Metalloproteinases from rabbit bone culture medium degrade types IV and V collagens, laminin and fibronectin

Abstract

Gel-filtration chromatography of culture medium from rabbit bone explants separates 3 latent metalloproteinases with activities against collagen, proteoglycan and gelatin, respectively. The fractions degrading proteoglycan also degrade laminin, fibronectin and the polymeric products of pepsin-solubilized type IV collagen and can also solubilize insoluble type IV collagen. The fractions degrading gelatin are capable of degrading solubilized type V and 1.alpha.,2.alpha.,3.alpha. (cartilage) collagens, as well as the lower-MW products of pepsin-solubilized type IV collagen. All activities can be inhibited by 1,10-phenanthroline and occur in either partially or totally latent forms that can be activated by 4-aminophenylmercuric acetate.