Homotrimeric MMP-9 is an active hitchhiker on alpha-2-macroglobulin partially escaping protease inhibition and internalization through LRP-1.


Journal

Cellular and molecular life sciences : CMLS
ISSN: 1420-9071
Titre abrégé: Cell Mol Life Sci
Pays: Switzerland
ID NLM: 9705402

Informations de publication

Date de publication:
Aug 2020
Historique:
received: 07 08 2019
accepted: 03 10 2019
revised: 27 09 2019
pubmed: 24 10 2019
medline: 1 8 2020
entrez: 24 10 2019
Statut: ppublish

Résumé

Proteolysis is a crucial process in life, tightly controlled by numerous natural protease inhibitors. In human blood, alpha-2-macroglobulin is an emergency protease inhibitor preventing coagulation and damage to endothelia and leukocytes. With the use of a unique protease trapping mechanism, alpha-2-macroglobulin lures active proteases into its snap-trap, shields these from potential substrates and 'flags' their complex for elimination by receptor-mediated endocytosis. Matrix metalloprotease-9/gelatinase B is a secreted protease increased in blood of patients with inflammations, vascular disorders and cancers. Matrix metalloprotease-9 occurs as monomers and stable homotrimers, but the reason for their co-existence remains obscure. We discovered that matrix metalloprotease-9 homotrimers undergo reduced anti-proteolytic regulation by alpha-2-macroglobulin and are able to travel as a proteolytically active hitchhiker on alpha-2-macroglobulin. As a comparison, we revealed that monomeric active matrix metalloprotease-9 is efficiently trapped by human plasma alpha-2-macroglobulin and this masks the detection of activated matrix metalloprotease-9 with standard analysis techniques. In addition, we show that alpha-2-macroglobulin/trimer complexes escape clearance through the receptor low-density lipoprotein receptor-related protein 1, also known as the alpha-2-macroglobulin receptor. Thus, the biochemistry and biology of matrix metalloprotease-9 monomers and trimers are completely different as multimerization enables active matrix metalloprotease-9 to partially avoid alpha-2-macroglobulin regulation both by direct protease inhibition and by removal from the extracellular space by receptor-mediated endocytosis. Finally, for the biomarker field, the analysis of alpha-2-macroglobulin/protease complexes with upgraded technology is advocated as a quotum for protease activation in human plasma samples.

Identifiants

pubmed: 31642940
doi: 10.1007/s00018-019-03338-4
pii: 10.1007/s00018-019-03338-4
doi:

Substances chimiques

Low Density Lipoprotein Receptor-Related Protein-1 0
Pregnancy-Associated alpha 2-Macroglobulins 0
Matrix Metalloproteinase 9 EC 3.4.24.35

Types de publication

Journal Article

Langues

eng

Sous-ensembles de citation

IM

Pagination

3013-3026

Subventions

Organisme : FWO-vlaanderen
ID : G0A7516N
Organisme : FWO-vlaanderen
ID : 12Z0920N
Organisme : FWO-Vlaanderen
ID : G0A5716N

Auteurs

Xena Serifova (X)

Laboratory of Immunobiology, Department of Microbiology and Immunology, Rega Institute for Medical Research, University of Leuven, KU Leuven, Herestraat 49, Bus 1044, 3000, Leuven, Belgium.

Estefania Ugarte-Berzal (E)

Laboratory of Immunobiology, Department of Microbiology and Immunology, Rega Institute for Medical Research, University of Leuven, KU Leuven, Herestraat 49, Bus 1044, 3000, Leuven, Belgium.

Ghislain Opdenakker (G)

Laboratory of Immunobiology, Department of Microbiology and Immunology, Rega Institute for Medical Research, University of Leuven, KU Leuven, Herestraat 49, Bus 1044, 3000, Leuven, Belgium.

Jennifer Vandooren (J)

Laboratory of Immunobiology, Department of Microbiology and Immunology, Rega Institute for Medical Research, University of Leuven, KU Leuven, Herestraat 49, Bus 1044, 3000, Leuven, Belgium. Jennifer.vandooren@kuleuven.be.

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Classifications MeSH