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November 1959

A Study of Uropepsin as a Reflection of Gastric Secretory Activity

AMA Arch Surg. 1959;79(5):761-768. doi:10.1001/archsurg.1959.04320110063011

Urine pepsinogen is a proenzyme with pepsin-like proteolytic activity in a highly acid substate. It was discovered by Brücke2 in 1860 and confirmed by Grützner6 in 1881-1882. The name, uropepsin, was originated by Bendersky1 in 1890.

Pepsinogen is known to be produced by the chief cells of the gastric glands and secreted mainly into the gastric lumen, where, under the acid conditions present, it is autocatalytically converted into pepsin. A certain controversial portion is thought to be secreted as an endocrine function of the chief cells directly into the blood stream where it is carried to and excreted by the kidneys (uropepsin).

The proenzyme, pepsinogen, found in the urine, has been considered by some investigators to reflect closely the activity of the gastric mucosa. Others, however, have considered the relationship to be highly variable and inaccurate. On the basis that it is a constant one, many clinical