Evidence map›Paper›PMID 19398782›Full record

ArticleThe Journal of biological chemistry2009

Heparan sulfate proteoglycans are receptors for the cell-surface trafficking and biological activity of transglutaminase-2.

Alessandra Scarpellini, Renée Germack, Hugues Lortat-Jacob, Takashi Muramatsu, Ellen Billett, Timothy Johnson, Elisabetta A M Verderio

Registry-linked trialOpen access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. It is linked to trial NCT03487861 (Development of a Diagnostic Kit for Urinary Transglutaminase 2 as a Biomarker for Kidney Allograft Fibrosis), which is not on this map. Cited by 56 papers.

0numbers the graph read from it
0cells of the map it votes in
56citing papers in PubMed
7.2field-weighted citation impact, top 3% 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.

NCT03487861 unknown statusnot on this mapstarted 2017, after this paper: background citation

Development of a Diagnostic Kit for Urinary Transglutaminase 2 as a Biomarker for Kidney Allograft Fibrosis

TypeobservationalSponsorAsan Medical CenterRan2017 to 2020Enrolled1,000ConditionsKidney Allograft Fibrosis, Kidney Transplant Failure and RejectionArmsobservational(urinary biomarker for kidney allograft fibrosis)
3 · Its place in the literature

Who cites it

56 citing papers in PubMed, 95 citations in OpenAlex.

  1. Review
  2. Review
  3. Article
  4. Article
  5. Article
  6. Review
  7. Article
  8. Review
  9. Review
  10. The matrix in cancer.Nature reviews. Cancer · 2021
    Review
  11. Article
  12. Article
  13. Spotlight on the Transglutaminase 2-Heparan Sulfate Interaction.Medical sciences (Basel, Switzerland) · 2019
    Review
  14. Transglutaminases in Monocytes and Macrophages.Medical sciences (Basel, Switzerland) · 2018
    Review
  15. Review
  16. Review
  17. Review
  18. Article
  19. Article
  20. Review
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

7 authors at 4 institutions in 3 countries.

Alessandra ScarpelliniSchool of Science and Technology, Nottingham Trent University, Clifton Lane, Nottingham NG11 8NS, United Kingdom.
Renée Germack
Hugues Lortat-Jacob
Takashi Muramatsu
Ellen Billett
Timothy Johnson
Elisabetta A M Verderio
Nottingham Trent University · GBAichi Gakuin University · JPUniversité Grenoble Alpes · FRUniversity of Sheffield · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Transglutaminase type 2 (TG2) is both a protein cross-linking enzyme and a cell adhesion molecule with an elusive unconventional secretion pathway. In normal conditions, TG2-mediated modification of the extracellular matrix modulates cell motility, proliferation and tissue repair, but under continuous cell insult, higher expression and elevated extracellular trafficking of TG2 contribute to the pathogenesis of tissue scarring. In search of TG2 ligands that could contribute to its regulation, we characterized the affinity of TG2 for heparan sulfate (HS) and heparin, an analogue of the chains of HS proteoglycans (HSPGs). By using heparin/HS solid-binding assays and surface plasmon resonance we showed that purified TG2 has high affinity for heparin/HS, comparable to that for fibronectin, and that cell-surface TG2 interacts with heparin/HS. We demonstrated that cell-surface TG2 directly associates with the HS chains of syndecan-4 without the mediation of fibronectin, which has affinity for both syndecan-4 and TG2. Functional inhibition of the cell-surface HS chains of wild-type and syndecan-4-null fibroblasts revealed that the extracellular cross-linking activity of TG2 depends on the HS of HSPG and that syndecan-4 plays a major but not exclusive role. We found that heparin binding did not alter TG2 activity per se. Conversely, fibroblasts deprived of syndecan-4 were unable to effectively externalize TG2, resulting in its cytosolic accumulation. We propose that the membrane trafficking of TG2, and hence its extracellular activity, is linked to TG2 binding to cell-surface HSPG.

Indexed as

AnimalsDermisExtracellular SpaceFibroblastsGTP-Binding ProteinsHeparan SulfateHeparan Sulfate ProteoglycansHeparinMiceMice, Inbred C57BLMice, Mutant StrainsProtein Glutamine gamma Glutamyltransferase 2Protein TransportReceptors, Cell SurfaceSyndecan-4TransfectionGTP-Binding ProteinsHeparan SulfateHeparan Sulfate ProteoglycansHeparinProtein Glutamine gamma Glutamyltransferase 2Receptors, Cell SurfaceSdc4 protein, mouseSyndecan-4Transglutaminases

Identifiers

PMID19398782
PMCPMC2709370
OpenAlexW1996112172

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

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.