Human proteinase 3 resistance to inhibition extends to alpha-2 macroglobulin.


Journal

The FEBS journal
ISSN: 1742-4658
Titre abrégé: FEBS J
Pays: England
ID NLM: 101229646

Informations de publication

Date de publication:
09 2020
Historique:
received: 27 10 2019
revised: 12 12 2019
accepted: 27 01 2020
pubmed: 30 1 2020
medline: 18 5 2021
entrez: 30 1 2020
Statut: ppublish

Résumé

Polymorphonuclear neutrophils contain at least four serine endopeptidases, namely neutrophil elastase (NE), proteinase 3 (PR3), cathepsin G (CatG), and NSP4, which contribute to the regulation of infection and of inflammatory processes. In physiological conditions, endogenous inhibitors including α2-macroglobulin (α2-M), serpins [α1-proteinase inhibitor (α1-PI)], monocyte neutrophil elastase inhibitor (MNEI), α1-antichymotrypsin, and locally produced chelonianins (elafin, SLPI) control excessive proteolytic activity of neutrophilic serine proteinases. In contrast to human NE (hNE), hPR3 is weakly inhibited by α1-PI and MNEI but not by SLPI. α2-M is a large spectrum inhibitor that traps a variety of proteinases in response to cleavage(s) in its bait region. We report here that α2-M was more rapidly processed by hNE than hPR3 or hCatG. This was confirmed by the observation that the association between α2-M and hPR3 is governed by a k

Identifiants

pubmed: 31995266
doi: 10.1111/febs.15229
doi:

Substances chimiques

Peptides 0
Pregnancy-Associated alpha 2-Macroglobulins 0
Recombinant Proteins 0
Myeloblastin EC 3.4.21.76

Types de publication

Journal Article Research Support, Non-U.S. Gov't

Langues

eng

Sous-ensembles de citation

IM

Pagination

4068-4081

Informations de copyright

© 2020 INSERM UMR. The FEBS Journal published by John Wiley & Sons Ltd on behalf of Federation of European Biochemical Societies.

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Auteurs

Koffi N'Guessan (K)

INSERM UMR-1100, CEPR "Centre d'Etude des Pathologies Respiratoires", Tours, France.
Université de Tours, France.

Renata Grzywa (R)

Faculty of Chemistry, Department of Organic and Medicinal Chemistry, Wroclaw University of Science and Technology, Poland.

Seda Seren (S)

INSERM UMR-1100, CEPR "Centre d'Etude des Pathologies Respiratoires", Tours, France.
Université de Tours, France.

Guillaume Gabant (G)

Centre de Biophysique Moléculaire, UPR4301, CNRS, Affiliated with Université d'Orléans, Orléans, France.

Maria A Juliano (MA)

Departamento de Biofísica, Escola Paulista Medicina, Universidade Federal de São Paulo, São Paulo, Brazil.

Marc Moniatte (M)

Proteomics Core Facility, École Polytechnique Fédérale de Lausanne (EPFL), Lausanne, Switzerland.

Alain van Dorsselaer (A)

LSMBO, CNRS UMR-7178 (CNRS-UdS), ECPM, Institut Pluridisciplinaire Hubert Curien, Strasbourg, France.

Joseph G Bieth (JG)

Laboratoire d'Enzymologie, INSERM U392, Université Louis Pasteur de Strasbourg, Illkirch, France.

Christine Kellenberger (C)

Laboratoire de Chimie Bactérienne, UMR-7283, CNRS, Marseille, France.

Francis Gauthier (F)

INSERM UMR-1100, CEPR "Centre d'Etude des Pathologies Respiratoires", Tours, France.
Université de Tours, France.

Magdalena Wysocka (M)

Faculty of Chemistry, University of Gdansk, Gdansk, Poland.

Adam Lesner (A)

Faculty of Chemistry, University of Gdansk, Gdansk, Poland.

Marcin Sienczyk (M)

Faculty of Chemistry, Department of Organic and Medicinal Chemistry, Wroclaw University of Science and Technology, Poland.

Martine Cadene (M)

Centre de Biophysique Moléculaire, UPR4301, CNRS, Affiliated with Université d'Orléans, Orléans, France.

Brice Korkmaz (B)

INSERM UMR-1100, CEPR "Centre d'Etude des Pathologies Respiratoires", Tours, France.
Université de Tours, France.

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