Evidence map›Paper›PMID 16352809›Full record

ArticleBlood2006

Arf6 plays an early role in platelet activation by collagen and convulxin.

Wangsun Choi, Zubair A Karim, Sidney W Whiteheart

Open access · greenAbstract read
In one paragraph

Article in Blood, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.

0numbers the graph read from it
0cells of the map it votes in
34citing papers in PubMed
1.2field-weighted citation impact, top 23% 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

34 citing papers in PubMed, 52 citations in OpenAlex.

  1. Trial
  2. Article
  3. A Review of Extracellular Vesicles in COVID-19 Diagnosis, Treatment, and Prevention.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2023
    Review
  4. Review
  5. Review
  6. Article
  7. Article
  8. Review
  9. Article
  10. Article
  11. Article
  12. Arhgef1 Plays a Vital Role in Platelet Function and Thrombogenesis.Journal of the American Heart Association · 2019
    Article
  13. Article
  14. Review
  15. Review
  16. Article
  17. Article
  18. Review
  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

3 authors at 1 institution in 1 country.

Wangsun ChoiDepartment of Molecular and Cellular Biochemistry, University of Kentucky College of Medicine, Lexington, KY 40536-0509, USA.
Zubair A Karim
Sidney W Whiteheart
University of Kentucky · US

Funding

UNDERSTANDING THE MOLECULAR BASIS OF EPIGENETIC TRANSCRIPTIONAL SILENCINGP20RR020171 · NCRR · UNIVERSITY OF KENTUCKY · PI LOUIS HERSH, LOUIS HERSH LOUIS HERSH · 2004 to 2011
$16.5M
MOLECULAR MECHANISMS OF PLATELET EXOCYTOSISR01HL056652 · NHLBI · UNIVERSITY OF KENTUCKY · PI WHITEHEART, SIDNEY WALDO · 1996 to 2019
$5.2M
NCRR NIH HHS P20 RR20171NHLBI NIH HHS HL-56652
6 · The paper itself

Abstract

Small GTPases play critical roles in hemostasis, though the roster of such molecules in platelets is not complete. In this study, we report the presence of Ras-related GTPases of the ADP-ribosylation factor (Arf) family. Platelets contain Arf1 or 3 and Arf6, with the latter being predominantly membrane associated. Using effector domain pull-down assays, we show, counter to other GTPases, that Arf6-GTP is present in resting platelets and decreases rapidly upon activation with collagen or convulxin. This decrease does not completely rely on secondary agonists (ADP and thromboxane A2) or require integrin signaling. The decrease in free Arf6-GTP temporally precedes activation of Rho family GTPases (RhoA, Cdc42, and Rac1). Using a membrane-permeant, myristoylated peptide, which mimics the N-terminus of Arf6, we show that the Arf6-GTP decrease is essential for collagen- and convulxin-induced aggregation, platelet adherence, and spreading on collagen-coated glass. Treatment with this peptide also affects the activation of Rho family GTPases, but has little effect on RalA and Rap1 or on agonist-induced calcium mobilization. These data show that Arf6 is a key element in activation through GPVI, and is required for activation of the Rho family GTPases and the subsequent cytoskeletal rearrangements needed for full platelet function.

Indexed as

CollagenAdenosine DiphosphateADP-Ribosylation Factor 1ADP-Ribosylation Factor 6ADP-Ribosylation FactorsCalcium Signalingcdc42 GTP-Binding ProteinCell MembraneCrotalid VenomsCytoskeletonEnzyme ActivationHumansLectins, C-TypePlatelet AdhesivenessPlatelet AggregationPlatelet Membrane GlycoproteinsAdenosine DiphosphateADP-Ribosylation Factor 1ADP-Ribosylation Factor 6ADP-Ribosylation FactorsARF3 protein, humanARF6 protein, humancdc42 GTP-Binding ProteinCollagenconvulxinCrotalid VenomsLectins, C-TypePlatelet Membrane Glycoproteinsplatelet membrane glycoprotein VIrap1 GTP-Binding ProteinsrhoA GTP-Binding ProteinThromboxane A2

Identifiers

PMID16352809
PMCPMC1895749
OpenAlexW1971178507

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.