Identification of PCPE-2 as the endogenous specific inhibitor of human BMP-1/tolloid-like proteinases - Inria - Institut national de recherche en sciences et technologies du numérique

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Journal Articles Nature Communications Year : 2023

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

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Sandrine Vadon-Le Goff

Function : Author
PersonId : 738363
IdHAL : sandrine-vadon-le-goff
ORCID : 0000-0002-4582-2273
IdRef : 253123305

Laboratoire de Biologie Tissulaire et d'ingénierie Thérapeutique UMR 5305

Agnès Tessier

Function : Author

Laboratoire de Biologie Tissulaire et d'ingénierie Thérapeutique UMR 5305

University of Freiburg [Freiburg]

Manon Napoli

Function : Author
PersonId : 1327126
ORCID : 0009-0006-9387-9713

Laboratoire de Biologie Tissulaire et d'ingénierie Thérapeutique UMR 5305

Cindy Dieryckx

Function : Author

Laboratoire de Biologie Tissulaire et d'ingénierie Thérapeutique UMR 5305

Julien Bauer

Function : Author

Laboratoire de Biologie Tissulaire et d'ingénierie Thérapeutique UMR 5305

Mélissa Dussoyer

Function : Author

Laboratoire de Biologie Tissulaire et d'ingénierie Thérapeutique UMR 5305

Priscillia Lagoutte

Function : Author

Laboratoire de Biologie Tissulaire et d'ingénierie Thérapeutique UMR 5305

Célian Peyronnel

Function : Author

Laboratoire de Biologie Tissulaire et d'ingénierie Thérapeutique UMR 5305

Lucie Essayan

Function : Author

Laboratoire de Biologie Tissulaire et d'ingénierie Thérapeutique UMR 5305

Svenja Kleiser

Function : Author
PersonId : 1327127
ORCID : 0000-0003-2448-1710

University of Freiburg [Freiburg]

Nicole Tueni

Function : Author
PersonId : 1327128
ORCID : 0000-0003-3873-0618

Mathematical and Mechanical Modeling with Data Interaction in Simulations for Medicine

Emmanuel Bettler

Function : Author

Laboratoire de Biologie Tissulaire et d'ingénierie Thérapeutique UMR 5305

Natacha Mariano

Function : Author

Laboratoire de Biologie Tissulaire et d'ingénierie Thérapeutique UMR 5305

Elisabeth Errazuriz-Cerda

Function : Author

Université de Lyon

Carole Fruchart Gaillard

Function : Author

Commissariat à l'énergie atomique et aux énergies alternatives

CEA- Saclay

Service d'Ingénierie Moléculaire pour la Santé (ex SIMOPRO)

Médicaments et Technologies pour la Santé

Florence Ruggiero

Function : Author
PersonId : 180172
IdHAL : florence-ruggiero
ORCID : 0000-0003-2915-5359
IdRef : 126183309

Institut de Génomique Fonctionnelle de Lyon

Christoph Becker-Pauly

Function : Author
PersonId : 1327129
ORCID : 0000-0002-5100-9916

Christian-Albrechts-Universität zu Kiel = Christian-Albrechts University of Kiel = Université Christian-Albrechts de Kiel

Jean-Marc Allain

Function : Author
PersonId : 7447
IdHAL : jean-marcallain
ORCID : 0000-0002-5273-7739
IdRef : 092413722

Mathematical and Mechanical Modeling with Data Interaction in Simulations for Medicine

Leena Bruckner-Tuderman

Function : Author

University of Freiburg [Freiburg]

Alexander Nyström

Function : Author
PersonId : 1327130
ORCID : 0000-0002-4666-2240

University of Freiburg [Freiburg]

Catherine Moali

Function : Author
PersonId : 774626
ORCID : 0000-0003-2479-4290
IdRef : 078123119

Laboratoire de Biologie Tissulaire et d'ingénierie Thérapeutique UMR 5305

Abstract

AbstractBMP-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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Life Sciences [q-bio]

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Identification of PCPE-2.pdf (5.73 Mo)

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https://hal.science/hal-04350568

Submitted on : Wednesday, January 17, 2024-5:04:20 PM

Last modification on : Wednesday, May 15, 2024-1:20:04 PM

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hal-04350568 , version 1 (17-01-2024)

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HAL Id : hal-04350568 , version 1
DOI : 10.1038/s41467-023-43401-0

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Sandrine Vadon-Le Goff, Agnès Tessier, Manon Napoli, Cindy Dieryckx, Julien Bauer, et al.. Identification of PCPE-2 as the endogenous specific inhibitor of human BMP-1/tolloid-like proteinases. Nature Communications, 2023, 14 (1), ⟨10.1038/s41467-023-43401-0⟩. ⟨hal-04350568⟩

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