Abstract

THE presence of a hyperglycemic substance was recognized in some of the earliest preparations of insulin. Murlin suggested the name of glucagon for this substance in 1923 (1). It was, however, the recent work of de Duve (2) and Sutherland (3, 4, 5) which stimulated the current interest. The hyperglycemic-glycogenolytic factor, or glucagon, has been found in pancreatic extracts of all species in which it has been sought (6, 7). In some species, but not all, it has also been found in extracts of gastric mucosa and to a lesser extent in duodenum and ileum (4). It has been postulated that the alpha cells are the main source of this substance in the pancreatic islets (8), though objections have been raised to this view (9). Glucagon has been recently obtained in a highly purified, crystalline form and it appears to have the properties of a protein (10). Its principal, and probably only site of action, is in the liver cell where it increases the amount of the active form of phosphorylase (5). This enzyme appears to be the rate-limiting factor in the glycogenolytic pathway to glucose. It has been suggested that glucagon is a true hormone and since it is a potent agent in carbohydrate and possibly fat metabolism (11, 12), much speculation has arisen concerning its possible role in man, particularly in human diabetes. Beyond the finding that glucagon is present in the human pancreas (6), little is known about endogenous glucagon in man. Because of the interesting possibilities of this substance in explaining certain aspects of the diabetic syndrome, it seemed desirable to attempt some direct measurements of glucagon in a series of human pancreases.

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