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Identification of PCPE-2 as the endogenous specific inhibitor of human BMP-1/tolloid-like proteinases

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 imp...

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Autores principales: Vadon-Le Goff, Sandrine, Tessier, Agnès, Napoli, Manon, Dieryckx, Cindy, Bauer, Julien, Dussoyer, Mélissa, Lagoutte, Priscillia, Peyronnel, Célian, Essayan, Lucie, Kleiser, Svenja, Tueni, Nicole, Bettler, Emmanuel, Mariano, Natacha, Errazuriz-Cerda, Elisabeth, Fruchart Gaillard, Carole, Ruggiero, Florence, Becker-Pauly, Christoph, Allain, Jean-Marc, Bruckner-Tuderman, Leena, Nyström, Alexander, Moali, Catherine
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Nature Publishing Group UK 2023
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10696041/
https://www.ncbi.nlm.nih.gov/pubmed/38049428
http://dx.doi.org/10.1038/s41467-023-43401-0
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author Vadon-Le Goff, Sandrine
Tessier, Agnès
Napoli, Manon
Dieryckx, Cindy
Bauer, Julien
Dussoyer, Mélissa
Lagoutte, Priscillia
Peyronnel, Célian
Essayan, Lucie
Kleiser, Svenja
Tueni, Nicole
Bettler, Emmanuel
Mariano, Natacha
Errazuriz-Cerda, Elisabeth
Fruchart Gaillard, Carole
Ruggiero, Florence
Becker-Pauly, Christoph
Allain, Jean-Marc
Bruckner-Tuderman, Leena
Nyström, Alexander
Moali, Catherine
author_facet Vadon-Le Goff, Sandrine
Tessier, Agnès
Napoli, Manon
Dieryckx, Cindy
Bauer, Julien
Dussoyer, Mélissa
Lagoutte, Priscillia
Peyronnel, Célian
Essayan, Lucie
Kleiser, Svenja
Tueni, Nicole
Bettler, Emmanuel
Mariano, Natacha
Errazuriz-Cerda, Elisabeth
Fruchart Gaillard, Carole
Ruggiero, Florence
Becker-Pauly, Christoph
Allain, Jean-Marc
Bruckner-Tuderman, Leena
Nyström, Alexander
Moali, Catherine
author_sort Vadon-Le Goff, Sandrine
collection PubMed
description 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.
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spelling pubmed-106960412023-12-06 Identification of PCPE-2 as the endogenous specific inhibitor of human BMP-1/tolloid-like proteinases Vadon-Le Goff, Sandrine Tessier, Agnès Napoli, Manon Dieryckx, Cindy Bauer, Julien Dussoyer, Mélissa Lagoutte, Priscillia Peyronnel, Célian Essayan, Lucie Kleiser, Svenja Tueni, Nicole Bettler, Emmanuel Mariano, Natacha Errazuriz-Cerda, Elisabeth Fruchart Gaillard, Carole Ruggiero, Florence Becker-Pauly, Christoph Allain, Jean-Marc Bruckner-Tuderman, Leena Nyström, Alexander Moali, Catherine Nat Commun Article 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. Nature Publishing Group UK 2023-12-04 /pmc/articles/PMC10696041/ /pubmed/38049428 http://dx.doi.org/10.1038/s41467-023-43401-0 Text en © The Author(s) 2023 https://creativecommons.org/licenses/by/4.0/Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/ (https://creativecommons.org/licenses/by/4.0/) .
spellingShingle Article
Vadon-Le Goff, Sandrine
Tessier, Agnès
Napoli, Manon
Dieryckx, Cindy
Bauer, Julien
Dussoyer, Mélissa
Lagoutte, Priscillia
Peyronnel, Célian
Essayan, Lucie
Kleiser, Svenja
Tueni, Nicole
Bettler, Emmanuel
Mariano, Natacha
Errazuriz-Cerda, Elisabeth
Fruchart Gaillard, Carole
Ruggiero, Florence
Becker-Pauly, Christoph
Allain, Jean-Marc
Bruckner-Tuderman, Leena
Nyström, Alexander
Moali, Catherine
Identification of PCPE-2 as the endogenous specific inhibitor of human BMP-1/tolloid-like proteinases
title Identification of PCPE-2 as the endogenous specific inhibitor of human BMP-1/tolloid-like proteinases
title_full Identification of PCPE-2 as the endogenous specific inhibitor of human BMP-1/tolloid-like proteinases
title_fullStr Identification of PCPE-2 as the endogenous specific inhibitor of human BMP-1/tolloid-like proteinases
title_full_unstemmed Identification of PCPE-2 as the endogenous specific inhibitor of human BMP-1/tolloid-like proteinases
title_short Identification of PCPE-2 as the endogenous specific inhibitor of human BMP-1/tolloid-like proteinases
title_sort identification of pcpe-2 as the endogenous specific inhibitor of human bmp-1/tolloid-like proteinases
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10696041/
https://www.ncbi.nlm.nih.gov/pubmed/38049428
http://dx.doi.org/10.1038/s41467-023-43401-0
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