Evidence map›Paper›PMID 9355765›Full record

ArticleThe Biochemical journal1997

Analysis of the tetraspanin CD9-integrin alphaIIbbeta3 (GPIIb-IIIa) complex in platelet membranes and transfected cells.

F E Indig, F Diaz-Gonzalez, M H Ginsberg

Open access · bronzeAbstract read
In one paragraph

Article in The Biochemical journal, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
3.8field-weighted citation impact, top 6% 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

21 citing papers in PubMed, 75 citations in OpenAlex.

  1. Article
  2. Article
  3. CD9, a tetraspanin target for cancer therapy?Experimental biology and medicine (Maywood, N.J.) · 2021
    Review
  4. Article
  5. Review
  6. Review
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  8. Review
  9. Enhanced Excitatory Connectivity and Disturbed Sound Processing in the Auditory Brainstem of Fragile X Mice.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2017
    Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Three-dimensional model of the human platelet integrin alpha IIbbeta 3 based on electron cryomicroscopy and x-ray crystallography.Proceedings of the National Academy of Sciences of the United States of America · 2002
    Article
  17. Article
  18. Article
  19. Article
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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

3 authors at 1 institution in 1 country.

F E IndigDepartment of Vascular Biology, The Scripps Research Institute, 10666 N. Torrey Pines Rd, La Jolla, CA 92307, USA.
F Diaz-Gonzalez
M H Ginsberg
Scripps Research Institute · US

Funding

REGULATION OF SECOND MESSENGERS BY BETA3 INTEGRINS IN THE VASCULAR SYSTEMP01HL048728 · NHLBI · SCRIPPS RESEARCH INSTITUTE · PI GINSBERG, MARK HOWARD · 1992 to 2003
$7.4M
Regulation of Integrin Alpha4 BetalR01AR027214 · NIAMS · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI GINSBERG, MARK HOWARD · 1986 to 2010
$3.5M
PLATELETS IN RHEUMATIC DISEASER37AR027214 · NIAMS · SCRIPPS RESEARCH INSTITUTE · PI GINSBERG, MARK HOWARD · 1991 to 2000
$279k
AFFINITY MODULATION OF INTEGRINSF32HL008986 · NHLBI · SCRIPPS RESEARCH INSTITUTE · PI INDIG, FRED E · 1993 to 1996
–
NHLBI NIH HHS HL08986-03NHLBI NIH HHS HL 48728NIAMS NIH HHS AR 27214
6 · The paper itself

Abstract

The platelet integrin, alphaIIbbeta3 (GPIIb-IIIa), and the tetraspanin, CD9, are integral membrane proteins that are abundant in platelet membranes. We have identified several proteins, including CD9, which were co-precipitated by anti-alphaIIbbeta3 antibody from untreated, resting platelets that were solubilized with the poly(oxyethylene) non-ionic detergent, Brij-35. Immunoblot and quantitative immunoprecipitation showed that the association of alphaIIbbeta3 with CD9 is specific and stoichiometric. The interaction between CD9 and alphaIIbbeta3 is probably hydrophobic, as Triton X-100 and hydrophobic detergents of the Brij series completely dissociated the CD9-alphaIIbbeta3 complex. Recombinant CD9 and alphaIIbbeta3 can associate after transfection into Chinese hamster ovary cells, as seen by co-immunoprecipitation and co-localization in the periphery of spreading cells and in the lamellipodia of cells plated on fibrinogen. This co-localization is absent from focal adhesions. Furthermore, anti-CD9-coated latex beads clustered alphaIIbbeta3 with CD9. This work indicates that the tetraspanin, CD9, is associated with beta3 integrins in resting platelets and transfected cells.

Indexed as

AnimalsAntibodies, MonoclonalAntigens, CDBiotinylationBlood PlateletsCHO CellsCricetinaeDetergentsHumansImmunoblottingMembrane GlycoproteinsPlatelet Glycoprotein GPIIb-IIIa ComplexPrecipitin TestsRecombinant ProteinsTetraspanin 29TransfectionAntibodies, MonoclonalAntigens, CDCD9 protein, humanDetergentsMembrane GlycoproteinsPlatelet Glycoprotein GPIIb-IIIa ComplexRecombinant ProteinsTetraspanin 29

Identifiers

PMID9355765
PMCPMC1218793
OpenAlexW1714169008

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.