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

The Journal of Investigative Dermatology
Daniel KronenbergChristoph Becker-Pauly

Abstract

Meprins α and β, 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 α and β 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 α is also shown to be expressed by human dermal fibroblasts. In the dermis of fibrotic skin (keloids), expression of meprin α increases and meprin β begins to be detected. Our study s...Continue Reading

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Citations

Sep 4, 2012·Cellular and Molecular Life Sciences : CMLS·Tamara JeffersonChristoph Becker-Pauly
Aug 14, 2013·Proceedings of the National Academy of Sciences of the United States of America·Claudia BroderChristoph Becker-Pauly
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Jun 16, 2019·Cellular and Molecular Life Sciences : CMLS·Franka ScharfenbergChristoph Becker-Pauly

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