Autor: |
Sandrine Vadon-Le Goff, Agnès Tessier, Manon Napoli, Cindy Dieryckx, Julien Bauer, Mélissa Dussoyer, Priscillia Lagoutte, Célian Peyronnel, Lucie Essayan, Svenja Kleiser, Nicole Tueni, Emmanuel Bettler, Natacha Mariano, Elisabeth Errazuriz-Cerda, Carole Fruchart Gaillard, Florence Ruggiero, Christoph Becker-Pauly, Jean-Marc Allain, Leena Bruckner-Tuderman, Alexander Nyström, Catherine Moali |
Jazyk: |
angličtina |
Rok vydání: |
2023 |
Předmět: |
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Zdroj: |
Nature Communications, Vol 14, Iss 1, Pp 1-18 (2023) |
Druh dokumentu: |
article |
ISSN: |
2041-1723 |
DOI: |
10.1038/s41467-023-43401-0 |
Popis: |
Abstract BMP-1/tolloid-like proteinases (BTPs) are major players in tissue morphogenesis, growth and repair. They act by promoting the deposition of structural extracellular matrix proteins and by controlling the activity of matricellular proteins and TGF-β superfamily growth factors. They have also been implicated in several pathological conditions such as fibrosis, cancer, metabolic disorders and bone diseases. Despite this broad range of pathophysiological functions, the putative existence of a specific endogenous inhibitor capable of controlling their activities could never be confirmed. Here, we show that procollagen C-proteinase enhancer-2 (PCPE-2), a protein previously reported to bind fibrillar collagens and to promote their BTP-dependent maturation, is primarily a potent and specific inhibitor of BTPs which can counteract their proteolytic activities through direct binding. PCPE-2 therefore differs from the cognate PCPE-1 protein and extends the possibilities to fine-tune BTP activities, both in physiological conditions and in therapeutic settings. |
Databáze: |
Directory of Open Access Journals |
Externí odkaz: |
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