UROPEPSIN EXCRETION BY MAN. I. THE SOURCE, PROPERTIES AND ASSAY OF UROPEPSIN 12

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Abstract
Inasmuch as repeated withdrawal of specimens of gastric juices as a method for study of gastric activity involves certain practical as well as theoretical disadvantages, an attempt was made to determine if the excretion of uropepsin could be utilized for the same purpose. It is known that uropepsin, a proteolytic enzyme active at acid reactions, which occurs in the urine of normal subjects, is not found in the absence of functional activity of the gastric mucosa. The stability of uropepsin during storage and the absence of inhibitors of this enzyme in the urine indicated that the described method of assay of uropepsin could be utilized to determine the true quantity of this enzyme as it is excreted in the urine. The proteolytic activity of urine at acid reactions is primarily due to uropepsin. The oral ingestion of gastric pepsin by normal subjects or patients with pernicious anemia or the intraven. injn. of pepsin failed to increase the urinary uropepsin. Oral admn. of pepsinogen, with or without a buffer, failed to increase uropepsin excretion but intraven. injn. of pepsinogen promptly increased urinary uropepsin. These facts are believed to indicate that uropepsin is derived from the direct secretion of pepsinogen into the blood stream by the secreting glands themselves and not from the reabsorption of pepsin from the lumen of the stomacho Uropepsin thus represents the excretion product of an endocrine-like secretion of the peptic cells of the stomach.

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