Evidence map›Paper›PMID 9931299›Full record

ArticleThe Biochemical journal1999

Transmembrane 4 superfamily protein CD151 (PETA-3) associates with beta 1 and alpha IIb beta 3 integrins in haemopoietic cell lines and modulates cell-cell adhesion.

S Fitter, P M Sincock, C N Jolliffe, L K Ashman

Open access · greenAbstract read
In one paragraph

Article in The Biochemical journal, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.

0numbers the graph read from it
0cells of the map it votes in
30citing papers in PubMed
3.5field-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

30 citing papers in PubMed, 107 citations in OpenAlex.

  1. CD151 interacts with integrin beta 2 in B cell lymphomas.Cellular and molecular life sciences : CMLS · 2025
    Article
  2. Review
  3. Article
  4. Review
  5. Review
  6. Review
  7. Article
  8. Review
  9. Blood Groups in Infection and Host Susceptibility.Clinical microbiology reviews · 2015
    Review
  10. Tetraspanins in cell migration.Cell adhesion & migration · 2015
    Review
  11. CD151 in cancer progression and metastasis: a complex scenario.Laboratory investigation; a journal of technical methods and pathology · 2014
    Review
  12. Article
  13. Article
  14. Article
  15. Article
  16. Review
  17. Tetraspanins and vascular functions.Cardiovascular research · 2009
    Review
  18. Article
  19. 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

4 authors at 2 institutions in 1 country.

S FitterDivision of Haematology, Hanson Centre for Cancer Research, Institute of Medical and Veterinary Science, Adelaide, SA, Australia.
P M Sincock
C N Jolliffe
L K Ashman
South Australia Pathology · AUUniversity of Adelaide · AU

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

CD151 (PETA-3/SFA-1) is a member of the transmembrane 4 superfamily (TM4SF) of cell-surface proteins and is expressed abundantly both on the cell surface and in intracellular membranes by the haemopoietic cell lines M07e, HEL and K562. In the presence of mild detergent (CHAPS), CD151 co-immunoprecipitated with integrin alpha 4 beta 1, alpha 5 beta 1, alpha 6 beta 1 and alpha IIb beta 3. The association of CD151 with alpha 4 beta 1 and alpha 5 beta 1 seemed to be constitutive, as it was not modified by treatment of M07e cells with cytokines that regulate integrin function by 'inside-out' signalling. CD151 also associated with other tetraspans in an apparently cell-type-specific fashion, as defined by its co-precipitation with CD9, CD63 and CD81 from M07e cells, but not from K562 cells, which express similar levels of these proteins. F(ab')2 fragments of monoclonal antibodies (mAbs) against CD151 caused homotypic adhesion of HEL and K562 cells that was dependent on energy and cytoskeletal integrity and was augmented in the presence of RGDS peptides. The adhesion was not blocked by function-inhibiting mAbs against beta 1 or beta 3 integrins, suggesting that cell-cell adhesion was not mediated by the binding of integrin to a cell-associated ligand. Furthermore, mAb CD151 did not affect adhesion of the cells to fibronectin, laminin, collagen or fibrinogen, which are ligands for alpha 4 beta 1, alpha 5 beta 1, alpha 6 beta 1 and alpha IIb beta 3 integrins. Taken together, these results indicate that the ligation of CD151 does not induce the up-regulation of integrin avidity, but might act as a component of integrin signalling complexes.

Indexed as

Antibodies, MonoclonalAntigens, CDBinding SitesCell AdhesionCell MembraneChemical PrecipitationCytoplasmDetergentsExtracellular MatrixHematopoietic Stem CellsHumansIntegrin beta1K562 CellsMacromolecular SubstancesMembrane ProteinsPlatelet Glycoprotein GPIIb-IIIa ComplexAntibodies, MonoclonalAntigens, CDCD151 protein, humanDetergentsIntegrin beta1Macromolecular SubstancesMembrane ProteinsPlatelet Glycoprotein GPIIb-IIIa ComplexTetraspanin 24

Identifiers

PMID9931299
PMCPMC1220025
OpenAlexW2128083140

What OpenQuestion holds

Textmetadata
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.