Collagenase activation of latent matrix-degrading proteinases from human plasma fibronectin.
Fibronectin contains two latent gelatinolytic enzymes, FN-gelatinase and FN-laminase that can be activated in the presence of Ca2+ from the purified cathepsin D-produced 190-kDa fibronectin fragment. The results of this work show that Achromobacter collagenase cleaves fibronectin and generates an active FN-gelatinase. In contrast to the cathepsin D digest, the collagenase digest directly exhibits gelatinolytic activity without additional activation. The gelatinolytic activity of the total collagenase digest can be inhibited by phenylmethanesulfonyl fluoride, a serine proteinase inhibitor and by pepstatin A, an aspartic-acid proteinase inhibitor. FN-laminase activity, when assayed with its synthetic substrate GPAGPR and also with laminin was revealed after separation of the collagenase digest of fibronectin on heparin Ultrogel. FN-gelatinase and FN-laminase activities were found in heparin unretained and heparin strongly retained fractions. These results have demonstrated that in contrast to cathepsin D, Achromobacter collagenase activates two matrix-degrading proteinases from fibronectin, FN-Gelatinase und FN-Laminase.
Imhoff
J M
JM
Unité de Chimie des Protéines, Institut Pasteur, Paris.
Blondeau
X
X
Planchenault
T
T
Emod
I
I
Keil-Dlouha
V
V
D000421:Alcaligenes / Q000201:enzymology; D002402:Cathepsin D / Q000378:metabolism; D003094:Collagen / Q000378:metabolism*; D004789:Enzyme Activation; D005353:Fibronectins / Q000032:analysis / Q000378:metabolism*; D005780:Gelatin / Q000378:metabolism*; D006801:Humans; D003012:Microbial Collagenase / Q000378:metabolism*; D010446:Peptide Fragments / Q000032:analysis* / Q000378:metabolism; D011480:Protease Inhibitors; D013379:Substrate Specificity
D005353:Fibronectins; D010446:Peptide Fragments; D011480:Protease Inhibitors; D005780:Gelatin; D003094:Collagen; D002402:Cathepsin D; D003012:Microbial Collagenase