Identification of PCPE-2 as the endogenous specific inhibitor of human BMP-1/tolloid-like proteinases.
Journal
Nature communications
ISSN: 2041-1723
Titre abrégé: Nat Commun
Pays: England
ID NLM: 101528555
Informations de publication
Date de publication:
04 Dec 2023
04 Dec 2023
Historique:
received:
24
08
2022
accepted:
08
11
2023
medline:
6
12
2023
pubmed:
5
12
2023
entrez:
4
12
2023
Statut:
epublish
Résumé
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.
Identifiants
pubmed: 38049428
doi: 10.1038/s41467-023-43401-0
pii: 10.1038/s41467-023-43401-0
pmc: PMC10696041
doi:
Substances chimiques
Peptide Hydrolases
EC 3.4.-
Glycoproteins
0
Extracellular Matrix Proteins
0
Intercellular Signaling Peptides and Proteins
0
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
8020Informations de copyright
© 2023. The Author(s).
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