PETER AGRE
Name: Bustamante, Cyra Joriel B.
LIFE OF PETER AGRE
 American doctor, corecipient of the Nobel Prize for Chemistry
in 2003 for his discovery of water channels in cell membranes.
He shared the award with Roderick MacKinnon, also of
the United States.
 Born on January 30, 1949 in Northfield, Minnesota, U.S.
 The second of six children. His father Courtland Agre worked at the
chemistry department at St Olaf College, later becoming professor
at Augsburg College in Minneapolis. Agre credits his father for
instilling in him an admiration for chemistry.
 He enrolled at Augsburg College to major in chemistry, with the
aim of going to medical school. Agre was accepted to the Johns
Hopkins medical school in 1970
 In 1974 Agre earned an M.D. degree from Johns
Hopkins University School of Medicine.
 In 1975, Agre married Mary Macgill, a biologist, and together they
moved to Cleveland, Ohio, where Agre completed clinical training
at Case Western University Hospitals.
 In the 1980s Agre began conducting his pioneering research on
water channels in cell membranes. First mentioned by scientists in
the mid-1800s, these specialized openings allow water to flow in
and out of cells.
 Agre joined the Department of Biological Chemistry at Johns
Hopkins University in 1992 and became full professor in 1993.
 Agre devotes much of his time to presenting his work around the
world (he has participated in eight Lindau Nobel Laureate Meetings
since winning the Nobel Prize in 2003).
 In 2008, Agre became director of the Johns Hopkins Malaria
Research Institute and since then he spends a third of every year
doing field work in malaria research in either Zambia or Zimbabwe.
Date: October 18, 2019
HIS DISCOVERY (AQUAPORIN)
Protein was named CHIP28 (CHannel-forming Integral Protein of 28 kD)
was responsible for water transport in red blood cells. The name
aquaporin, abbreviated to AQP1, was coined soon after, and replaced
CHIP28. Since the discovery of AQP1 in the early 1990s, much research
has been focused on determining various aquaporin isoforms and their
functions, what is now often termed as the aquaporin superfamily. To
date, 13 isoforms have been identified in mammals and many more in
plants and bacteria. Classical (or orthodox) aquaporins are now known to
constitute one branch of a larger group. They are highly permeable to
water. Aquaglycerolporins are permeable to water, glycerol and small
solutes. S-aquaporins are present only in animals, and the specifics of
their permeability are still being determined.
Aquaporins are abundant in many different types of cells, with large
amounts concentrated in the skin, brain, kidneys and lungs. Peter Agre
refers to aquaporins as the “plumbing system for cells” hence the study of
various aquaporins leads to answers on fluid transport between cells.
AQP2 is necessary for the proper function of kidneys, as it is essential for
the concentration of urine in the collecting duct. Abnormalities in AQP2
function lead to often severe illnesses concerning water balance
irregularities. AQP3 is a water and glycerol channel located mainly in the
kidneys and outer layers of the skin. Recent studies have shown that AQP3
may control the migration of breast cancer cells through the regulation of
hydrogen peroxide transport. Agre and his team, along with researchers
from the University of Aarhus in Denmark, cloned AQP4, which is a key
component of the blood brain barrier and also responsible for proper
function of the retina, inner ear and olfactory system. Yet another
aquaporin, AQP5, plays a significant role in the production of saliva, sweat
and tears.
Schedule and Section: BSN 1-H; 2:30-4:30PM MWF Instructor: Miss Steffy Jell C. Largo