Evidence map›Paper›PMID 18827060›Full record

ReviewLupus2008

Annexin A2: biology and relevance to the antiphospholipid syndrome.

E Cockrell, R G Espinola, K R McCrae

Abstract readReview
In one paragraph

Review in Lupus, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed
2.2field-weighted citation impact, top 13% 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

28 citing papers in PubMed, 48 citations in OpenAlex.

  1. Review
  2. Review
  3. Review
  4. Review
  5. Review
  6. Annexin A2 in Fibrinolysis, Inflammation and Fibrosis.International journal of molecular sciences · 2021
    Review
  7. Article
  8. Review
  9. Review
  10. Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. The Biology of Annexin A2: From Vascular Fibrinolysis to Innate Immunity.Transactions of the American Clinical and Climatological Association · 2015
    Review
  16. Article
  17. Article
  18. Annexin A2 system in human biology: cell surface and beyond.Seminars in thrombosis and hemostasis · 2013
    Review
  19. Annexin A2 heterotetramer: structure and function.International journal of molecular sciences · 2013
    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

3 authors at 1 institution in 1 country.

E CockrellDivision of Pediatric, Case Western Reserve University School of Medicine, Cleveland, Ohio 44106, USA.
R G Espinola
K R McCrae
Case Western Reserve University · US

Funding

ROLE OF MICROPARTICLES IN THE ANTI-PHOSPHOLIPID SYNDROMEP50HL081011 · NHLBI · CLEVELAND CLINIC LERNER COM-CWRU · PI MCINTYRE, THOMAS · 2006 to 2010
$12.9M
NHLBI NIH HHS P50 HL081011
6 · The paper itself

Abstract

Antiphospholipid antibodies (aPL), the majority of which are directed against beta(2)-glycoprotein I (beta(2)GPI), are associated with an increased incidence of venous and arterial thrombosis. The pathogenesis of antiphospholipid/anti-beta(2)GPI-associated thrombosis has not been defined, and is likely multifactorial. However, accumulating evidence suggests an important role for endothelial cell activation with the acquisition of a procoagulant phenotype by the activated endothelial cell. Previous work demonstrated that endothelial activation by antiphospholipid/anti-beta(2)GPI antibodies is beta(2)GPI-dependent. We extended these observations by defining annexin A2 as an endothelial beta(2)GPI binding site. We also observed that annexin A2 plays a critical role in endothelial cell activation induced by anti-beta(2)GPI antibodies, and others have described direct endothelial activation by anti-annexin A2 antibodies in patients with aPL . Similar findings have been reported using human monocytes, which also express annexin A2. Because annexin A2 is not a transmembrane protein, how binding of beta(2)GPI/anti-beta(2)GPI antibodies, or anti-annexin A2 antibodies, to endothelial annexin A2 causes cellular activation is unknown. Recent studies, however, suggest an important role for the Toll-like receptor family, particularly TLR4. In this article, we review the role of these interactions in the activation of endothelial cells by aPL . The influence of these antibodies on the ability of annexin A2 to enhance t-PA-mediated plasminogen activation is also discussed.

Indexed as

Binding Sites, AntibodyAnnexin A2Antibodies, AntiphospholipidAntiphospholipid Syndromebeta 2-Glycoprotein IEndothelial CellsFibrinolysisHumansPhospholipidsThrombosisAnnexin A2Antibodies, Antiphospholipidbeta 2-Glycoprotein IPhospholipids

Identifiers

PMID18827060
PMCPMC3417102
OpenAlexW2038610371

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.