[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.
Imhoff
J M
JM
Unité de Chimie des Protéines, Institut Pasteur, Paris, France.
Blondeau
X
X
Planchenault
T
T
Emod
I
I
Keil-Dlouha
V
V
D005353:Fibronectins / Q000737:chemistry / Q000302:isolation & purification* / Q000378:metabolism; D003012:Microbial Collagenase / Q000494:pharmacology*; D010447:Peptide Hydrolases / Q000378:metabolism*
D005353:Fibronectins; D010447:Peptide Hydrolases; D003012:Microbial Collagenase
Rôle d'une collagénase dans l'activité protéolytique latente de la fibronectine.