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Science 16 June 1995:
Vol. 268. no. 5217, pp. 1609 - 1612
DOI: 10.1126/science.7777858
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Articles

Science, Vol 268, Issue 5217, 1609-1612
Copyright © 1995 by American Association for the Advancement of Science

articles

Identification of a stimulator of steroid hormone synthesis isolated from testis

N Boujrad, SO Ogwuegbu, M Garnier, CH Lee, BM Martin, and V Papadopoulos

Department of Cell Biology, Georgetown University Medical Center, Washington, DC 20007, USA.

Gonadal steroidogenesis is regulated by pituitary gonadotropins and a locally produced, unidentified factor. A 70-kilodalton (kD) protein complex secreted from rat Sertoli cells was isolated. The complex, composed of 28- and 38-kD proteins, stimulated steroidogenesis by Leydig cells and ovarian granulosa cells in a dose-dependent and adenosine 3',5'-monophosphate-independent manner. The follicle-stimulating hormone-induced 28-kD protein appeared to be responsible for the bioactivity, but the 38-kD protein was indispensable for maximal activity. The 28- and 38-kD proteins were shown to be identical to the tissue inhibitor of metalloproteinase-1 (TIMP-1) and the proenzyme form of cathepsin L, respectively. Thus, a TIMP-1-procathepsin L complex is a potent activator of steroidogenesis and may regulate steroid concentrations and, thus, germ cell development in both males and females.


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