title: Direct activation of human neutrophil procollagenase by recombinant stromelysin.
abstract: Human neutrophil procollagenase was activated by incubation with recombinant active stromelysin. Activation was achieved by cleavage of the Gly78-Phe79 peptide bond at the end of the propeptide domain in a single-step activation mechanism. In addition, accelerated activation was achieved when N-terminally truncated, latent collagenase (with Phe49 as its N-terminal residue) was incubated with recombinant active stromelysin. Determination of the specific activity of recombinant-stromelysin-activated neutrophil collagenase with dinitrophenyl-octapeptide or type I collagen demonstrated the generation of high specific activity. The specific activity of stromelysin-activated enzyme was considerably higher than that of trypsin- or HgCl2-activated collagenase. Thus human neutrophil collagenase is superactivated, like the homologous fibroblast collagenase [Murphy, Cockett, Stephens, Smith and Docherty (1987) Biochem. J. 248, 265-268]. The occurrence of Phe79 at the N-terminus of the neutrophil collagenase seemed to be critical for superactivation, which is in agreement with data published by Suzuki, Enghild, Morodomi, Salvesen and Nagase [(1990) Biochemistry 29, 10261-10270] on fibroblast collagenase.
authors.affiliation: University of Bielefeld, Faculty of Chemistry, Department of Biochemistry, Germany.
authors.forename: V
authors.initials: V
authors.lastname: Knäuper
authors.forename: S M
authors.initials: SM
authors.lastname: Wilhelm
authors.forename: P K
authors.initials: PK
authors.lastname: Seperack
authors.forename: Y A
authors.initials: YA
authors.lastname: DeClerck
authors.forename: K E
authors.initials: KE
authors.lastname: Langley
authors.forename: A
authors.initials: A
authors.lastname: Osthues
authors.forename: H
authors.initials: H
authors.lastname: Tschesche
mesh_terms: D000595:Amino Acid Sequence; D017364:Collagenases / Q000737:chemistry / Q000378:metabolism*; D004789:Enzyme Activation; D004792:Enzyme Precursors / Q000037:antagonists & inhibitors / Q000737:chemistry / Q000378:metabolism*; D004795:Enzyme Stability; D006023:Glycoproteins / Q000494:pharmacology; D006801:Humans; D019278:Matrix Metalloproteinase 3; D061965:Matrix Metalloproteinase Inhibitors; D008666:Metalloendopeptidases / Q000378:metabolism / Q000494:pharmacology*; D008969:Molecular Sequence Data; D009363:Neoplasm Proteins / Q000494:pharmacology; D009504:Neutrophils / Q000201:enzymology*; D011994:Recombinant Proteins / Q000494:pharmacology; D019716:Tissue Inhibitor of Metalloproteinase-2; D019714:Tissue Inhibitor of Metalloproteinases
chemical_list: D004792:Enzyme Precursors; D006023:Glycoproteins; D061965:Matrix Metalloproteinase Inhibitors; D009363:Neoplasm Proteins; D011994:Recombinant Proteins; D019714:Tissue Inhibitor of Metalloproteinases; D019716:Tissue Inhibitor of Metalloproteinase-2; D017364:Collagenases; D008666:Metalloendopeptidases; C022440:procollagenase; D019278:Matrix Metalloproteinase 3