Activation of human neutrophil procollagenase by stromelysin 2

Knauper, Vera ORCID: https://orcid.org/0000-0002-3965-9924, Murphy, Gillian and Tschesche, Harald 1996. Activation of human neutrophil procollagenase by stromelysin 2. European Journal of Biochemistry 235 (1-2) , pp. 187-191. 10.1111/j.1432-1033.1996.00187.x

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Abstract

Neutrophil procollagenase (MMP-8) was efficiently activated by incubation with active stromelysin 2 (MMP-10). A single-step activation mechanism involving the cleavage of the Gly78-Phe79 peptide bond at the end of the propeptide domain was observed. Determination of the collagenolytic activity revealed the generation of active neutrophil collagenase displaying high specific activity. When compared with the specific activity following mercurial activation, which generates active collagenase by autoproteolytic cleavage of either Phe79-Met80 or Met80-Leu81 peptide bonds [Bläser, J., Knäuper, V., Osthues, A., Reinke, H. & Tschesche, H. (1991) Eur J. Biochem. 202, 1223–1230], the specific activity of the stromelysin-2-activated enzyme was considerably higher. Thus, human neutrophil procollagenase was ‘superactivated’ by stromelysin 2, as was recently shown for the stromelysin-1-activated enzyme [Knäuper, V., Wilhelm, S. M., Seperack, P. K., De Clerck, Y. A., Langley, K. E., Osthues, A. & Tschesche, H. (1993a) Biochem. J. 295, 581–586].

Item Type:	Article
Date Type:	Publication
Status:	Published
Schools:	Dentistry
Publisher:	Wiley: No OnlineOpen
ISSN:	0014-2956
Last Modified:	15 Sep 2023 09:56
URI:	https://orca.cardiff.ac.uk/id/eprint/161609

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