Evidence map›Paper›PMID 10684262›Full record

ArticleThe Journal of cell biology2000

Tissue transglutaminase is an integrin-binding adhesion coreceptor for fibronectin.

S S Akimov, D Krylov, L F Fleischman, A M Belkin

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 212 papers.

0numbers the graph read from it
0cells of the map it votes in
212citing papers in PubMed
13.0field-weighted citation impact, top 1% 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

212 citing papers in PubMed, 489 citations in OpenAlex.

  1. Article
  2. Review
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  4. Review
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  8. Article
  9. α9β1 integrin & its ligands as new potential biomarkers in FMF.The Indian journal of medical research · 2024
    Article
  10. Review
  11. Shaping Oncogenic Microenvironments: Contribution of Fibronectin.Frontiers in cell and developmental biology · 2024
    Review
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Review
  18. Article
  19. Article
  20. Article

152 more citing papers are in PubMed but not listed here.

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

4 authors at 1 institution in 1 country.

S S AkimovDepartment of Biochemistry, American Red Cross, Rockville, Maryland 20855, USA.
D Krylov
L F Fleischman
A M Belkin
American Red Cross · US

Funding

PHYSICAL CHEMISTRY OF THERAPEUTIC PLASMA PROTEINSR01HL021791 · NHLBI · AMERICAN NATIONAL RED CROSS · PI INGHAM, KENNETH C. · 1985 to 2000
$252k
FUNCTIONAL CHARACTERIZATION OF BETA 1D INTEGRINR29CA077697 · NCI · AMERICAN NATIONAL RED CROSS · PI BELKIN, ALEXEY M · 1997 to 2001
$206k
NCI NIH HHS R29CA77697NHLBI NIH HHS HL21791
6 · The paper itself

Abstract

The protein cross-linking enzyme tissue transglutaminase binds in vitro with high affinity to fibronectin via its 42-kD gelatin-binding domain. Here we report that cell surface transglutaminase mediates adhesion and spreading of cells on the 42-kD fibronectin fragment, which lacks integrin-binding motifs. Overexpression of tissue transglutaminase increases its amount on the cell surface, enhances adhesion and spreading on fibronectin and its 42-kD fragment, enlarges focal adhesions, and amplifies adhesion-dependent phosphorylation of focal adhesion kinase. These effects are specific for tissue transglutaminase and are not shared by its functional homologue, a catalytic subunit of factor XIII. Adhesive function of tissue transglutaminase does not require its cross-linking activity but depends on its stable noncovalent association with integrins. Transglutaminase interacts directly with multiple integrins of beta1 and beta3 subfamilies, but not with beta2 integrins. Complexes of transglutaminase with integrins are formed inside the cell during biosynthesis and accumulate on the surface and in focal adhesions. Together our results demonstrate that tissue transglutaminase mediates the interaction of integrins with fibronectin, thereby acting as an integrin-associated coreceptor to promote cell adhesion and spreading.

Indexed as

Cell AdhesionAnimalsAntigens, CDCell Adhesion MoleculesCell LineCell MembraneCell SizeCross-Linking ReagentsFibronectinsFocal Adhesion Kinase 1Focal Adhesion Protein-Tyrosine KinasesGTP-Binding ProteinsHumansIntegrin beta1Integrin beta3IntegrinsAntigens, CDCell Adhesion MoleculesCross-Linking ReagentsFibronectinsFocal Adhesion Kinase 1Focal Adhesion Protein-Tyrosine KinasesGTP-Binding ProteinsIntegrin beta1Integrin beta3IntegrinsPeptide FragmentsPlatelet Membrane GlycoproteinsProtein Glutamine gamma Glutamyltransferase 2Protein-Tyrosine KinasesPTK2 protein, humanPtk2 protein, ratReceptors, Cell SurfaceTetradecanoylphorbol AcetateTransglutaminases

Identifiers

PMID10684262
PMCPMC2169362
OpenAlexW2036806537

What OpenQuestion holds

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LicenceCC BY-NC-SA
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.