Metalloproteinases from rabbit bone culture medium degrade types IV and V collagens, laminin and fibronectin.
Gel-filtration chromatography of culture medium from rabbit bone explants separates three 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-molecular-weight 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.
D000818:Animals; D001842:Bone and Bones / Q000201:enzymology*; D002478:Cells, Cultured; D003094:Collagen / Q000378:metabolism; D004591:Electrophoresis, Polyacrylamide Gel; D010450:Endopeptidases / Q000378:metabolism*; D005353:Fibronectins / Q000378:metabolism; D006023:Glycoproteins / Q000378:metabolism; D007797:Laminin; D008565:Membrane Proteins / Q000378:metabolism; D008666:Metalloendopeptidases; D011817:Rabbits
D005353:Fibronectins; D006023:Glycoproteins; D007797:Laminin; D008565:Membrane Proteins; D003094:Collagen; D010450:Endopeptidases; D008666:Metalloendopeptidases