Evidence map›Paper›PMID 26378094›Full record

ArticleJournal of lipid research2015

Modification of platelet proteins by malondialdehyde: prevention by dicarbonyl scavengers.

Irene Zagol-Ikapite, Iberia R Sosa, Denise Oram, Audra Judd, Kalyani Amarnath, Venkataraman Amarnath, Donald Stec, John A Oates, Olivier Boutaud

Open access · hybridAbstract read
In one paragraph

Article in Journal of lipid research, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
1.9field-weighted citation impact, top 14% 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

11 citing papers in PubMed, 27 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. The Role and Regulation of Thromboxane AMolecules (Basel, Switzerland) · 2022
    Review
  5. Article
  6. Review
  7. Article
  8. Review
  9. Isolevuglandins and cardiovascular disease.Prostaglandins & other lipid mediators · 2018
    Review
  10. Article
  11. Review
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

9 authors at 1 institution in 1 country.

Irene Zagol-IkapiteDepartment of Medicine, Vanderbilt University, Nashville, TN.
Iberia R SosaDepartment of Medicine, Vanderbilt University, Nashville, TN.
Denise OramDepartment of Medicine, Vanderbilt University, Nashville, TN.
Audra JuddDepartment of Medicine, Vanderbilt University, Nashville, TN.
Kalyani AmarnathDepartment of Pharmacology, Vanderbilt University, Nashville, TN.
Venkataraman AmarnathDepartment of Pathology, Microbiology and Immunology, Vanderbilt University, Nashville, TN.
Donald StecDepartment of Chemistry, Vanderbilt University, Nashville, TN.
John A OatesDepartment of Medicine, Vanderbilt University, Nashville, TN Department of Pharmacology, Vanderbilt University, Nashville, TN.
Olivier BoutaudDepartment of Pharmacology, Vanderbilt University, Nashville, TN.
Vanderbilt University · US

Funding

Non-coding RNA & Bioinformatics CoreP01HL116263 · NHLBI · VANDERBILT UNIVERSITY MEDICAL CENTER · PI DAVIES, SEAN STEPHEN · 2014 to 2025
$24.7M
THE PHARMACOLOGY OF ASPIRINP50HL081009 · NHLBI · VANDERBILT UNIVERSITY · PI LIEBLER, DANIEL · 2006 to 2010
$16.3M
CLINICAL PHARMACOLOGY TRAINING PROGRAMT32GM007569 · NIGMS · VANDERBILT UNIVERSITY MEDICAL CENTER · PI Bjorn C Knollmann · 1985 to 2026
$12.4M
Lipid Modification of Proteins by the PGH SynthasesR01GM087603 · NIGMS · VANDERBILT UNIVERSITY · PI OATES, JOHN ALEXANDER · 2009 to 2010
$683k
NHLBI NIH HHS P01 HL116263NHLBI NIH HHS P50 HL081009NHLBI NIH HHS P50HL81009NIGMS NIH HHS R01 GM087603NIGMS NIH HHS R01GM087603NIGMS NIH HHS T32 GM007569NIGMS NIH HHS T32 GM007569-36
6 · The paper itself

Abstract

The thromboxane synthase converts prostaglandin H(2) to thromboxane A(2) and malondialdehyde (MDA) in approximately equimolar amounts. A reactive dicarbonyl, MDA forms covalent adducts of amino groups, including the ε-amine of lysine, but the importance of this reaction in platelets was unknown. Utilizing a novel LC/MS/MS method for analysis of one of the MDA adducts, the dilysyl-MDA cross-link, we demonstrated that dilysyl-MDA cross-links in human platelets are formed following platelet activation via the cyclooxygenase (COX)-1/thromboxane synthase pathway. Salicylamine and analogs of salicylamine were shown to react with MDA preferentially, thereby preventing formation of lysine adducts. Dilysyl-MDA cross-links were measured in two diseases known to be associated with increased platelet activation. Levels of platelet dilysyl-MDA cross-links were increased by 2-fold in metabolic syndrome relative to healthy subjects, and by 1.9-fold in sickle cell disease (SCD). In patients with SCD, the reduction of platelet dilysyl-MDA cross-links following administration of nonsteroidal anti-inflammatory drug provided evidence that MDA modifications of platelet proteins in this disease are derived from the COX pathway. In summary, MDA adducts of platelet proteins that cross-link lysines are formed on platelet activation and are increased in diseases associated with platelet activation. These protein modifications can be prevented by salicylamine-related scavengers.

Indexed as

AdultAgedAminosalicylic AcidsAnemia, Sickle CellBlood PlateletsBlood ProteinsDrug Evaluation, PreclinicalHumansMalondialdehydeMetabolic SyndromeMiddle AgedPlatelet ActivationAminosalicylic AcidsBlood ProteinsMalondialdehydecross-linkcyclooxygenasemass spectrometrymetabolic syndromenonsteroidal anti-inflammatory drugsalicylaminesickle cell diseasethromboxane synthase

Identifiers

PMID26378094
PMCPMC4617406
OpenAlexW2221321296

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.