Uropepsin excretion in thalassemia.

Abstract

Bruke in 1861 was the first to describe how the urine of normal individuals contains a proenzyme, which by acidification is converted to a proteolytic enzyme, identical with gastric pepsin. The name of uropepsin was later applied to this enzyme by Bendersky. The evidence indicates that pepsinogen is produced by the parietal cells of gastric mucosa [2]; most of the pepsinogen is secreted into the lumen of the stomach, where it is converted into pepsin by the action of hydrochloric acid, while another fraction is taken up by the blood stream and is excreted, apparently unaltered, in the urine as uropepsinogen [2]. Disturbances in uropepsin excretion are mainly associated with functional and structural changes of gastric mucosa, and to a lesser degree with functional disturbances of the adrenal and pituitary glands [a, 61. It is a well-established fact that patients with gastric and duodenal ulcers, as well as those with hyperfunction of the adrenal and pituitary glands have an increased uropepsin excretion [4, 91. Uropepsin excretion is absent or very low in patients with gastrectomy, pernicious anemia and Addison’s disease [7, 9, lo]. In some cases of iron deficiency anemia and macrocytic anemias slight decreases of uropepsin have been reported [S]. We are not aware of reports concerning the excretion of uropepsin in cases of congenital hemolytic anemias. Because there is hypochlorhydria and reduction of gastric excretion [l] in patients with thalassemia, we have investigated uropepsin excretion in children with this disease.