ROLE OF A COLLAGENASE IN THE LATENT PROTEOLYTIC ACTIVITY OF FIBRONECTIN

Fibronectin fragments generated by Achromobacter iophagus collagenase exhibit a gelatinolytic activity. This activity is inhibited by phenyl-methyl-sulfonyl fluoride and pepstatin A. After separation of this collagenase digest of fibronectin on heparin Ultrogel, a laminase activity was also evidenced using laminin and the synthetic peptide Gly-Pro-Ala-Gly-Pro-Arg as substrates. Different results were obtained with a cathepsin D digest of fibronectin that exhibited gelatinolytic and laminolytic activities only after incubation with Ca++. This suggests that the proteinases produced by hydrolysis of fibronectin enhance the effect of collagenase on extracellular matrix proteins.