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Estradiol Stimulates a Uterine Plasma Membrane Protease Activator^*

Wadsworth Center for Laboratories and Research, New York State Department of Health and School of Public Health Sciences Albany, New York 12201

Address requests for reprints to: Elena E. Jazin, Wadsworth Center for Laboraties and Research, New York State Department of Health, Empire State Plaza, Albany, New York 12201.

Abstract

An estrogen-regulated arginine esteropeptidase is present in the immature rat uterus. The enzymatic complex consists of a membrane-bound activator and a soluble proenzyme. The activator is under strong estrogen control; its activity increases 10-fold 3 h after a single dose of 17β-estradiol. The subcellular localization of the activator is determined by a radioactive assay of fractions prepared by sucrose density centrifugation. The distribution of activity parallels the distribution of two plasma membrane markers, Mg²⁺-ATPase and 5'-nucleotidase. Electron micrographic visualization of the gradient fractions containing the activator reveals a population of vesicles 0.2–0.5 µm in diameter (Endocrinology 122: 500–503, 1988)

Footnotes

^* This work was supported in part by NSF Grant DCB-8507667. A preliminary report of these results was presented at the American Society of Biological Chemists, Philadelphia, PA, June 7-11,1987.

Received September 25, 1987.