Evidence map›Paper›PMID 20093722›Full record

ReviewGeneral physiology and biophysics2009

The endothelial cell annexin A2 system and vascular fibrinolysis.

MaryAnn Dassah, Arun B Deora, Kaili He, Katherine A Hajjar

Abstract readReview
In one paragraph

Review in General physiology and biophysics, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed
1.9field-weighted citation impact, top 15% 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

29 citing papers in PubMed, 45 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Review
  5. Article
  6. Article
  7. Review
  8. Annexin A2 and Kidney Diseases.Frontiers in cell and developmental biology · 2022
    Review
  9. Annexin A2 in Fibrinolysis, Inflammation and Fibrosis.International journal of molecular sciences · 2021
    Review
  10. Article
  11. Review
  12. Review
  13. Article
  14. Article
  15. Article
  16. The Biology of Annexin A2: From Vascular Fibrinolysis to Innate Immunity.Transactions of the American Clinical and Climatological Association · 2015
    Review
  17. Dynamic reciprocity: the role of annexin A2 in tissue integrity.Journal of cell communication and signaling · 2014
    Article
  18. Article
  19. New insights into the role of Plg-RKT in macrophage recruitment.International review of cell and molecular biology · 2014
    Review
  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 1 institution in 1 country.

MaryAnn DassahDepartment of Cell and Developmental Biology, Weill Cornell Medical College, New York, NY 10065, USA.
Arun B Deora
Kaili He
Katherine A Hajjar
Cornell University · US

Funding

Vascular signaling via scavenger receptorsP01HL046403 · NHLBI · WEILL MEDICAL COLL OF CORNELL UNIV · PI HAJJAR, KATHERINE AMBERSON · 1991 to 2011
$26.7M
Regulation of Endothelial Cell Function in AngiogenesisP01HL067839 · NHLBI · WEILL MEDICAL COLLEGE OF CORNELL UNIV · PI RAFII, SHAHIN · 2001 to 2005
$6.7M
NEW THROMBOREGULATORY PROTEIN, ANNEXIN IIR01HL042493 · NHLBI · WEILL MEDICAL COLL OF CORNELL UNIV · PI HAJJAR, KATHERINE AMBERSON · 1989 to 2016
$4.9M
Annexin 2 in AngiogenesisR01HL090895 · NHLBI · WEILL MEDICAL COLL OF CORNELL UNIV · PI HAJJAR, KATHERINE AMBERSON · 2008 to 2011
$1.7M
NHLBI NIH HHS HL 42493NHLBI NIH HHS HL 46403NHLBI NIH HHS HL 67839NHLBI NIH HHS P01 HL046403NHLBI NIH HHS P01 HL067839NHLBI NIH HHS R01 HL042493NHLBI NIH HHS R01 HL090895
6 · The paper itself

Abstract

Vascular endothelial cell surface expression of annexin A2 and its binding partner p11 is a key element in maintaining fibrinolytic balance on blood vessel surfaces. In the recent decade, investigators have made significant progress toward understanding the mechanisms that regulate heterotetrameric (A2*p11)(2) receptor translocation from the cytoplasm to the outer cell surface. Accumulating evidence now shows that heterotetrameric (A2*p11)(2) cell surface expression is a dynamic process that modulates plasmin activation during periods of vascular stress or injury, and is independent of the classical endoplasmic reticulum-Golgi pathway. Translocation of heterotetrameric (A2*p11)(2) is facilitated both by src-kinase mediated phosphorylation of A2 at tyrosine 23, and by expression of and partnering with p11. In the absence of A2 both in vivo and in vitro, p11 is expressed at very low levels in endothelial cells, because unpartnered p11 is polyubiquitinated and rapidly degraded through a proteasome-dependent mechanism. A2 directly binds and stabilizes intracellular p11 by masking an autonomous polyubiquitination signal on p11. This modulatory role of A2 binding prevents accumulation of unpartnered p11 within the endothelial cell, and ultimately suggests that the regulation of heterotetrameric (A2*p11)(2) receptor surface expression is precisely attuned to the intracellular level of p11.

Indexed as

FibrinolysisAnimalsAnnexin A2Binding SitesEndothelial CellsFibrinolysinHomeostasisHumansModels, BiologicalPhosphorylationPlasminogenProtein BindingProtein Structure, TertiaryReceptors, Urokinase Plasminogen ActivatorUbiquitinAnnexin A2FibrinolysinPlasminogenReceptors, Urokinase Plasminogen ActivatorUbiquitin

Identifiers

PMID20093722
PMCPMC3014645
OpenAlexW2106915210

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.