Evidence map›Paper›PMID 32694578›Full record

ArticleScientific reports2020

TIMP-3 facilitates binding of target metalloproteinases to the endocytic receptor LRP-1 and promotes scavenging of MMP-1.

Anna P Carreca, Veronica M Pravatà, Matthew Markham, Simone Bonelli, Gillian Murphy, Hideaki Nagase, Linda Troeberg, Simone D Scilabra

Abstract read
In one paragraph

Article in Scientific reports, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed, 1 pooled it
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

24 citing papers in PubMed, 1 synthesis or guideline pooled it.

  1. Pooled it
  2. Article
  3. Matrix Metalloproteinase 14 in Corneal Neovascularization.International journal of molecular sciences · 2026
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  11. The TIMP protein family: diverse roles in pathophysiology.American journal of physiology. Cell physiology · 2024
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  12. ADAM10-a "multitasker" in sepsis: focus on its posttranslational target.Inflammation research : official journal of the European Histamine Research Society ... [et al.] · 2023
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

8 authors.

Anna P CarrecaDepartment of Research, Fondazione Ri.MED - ISMETT, Via Ernesto Tricomi 5, 90145, Palermo, Italy.
Veronica M PravatàDivision of Gene Regulation and Expression, School of Life Sciences, University of Dundee, Dundee, DD1 5EH, UK.
Matthew MarkhamNorwich Medical School, University of East Anglia, Norwich, NR4 7UQ, UK.
Simone BonelliDepartment of Research, Fondazione Ri.MED - ISMETT, Via Ernesto Tricomi 5, 90145, Palermo, Italy.
Gillian MurphyLi Ka Shing Centre, Cancer Research UK, Cambridge Institute, Robinson Way, Cambridge, CB2 0RE, UK.
Hideaki NagaseNuffield Department of Orthopaedics, Rheumatology and Musculoskeletal Sciences, Kennedy Institute of Rheumatology, University of Oxford, Headington, Oxford, UK.
Linda Troeberg *Norwich Medical School, University of East Anglia, Norwich, NR4 7UQ, UK.
Simone D Scilabra *Department of Research, Fondazione Ri.MED - ISMETT, Via Ernesto Tricomi 5, 90145, Palermo, Italy. sdscilabra@fondazionerimed.com.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

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

Indexed as

EndocytosisHumansKineticsLow Density Lipoprotein Receptor-Related Protein-1Matrix Metalloproteinase 1Matrix MetalloproteinasesMultiprotein ComplexesProtein BindingTissue Inhibitor of Metalloproteinase-3Low Density Lipoprotein Receptor-Related Protein-1LRP1 protein, humanMatrix Metalloproteinase 1Matrix MetalloproteinasesMultiprotein ComplexesTIMP3 protein, humanTissue Inhibitor of Metalloproteinase-3

Identifiers

PMID32694578
PMCPMC7374751

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.