Somatomedin-C/insulin-like growth factor 1-like material secreted by porcine sertoli cells in vitro: Characterization and regulation

Abstract

Conditioned medium from pig Sertoli cells cultured in a chemically defined medium containing 3H-leucine contains a peptide with properties similar to that of human purified plasma and recombinant DNA somatomedin-C/insulin-like growth factor 1 (Sm-C/IGF-1). Purification of this peptide was achieved by affinity chromatography using mouse monoclonal anti-Sm-C/IGF-1 antibodies and reversephase high pressure liquid chromatography on a Bondapak C18 column. Polyacrylamide gel electrophoresis of the purified material gives a single spot after staining or in the autoradiogram, with identical molecular weight to that of pure human Sm-C/IGF-1. The purified peptide behaves like both the pure and recombinant DNA Sm-C/IGF-1 in the specific RIA and/or radioreceptor assays. Under basal conditions the amount of Sm-C/IGF-1 secreted by Sertoli cells was about 4 ng/10 6 cells/24h, but it decreased during culture. Neither growth hormone nor follitropin were able to stimulate Sm-C/IGF-1 secretion, but both fibroblast growth factor and epidermal growth factor enhanced two- to three-fold its secretion. In addition, cells pretreated for 24 h with these growth factors became sensitive to the stimulatory effect of FSH. Since previous in vitro studies have shown that Sm-C/IGF-1 is a mitogenic and differentiating factor for both Sertoli and Leydig cells, it is possible that Sm-C/IGF-1 secreted by Sertoli cells might play a paracrine and/or autocrine role in the regulation of testicular function.