Function and structure of human leucocyte collagenase

Tschesche, H., Knauper, V. ORCID: https://orcid.org/0000-0002-3965-9924, Kleine, T., Reinemer, P., Schnierer, S., Grams, F. and Bode, W. 1994. Function and structure of human leucocyte collagenase. Protein Journal 13 (5) , pp. 460-461. 10.1007/978-1-4899-1031-8_34

Full text not available from this repository.

Abstract

Human leucocyte collagenase is one member of the growing protein family of matrix metalloproteinases (MMPs) [Knäuper et al., 1990]. It is a calcium-containing Zn-endoproteinase (MMP-8) that cleaves preferentially interstitial native triple-helical type I but also type II and type III collagen into one-quarter and three quarter fragments of the native chain length. If thus differs from the fibroblast interstitial collagenase that preferentially cleaves type III. About one-third of its mass of 65 kDa (for active enzyme) is carbohydrates in contrast to the homologous interstitial collagenase from fibroblasts which carries only a small carbohydrate portion [Tschesche et al., 1992]. The enzyme is stored in the specific granules of granulocytes and is released as a proenzyme, also designated latent enzyme, upon stimulation of the cells by various chemotactic agents, such as formylpeptides, LTB4, C5a, Fla and Zymosan amongst others, [Tschesche et al., 1989 and 1991]. Extracellular activation is then achieved by various different proteinases, such as trypsin, kallikrein, chymotrypsin, cathepsin G [Tschesche et al., 1992] or stromelysin [Knäuper et al., 1993]. However, the physiological process of activation is not yet fully understood, since activation was also observed by isolated leucocyte membranes [Tschesche unpublished].

Item Type:	Article
Status:	Published
Schools:	Dentistry
Publisher:	Springer
ISSN:	1572-3887
Last Modified:	15 Sep 2023 08:31
URI:	https://orca.cardiff.ac.uk/id/eprint/161646

Actions (repository staff only)

Edit Item