientist
who determined the spatial structure of cell membrane channels that
control passage of salts.
The
discovery of the water channel, dubbed "water pore" or aquaporin, ushered
in a golden age of biochemical, physiological and genetic studies of these
proteins in bacteria, plants and mammals, and fundamental understanding --
at the molecular level -- of malfunctioning channels associated with many
diseases of the kidneys, skeletal muscle and other organs. Working from
this basic knowledge, scientists are searching for drugs that can
specifically target water channel defects.
"It is a remarkable honor to receive a
Nobel Prize, because it not only recognizes discoveries, but also their
usefulness to the advancement of fundamental science," says Agre, a member
of Hopkins' Institute for Basic Biomedical Sciences. "It is amazing and
gratifying that the Nobel committee feels our work has accomplished that
milestone in just 12 years. That's warp speed in molecular chemistry and
it could never have happened as fast as it did without the wonderful
resources and collaborators available at Johns Hopkins. This is an honor
for the entire Hopkins family."
"This is a great day for the school of
medicine and the university at large," says Edward D. Miller, M.D., dean
of the medical faculty and CEO of Johns Hopkins Medicine. "There are few
happier occasions to celebrate at an academic medical center."
"This
is a terrific day for Peter and a tremendous day for the Hopkins
community," adds Chi Dang, M.D., vice dean for research at Johns Hopkins.
"The prize is not only a recognition of the important discoveries on how
materials are transferred into and out of cells, but it's also symbolic -
in the case of Peter Agre - of being rewarded for a job superbly done with
great depth, without fanfare. This should be an encouragement for the
young scientists that persistence and dedication will yield the joy of
discoveries and occasionally, fringe benefits. It also highlights that the
prepared mind can turn serendipity, as in the case of the discovery of
water channels, into a paradigm breaking moment."
William R Brody, M.D., Ph.D., president
of the Johns Hopkins University, adds: "The world-wide Johns Hopkins
community joins with the School of Medicine in congratulating Peter for
his laboratory's great achievement."
Since a 1992 paper in Science by Agre and
Hopkins physiologist Bill Guggino, Ph.D., which documented the discovery
of the very first water channel protein, 10 more have been found in
mammals, and hundreds more in plants, bacteria and other forms of life. In
Agre's lab alone, aquaporins have been discovered to be part of the
blood-brain barrier and also associated with critical water transport in
skeletal muscle, lung and kidney. Members of Agre's lab also have found
aquaporins in the eye and in salivary and tear glands. Researchers around
the world now study aquaporins in many species of plants, bacteria and
animals, and have linked aberrant water transport to a multitude of human
diseases and conditions.
"I am so pleased that Peter has been
recognized for his outstanding work on aquaporins," says Gerald Hart,
Ph.D., director of biological chemistry, the division housing Agre's
laboratory. "He has been part of the Johns Hopkins family for more than 20
years, and we just couldn't be prouder."
The
discovery of aquaporin is an example of luck favoring the well-prepared.
Beginning in the mid-1980s, he and his colleagues, including technician
Barbara Smith and then post-doc Gregory Preston, Ph.D., were searching for
proteins that are part of the Rh-factor when they happened across an
abundant and much smaller protein. The researchers pursued the unexpected
protein visitor -- they isolated it and discovered that it was widely
expressed -- and within a year had cloned its complementary DNA. In
dramatic experiments with frogs' eggs, the scientists next proved that the
unknown protein was in fact biology's elusive cellular regulator of water
transport.
Although Agre started his career in
medicine, he gradually shifted to laboratory research so that he could
investigate fundamental biological questions whose answers would have
clinical relevance.
"I am certain that in the future, we will be able to capitalize on our
understanding of aquaporins to benefit medicine, biotechnology and even
agriculture," says Agre. "We still have much to learn, and the
possibilities of where aquaporins will take us are unlimited. "
Born in Northfield, Minn., in 1949, Agre
went to Theodore Roosevelt High School in Minneapolis, and in 1970 earned
his bachelor's degree in chemistry from Augsburg College in that city. He
received his medical doctorate from Johns Hopkins in 1974. In 1981, after
post-graduate medical training and then a fellowship at the University of
North Carolina at Chapel Hill, Agre returned to Hopkins, where he
progressed through the ranks of the departments of medicine and cell
biology. In 1993, he was recruited by then-department director Daniel
Lane, Ph.D., to become a professor in the department of biological
chemistry, a position he still holds.
Agre was elected to membership in the
National Academy of Sciences in 2000 and to the American Academy of Arts
and Sciences in 2003. He holds two U.S. patents on the isolation, cloning
and expression of aquaporins 1 and 5 and is the principal investigator on
four current National Institutes of Health grants.
It has been 25 years since a current
Hopkins School of Medicine faculty member was awarded a Nobel Prize. In
1978, scientists Hamilton Smith and Daniel Nathans shared the prize with
Werner Arber for development and application of restriction enzymes --
molecular scissors that cut DNA in predictable places.
On the Web:
Peter Agre's speech at the Nobel Banquet, December 10, 2003
http://www.nobel.se/chemistry/laureates/2003/press.html
http://www.nobel.se/chemistry/laureates/2003/public.html
http://webapps.jhu.edu/jhuniverse/information_about_hopkins/facts_and_statistics/nobel_prize_winners/index.cfm
