Processing of procollagen III by meprins: new players in extracellular matrix assembly?

Kronenberg, Daniel; Bruns, Bernd C; Moali, Catherine; Vadon-Le Goff, Sandrine; Sterchi, Erwin E; Traupe, Heiko; Böhm, Markus; Hulmes, David J S; Stöcker, Walter; Becker-Pauly, Christoph (2010). Processing of procollagen III by meprins: new players in extracellular matrix assembly? Journal of Investigative Dermatology, 130(12), pp. 2727-35. New York, N.Y.: Nature Publishing 10.1038/jid.2010.202

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Meprins ? and ?, a subgroup of zinc metalloproteinases belonging to the astacin family, are known to cleave components of the extracellular matrix, either during physiological remodeling or in pathological situations. In this study we present a new role for meprins in matrix assembly, namely the proteolytic processing of procollagens. Both meprins ? and ? release the N- and C-propeptides from procollagen III, with such processing events being critical steps in collagen fibril formation. In addition, both meprins cleave procollagen III at exactly the same site as the procollagen C-proteinases, including bone morphogenetic protein-1 (BMP-1) and other members of the tolloid proteinase family. Indeed, cleavage of procollagen III by meprins is more efficient than by BMP-1. In addition, unlike BMP-1, whose activity is stimulated by procollagen C-proteinase enhancer proteins (PCPEs), the activity of meprins on procollagen III is diminished by PCPE-1. Finally, following our earlier observations of meprin expression by human epidermal keratinocytes, meprin ? is also shown to be expressed by human dermal fibroblasts. In the dermis of fibrotic skin (keloids), expression of meprin ? increases and meprin ? begins to be detected. Our study suggests that meprins could be important players in several remodeling processes involving collagen fiber deposition.

Item Type:	Journal Article (Original Article)
Division/Institute:	04 Faculty of Medicine > Pre-clinic Human Medicine > Institute of Biochemistry and Molecular Medicine
UniBE Contributor:	Sterchi, Erwin-Ernst
ISSN:	0022-202X
Publisher:	Nature Publishing
Language:	English
Submitter:	Factscience Import
Date Deposited:	04 Oct 2013 14:12
Last Modified:	05 Dec 2022 14:01
Publisher DOI:	10.1038/jid.2010.202
PubMed ID:	20631730
Web of Science ID:	000284151000009
URI:	https://boris.unibe.ch/id/eprint/2419 (FactScience: 204912)