Purification and partial characterization of prostate-derived growth factor

Abstract

A potent growth-promoting polypeptide, the prostate-derived growth factor (PrDGF), has been purified to apparent homogeneity from acid extracts of rat prostatic tissue using ion-exchange, reverse-phase, and gel-permeation chromatography. PrDGF migrates as a single protein-staining band in NaDodSO4/PAGE in precise correspondence to extractable PrDGF activity in nonstained NaDodSO4 gels. PrDGF is acid- and heat-stable but is sensitive to reduction or protease treatment. PrDGF is an acidic (pI 5.0) protein of approximately equal to 25 kDa in NaDodSO4/polyacrylamide gels and of approximately equal to 6-8 kDa in reduced NaDodSO4/polyacrylamide gels. PrDGF stimulates the linear incorporation of [methyl-3H]thymidine into normal rat kidney cells between 0 and 16 ng/ml. PrDGF appears to differ from other known growth factors in chemical composition and biological properties, suggesting that PrDGF is a previously undescribed growth factor.