Evidence map›Paper›PMID 24742684›Full record

ArticleThe Journal of biological chemistry2014

Cell surface translocation of annexin A2 facilitates glutamate-induced extracellular proteolysis.

Mallika Valapala, Sayantan Maji, Julian Borejdo, Jamboor K Vishwanatha

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
1.3field-weighted citation impact, top 21% 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

17 citing papers in PubMed, 30 citations in OpenAlex.

  1. Article
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  9. Review
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  12. Unconventional secretion of annexins and galectins.Seminars in cell & developmental biology · 2018
    Review
  13. Article
  14. 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

4 authors at 2 institutions in 2 countries.

Mallika ValapalaFrom the Department of Molecular and Medical Genetics and.
Sayantan MajiFrom the Department of Molecular and Medical Genetics and.
Julian BorejdoDepartment of Cell Biology and Immunology University of North Texas Health Science Center, Fort Worth, Texas 76107.
Jamboor K VishwanathaFrom the Department of Molecular and Medical Genetics and jamboor.vishwanatha@unthsc.edu.
Laboratory of Molecular Genetics · PLUniversity of North Texas · US

Funding

Triple Negative Breast Cancer: Novel Biomarkers and Therapeutic StrategiesP20MD006882 · NIMHD · UNIVERSITY OF NORTH TEXAS HLTH SCI CTR · PI VISHWANATHA, JAMBOOR K. · 2012 to 2016
$5.8M
NIMHD NIH HHS 1P20 MD006882NIMHD NIH HHS P20 MD006882
6 · The paper itself

Abstract

Glutamate-induced elevation in intracellular Ca(2+) has been implicated in excitotoxic cell death. Neurons respond to increased glutamate levels by activating an extracellular proteolytic cascade involving the components of the plasmin-plasminogen system. AnxA2 is a Ca(2+)-dependent phospholipid binding protein and serves as an extracellular proteolytic center by recruiting the tissue plasminogen activator and plasminogen and mediating the localized generation of plasmin. Ratiometric Ca(2+) imaging and time-lapse confocal microscopy demonstrated glutamate-induced Ca(2+) influx. We showed that glutamate translocated both endogenous and AnxA2-GFP to the cell surface in a process dependent on the activity of the NMDA receptor. Glutamate-induced translocation of AnxA2 is dependent on the phosphorylation of tyrosine 23 at the N terminus, and mutation of tyrosine 23 to a non-phosphomimetic variant inhibits the translocation process. The cell surface-translocated AnxA2 forms an active plasmin-generating complex, and this activity can be neutralized by a hexapeptide directed against the N terminus. These results suggest an involvement of AnxA2 in potentiating glutamate-induced cell death processes.

Indexed as

AnimalsAnnexin A2CalciumCell Line, TransformedExtracellular SpaceFibrinolysinGlutamic AcidGreen Fluorescent ProteinsMicePhosphorylationProtein TransportProteolysisTyrosineAnnexin A2CalciumFibrinolysinGlutamic AcidGreen Fluorescent ProteinsTyrosineAnnexinCalciumCell Surface ProteinGlutamatePlasminProteolysis

Identifiers

PMID24742684
PMCPMC4047365
OpenAlexW2041849046

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.