Evidence map›Paper›PMID 20156196›Full record

ArticleThe Biochemical journal2010

Transglutaminase-2: a new endostatin partner in the extracellular matrix of endothelial cells.

Clément Faye, Antonio Inforzato, Marine Bignon, Daniel J Hartmann, Laurent Muller, Lionel Ballut, Bjorn R Olsen, Anthony J Day, Sylvie Ricard-Blum

Open access · greenAbstract read
In one paragraph

Article in The Biochemical journal, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
3.8field-weighted citation impact, top 7% of its field
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

25 citing papers in PubMed, 50 citations in OpenAlex.

  1. Review
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  7. Review
  8. Review
  9. Article
  10. Review
  11. Article
  12. Review
  13. Tissue Transglutaminase Mediated Tumor-Stroma Interaction Promotes Pancreatic Cancer Progression.Clinical cancer research : an official journal of the American Association for Cancer Research · 2015
    Article
  14. Regulation of allergic lung inflammation by endothelial cell transglutaminase 2.American journal of physiology. Lung cellular and molecular physiology · 2015
    Article
  15. Review
  16. Article
  17. Article
  18. Article
  19. Inhibition of allergic inflammation by supplementation with 5-hydroxytryptophan.American journal of physiology. Lung cellular and molecular physiology · 2012
    Article
  20. Article
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

9 authors at 4 institutions in 3 countries.

Clément FayeInstitut de Biologie et Chimie des Protéines, UMR Centre National de la Recherche Scientifique, University Lyon, France.
Antonio Inforzato
Marine Bignon
Daniel J Hartmann
Laurent Muller
Lionel Ballut
Bjorn R Olsen
Anthony J Day
Sylvie Ricard-Blum
Université Claude Bernard Lyon 1 · FRInserm · FRWellcome Centre for Cell-Matrix Research · GBHarvard University · US

Funding

COLLAGEN GENE STRUCTURE AND EXPRESSIONR01AR036820 · NIAMS · HARVARD UNIVERSITY (MEDICAL SCHOOL) · PI OLSEN, BJORN REINO · 1986 to 2013
$6.7M
NIAMS NIH HHS R01 AR036820Wellcome Trust 088785
6 · The paper itself

Abstract

Endostatin, a C-terminal fragment of collagen XVIII, binds to TG-2 (transglutaminase-2) in a cation-dependent manner. Recombinant human endostatin binds to TG-2 with an affinity in the nanomolar range (Kd=6.8 nM). Enzymatic assays indicated that, in contrast with other extracellular matrix proteins, endostatin is not a glutaminyl substrate of TG-2 and is not cross-linked to itself by the enzyme. Two arginine residues of endostatin, Arg27 and Arg139, are crucial for its binding to TG-2. They are also involved in the binding to heparin [Sasaki, Larsson, Kreuger, Salmivirta, Claesson-Welsh, Lindahl, Hohenester and Timpl (1999) EMBO J. 18, 6240-6248], and to alpha5beta1 and alphavbeta3 integrins [Faye, Moreau, Chautard, Jetne, Fukai, Ruggiero, Humphries, Olsen and Ricard-Blum (2009) J. Biol. Chem. 284, 22029-22040], suggesting that endostatin is not able to interact simultaneously with TG-2 and heparan sulfate, or with TG-2 and integrins. Inhibition experiments support the hypothesis that the GTP-binding site of TG-2 is a potential binding site for endostatin. Endostatin and TG-2 are co-localized in the extracellular matrix secreted by endothelial cells under hypoxia, which stimulates angiogenesis. This interaction, occurring in a cellular context, might participate in the concerted regulation of angiogenesis and tumorigenesis by the two proteins.

Indexed as

Cells, CulturedCollagen Type XVIIIEndostatinsEndothelial CellsExtracellular MatrixGTP-Binding ProteinsHumansImmunohistochemistryProtein BindingProtein Glutamine gamma Glutamyltransferase 2Protein Structure, TertiarySurface Plasmon ResonanceTransglutaminasesCollagen Type XVIIIEndostatinsGTP-Binding ProteinsProtein Glutamine gamma Glutamyltransferase 2Transglutaminases

Identifiers

PMID20156196
PMCPMC2876729
OpenAlexW1994531766

What OpenQuestion holds

Textmetadata
LicenceTDM
Read underepoch 390

Registered trials

None linked

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.