title: [Role of a collagenase in the latent proteolytic activity of fibronectin].
abstract: 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.
authors.affiliation: Unité de Chimie des Protéines, Institut Pasteur, Paris, France.
authors.forename: J M
authors.initials: JM
authors.lastname: Imhoff
authors.forename: X
authors.initials: X
authors.lastname: Blondeau
authors.forename: T
authors.initials: T
authors.lastname: Planchenault
authors.forename: I
authors.initials: I
authors.lastname: Emod
authors.forename: V
authors.initials: V
authors.lastname: Keil-Dlouha
mesh_terms: D005353:Fibronectins / Q000737:chemistry / Q000302:isolation & purification* / Q000378:metabolism; D003012:Microbial Collagenase / Q000494:pharmacology*; D010447:Peptide Hydrolases / Q000378:metabolism*
chemical_list: D005353:Fibronectins; D010447:Peptide Hydrolases; D003012:Microbial Collagenase
vernacular_title: Rôle d'une collagénase dans l'activité protéolytique latente de la fibronectine.