Earl Wilbur Sutherland, Jr. bigraphy, stories - American pharmacologist

Earl Wilbur Sutherland, Jr. : biography

November 19, 1915 - March 9, 1974

Earl Wilbur Sutherland Jr. (November 19, 1915 – March 9, 1974) was an American pharmacologist and biochemist born in Burlingame, Kansas. Sutherland won a Nobel Prize in Physiology or Medicine in 1971 "for his discoveries concerning the mechanisms of the action of hormones," especially epinephrine, via second messengers, namely cyclic adenosine monophosphate, or cyclic AMP. Sutherland died on March 9, 1974 in Miami, Florida, at the age of 58.

Discovery of cyclic AMP

While working in Cori’s laboratory, Sutherland, with the help of his co-workers, made several discoveries concerning the mechanism of glycogen metabolism, that years later, led him to his discovery of the biological activity of cyclic AMP. Cori’s laboratory had previously established the basic mechanism of glycogen metabolism, for which they were awarded the Nobel Prize in Physiology or Medicine. Sutherland helped to identify the importance of liver phosphorylase (LP) in the process of glycogenolysis. Of the three basic enzymes involved in glycogenolysis, Sutherland found that LP was rate-limiting, meaning that the progression of glycogen metabolism is dependent on this enzyme. LP would become the subject of Sutherland’s research for the next several years, and it was through experimentation on LP and hormone interaction that Sutherland’s most renowned discovery was made.

After identifying the importance of LP, Sutherland moved his research efforts to Western Reserve University. There, he worked in collaboration with Ted Rall, Walter D Wosilait, and Jacques Berthet to publish a series of papers in the Journal of Biological Chemistry titled “The Relationship of Epinephrine and Glucagon to Liver Phosphorylase,” in four parts.Sutherland, Earl W; Wosilait, WD (1 January 1956). “The relationship of epinephrine and glucagon to liver phosphorylase. I. Liver phosphorylase; preparation and properties”. The Journal of Biological Chemistry 218: 459-468.Wosilait, WD; Sutherland, EW (1 January 1956). “The relationship of epinephrine and glucagon to liver phosphorylase. II. Enzymatic inactivation of liver phosphorylase”. The Journal of Biological Chemistry 218: 469-481.Rall TW; Sutherland EW; Wosilait WD (1 January 1956). “The relationship of epinephrine and glucagon to liver phosphorylase. III. Reactivation of liver phosphorylase in slices and in extracts”. The Journal of Biological Chemistry 218: 483-495.Berthet, Jacques; Rall, TW; Sutherland, EW (1 January 1957). “The Relationship of Epinephrine and Glucagon to Liver Phosphorylase:IV Effect of Epinephrine and Glucagon on the Reactivation of Phosphorylase in Liver Homogenates”. The Journal of Biological Chemistry 224: 463-475. These four papers document the purification of LP and the analysis of several of its properties. First, it was determined that the enzymatic activity of LP depends on the addition or removal of a phosphate group, a process called phosphorylation. Rall TW; Sutherland EW; Wosilait WD (1 January 1956). “The relationship of epinephrine and glucagon to liver phosphorylase. III. Reactivation of liver phosphorylase in slices and in extracts”. The Journal of Biological Chemistry 218: 483-495. In a later experiment, they demonstrated that more phosphate is taken up in liver slices when epinephrine and glucagon are added, suggesting that these hormones were promoting the phosphorylation of LP, activating the enzyme. Rall TW; Sutherland EW; Wosilait WD (1 January 1956). “The relationship of epinephrine and glucagon to liver phosphorylase. III. Reactivation of liver phosphorylase in slices and in extracts”. The Journal of Biological Chemistry 218: 483-495. The results of a later paper in the series suggested that this phosphorylation and activation of LP was a result of the action of dephosphorlyase kinase. This series also investigated the inactivation of liver phosphorylase and characterized an enzyme they initially called LP-inactivating enzyme, which functions by cleaving the phosphate group. This enzyme was later renamed liver phosphorylase phosphatase. These papers also characterized LP in terms of molecular weight and other factors. During their analysis, they found the unexpected result that LP activation increased with the addition of 5-AMP, which is a precursor of cAMP; however, this was not known at the time.

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