Direct activation of human neutrophil procollagenase by recombinant stromelysin

Knauper, V ORCID: https://orcid.org/0000-0002-3965-9924, Wilhelm, S, Seperack, P K, DeClerck, Y A, Langley, K E, Osthues, A and Tschesche, H 1993. Direct activation of human neutrophil procollagenase by recombinant stromelysin. Biochemical Journal 295 (2) , pp. 581-586. 10.1042/bj2950581

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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.

Item Type:	Article
Date Type:	Publication
Status:	Published
Schools:	Dentistry
Publisher:	Portland Press
ISSN:	0264-6021
Last Modified:	31 Aug 2023 11:45
URI:	https://orca.cardiff.ac.uk/id/eprint/161614

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