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

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 and Catherine Moali ()
Additional contact information
Sandrine Vadon-Le Goff: Tissue Biology and Therapeutic Engineering Laboratory (LBTI)
Agnès Tessier: Tissue Biology and Therapeutic Engineering Laboratory (LBTI)
Manon Napoli: Tissue Biology and Therapeutic Engineering Laboratory (LBTI)
Cindy Dieryckx: Tissue Biology and Therapeutic Engineering Laboratory (LBTI)
Julien Bauer: Tissue Biology and Therapeutic Engineering Laboratory (LBTI)
Mélissa Dussoyer: Tissue Biology and Therapeutic Engineering Laboratory (LBTI)
Priscillia Lagoutte: Tissue Biology and Therapeutic Engineering Laboratory (LBTI)
Célian Peyronnel: Tissue Biology and Therapeutic Engineering Laboratory (LBTI)
Lucie Essayan: Tissue Biology and Therapeutic Engineering Laboratory (LBTI)
Svenja Kleiser: Medical Center - University of Freiburg
Nicole Tueni: Institut Polytechnique de Paris
Emmanuel Bettler: Tissue Biology and Therapeutic Engineering Laboratory (LBTI)
Natacha Mariano: Tissue Biology and Therapeutic Engineering Laboratory (LBTI)
Elisabeth Errazuriz-Cerda: SFR Santé-Lyon Est
Carole Fruchart Gaillard: Médicaments et Technologies pour la Santé (MTS), SIMoS
Florence Ruggiero: Institut de Génomique Fonctionnelle de Lyon (IGFL)
Christoph Becker-Pauly: Unit for Degradomics of the Protease Web
Jean-Marc Allain: Institut Polytechnique de Paris
Leena Bruckner-Tuderman: Medical Center - University of Freiburg
Alexander Nyström: Medical Center - University of Freiburg
Catherine Moali: Tissue Biology and Therapeutic Engineering Laboratory (LBTI)

Nature Communications, 2023, vol. 14, issue 1, 1-18

Abstract: 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.

Date: 2023
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DOI: 10.1038/s41467-023-43401-0

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