Alfred Gilman

(1941- )

Alfred Goodman Gilman was born on July 1, 1941, in New Haven, Connecticut. Gilman graduated from Yale with his B.S. of Biochemistry in 1962. He then entered a M.D.-Ph.D. program at Case Western Reserve University in Cleveland, Ohio where he studied under Nobel laurate Earl Sutherland. Gilman graduated from Case Western in 1969, then did his post-doctoral studies at the National Institutes of Health with Nobel laurate Marshall Nirenberg from 1969 until 1971.

In 1971 Dr. Gilman became a professor at the University of Virginia in Charlottesville, Virginia. In 1981, he beame chairman of the Department of Pharmacology at the University of Texas Southwestern Medical Center in Dallas, Texas. He was elected as a member of the National Academy of Sciences in 1986. In addition to the Nobel Prize, he won the Albert Lasker Award for Basic Medical Research in 1989.

He shared the 1994 Nobel Prize in Physiology or Medicine with Martin Rodbell for their discoveries regarding G-proteins. G-proteins are a vital intermediary between the activation of receptors on the cell membrane and actions within the cell. Rodbell had shown in the 1960s that GTP was involved in cell signaling. It was Gilman who actually discovered the protiens that interacted with the GTP to initiate signalling cascades within the cell.

The following press release from the Royal Swedish Academy of Sciences describes Gilman's work:

It has been known for some time that cells communicate with each other by means of hormones and other signal substances, which are released from glands, nerves and other tissues. It is only recently that we have begun to understand how the cell handles this information from the outside and converts it into relevant action - i.e. how signals are transduced in cells.

The discoveries of the G-proteins by the Americans Alfred G. Gilman and Martin Rodbell have been of paramount importance in this context, and have opened up a new and rapidly expanding area of knowledge.

G-proteins have been so named because they bind guanosine triphosphate (GTP). Gilman and Rodbell found that G-proteins act as signal transducers, which transmit and modulate signals in cells. G-proteins have the ability to activate different cellular amplifier systems. They receive multiple signals from the exterior, integrate them and thus control fundamental life processes in the cells.

Disturbances in the function of G-proteins - too much or too little of them, or genetically determined alterations in their composition - can lead to disease. The dramatic loss of salt and water in cholera is a direct consequence of the action of cholera toxin on G-proteins. Some hereditary endocrine disorders and tumours are other examples. Furthermore, some of the symptoms of common diseases such as diabetes or alcoholism may depend on altered transduction of signals through G-proteins.