TIMP-3 facilitates binding of target metalloproteinases to the endocytic receptor LRP-1 and promotes scavenging of MMP-1.
Journal
Scientific reports
ISSN: 2045-2322
Titre abrégé: Sci Rep
Pays: England
ID NLM: 101563288
Informations de publication
Date de publication:
21 07 2020
21 07 2020
Historique:
received:
22
01
2020
accepted:
06
07
2020
entrez:
23
7
2020
pubmed:
23
7
2020
medline:
22
12
2020
Statut:
epublish
Résumé
Matrix metalloproteinases (MMPs) and the related families of disintegrin metalloproteinases (ADAMs) and ADAMs with thrombospondin repeats (ADAMTSs) play a crucial role in extracellular matrix (ECM) turnover and shedding of cell-surface molecules. The proteolytic activity of metalloproteinases is post-translationally regulated by their endogenous inhibitors, known as tissue inhibitors of metalloproteinases (TIMPs). Several MMPs, ADAMTSs and TIMPs have been reported to be endocytosed by the low-density lipoprotein receptor-related protein-1 (LRP-1). Different binding affinities of these proteins for the endocytic receptor correlate with different turnover rates which, together with differences in their mRNA expression, determines their nett extracellular levels. In this study, we used surface plasmon resonance to evaluate the affinity between LRP-1 and a number of MMPs, ADAMs, ADAMTSs, TIMPs and metalloproteinase/TIMP complexes. This identified MMP-1 as a new LRP-1 ligand. Among the proteins analyzed, TIMP-3 bound to LRP-1 with highest affinity (K
Identifiants
pubmed: 32694578
doi: 10.1038/s41598-020-69008-9
pii: 10.1038/s41598-020-69008-9
pmc: PMC7374751
doi:
Substances chimiques
LRP1 protein, human
0
Low Density Lipoprotein Receptor-Related Protein-1
0
Multiprotein Complexes
0
TIMP3 protein, human
0
Tissue Inhibitor of Metalloproteinase-3
0
Matrix Metalloproteinases
EC 3.4.24.-
Matrix Metalloproteinase 1
EC 3.4.24.7
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
12067Références
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