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Metalloproteases meprin α and meprin β were recently discovered as procollagen proteinases, capable of cleaving off the globular C- and N-terminal prodomains of fibrillar collagen type I and type III. This proteolytic process is indeed sufficient to induce collagen fibril assembly as visualized by transmission electron microscopy. The biological relevance was demonstrated with the help of meprin α and meprin β knock-out mice, which exhibit decreased collagen deposition in skin resulting in impaired tensile strength. On the other hand, overexpression of meprin metalloproteases was found under fibrotic conditions in the skin (keloids) and the lung (pulmonary hypertension). Thus, regulation of meprin activity by specific inhibition to reduce collagen maturation might be a suitable approach for the treatment of certain pathological conditions. Copyright © 2015 International Society of Matrix Biology. Published by Elsevier B.V. All rights reserved.

Citation

Johannes Prox, Philipp Arnold, Christoph Becker-Pauly. Meprin α and meprin β: Procollagen proteinases in health and disease. Matrix biology : journal of the International Society for Matrix Biology. 2015 May-Jul;44-46:7-13

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PMID: 25617491

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