Evidence map›Paper›PMID 26209658›Full record

ArticleBlood2015

Autophagy is induced upon platelet activation and is essential for hemostasis and thrombosis.

Madhu M Ouseph, Yunjie Huang, Meenakshi Banerjee, Smita Joshi, Laura MacDonald, Yu Zhong, Huijuan Liu, Xianting Li, Binggang Xiang, Guoying Zhang and 7 more

Erratum issuedOpen access · bronzeAbstract read
In one paragraph

Article in Blood, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 92 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
92citing papers in PubMed, 1 pooled it
8.1field-weighted citation impact, top 2% 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

92 citing papers in PubMed, 1 synthesis or guideline pooled it, 145 citations in OpenAlex.

  1. Guideline
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  14. DUT (p.Y116C)-Mutation-Induced Thrombocytopenia in Rabbits.International journal of molecular sciences · 2025
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32 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

  • Erratum issued
    Komatsu, Massaki [corrected to Komatsu, Masaaki]
5 · Who and what money

Authors and funding

17 authors at 5 institutions in 2 countries.

Madhu M OusephDepartment of Molecular and Cellular Biochemistry, University of Kentucky, Lexington, KY;
Yunjie HuangDepartment of Molecular and Cellular Biochemistry, University of Kentucky, Lexington, KY;
Meenakshi BanerjeeDepartment of Molecular and Cellular Biochemistry, University of Kentucky, Lexington, KY;
Smita JoshiDepartment of Molecular and Cellular Biochemistry, University of Kentucky, Lexington, KY;
Laura MacDonaldDepartment of Physiology and Biophysics, University of Arkansas for Medical Sciences, Little Rock, AR;
Yu ZhongDepartment of Molecular and Cellular Biochemistry, University of Kentucky, Lexington, KY;
Huijuan LiuDepartment of Molecular and Cellular Biochemistry, University of Kentucky, Lexington, KY;
Xianting LiDepartment of Neurology and Department of Neuroscience, Friedman Brain Institute, Icahn School of Medicine at Mount Sinai, New York, NY;
Binggang XiangDivision of Cardiovascular Medicine, Department of Internal Medicine, University of Kentucky, Lexington, KY;
Guoying ZhangDivision of Cardiovascular Medicine, Department of Internal Medicine, University of Kentucky, Lexington, KY;
Masaaki Komatsu
Massaki KomatsuProtein Metabolism Project, Tokyo Metropolitan Institute of Medical Science, Tokyo, Japan; and Department of Biochemistry, School of Medicine, Niigata University, Niigata, Japan.
Zhenyu YueDepartment of Neurology and Department of Neuroscience, Friedman Brain Institute, Icahn School of Medicine at Mount Sinai, New York, NY;
Zhenyu LiDivision of Cardiovascular Medicine, Department of Internal Medicine, University of Kentucky, Lexington, KY;
Brian StorrieDepartment of Physiology and Biophysics, University of Arkansas for Medical Sciences, Little Rock, AR;
Sidney W WhiteheartDepartment of Molecular and Cellular Biochemistry, University of Kentucky, Lexington, KY;
Qing Jun WangDepartment of Molecular and Cellular Biochemistry, University of Kentucky, Lexington, KY;
University of Kentucky · USUniversity of Arkansas for Medical Sciences · USAllen Institute for Brain Science · USIcahn School of Medicine at Mount Sinai · USTokyo Metropolitan Institute of Medical Science · JP

Funding

Neuronal Autophagy: a Cell-Autonomous Protection MechanismR01NS060123 · NINDS · ICAHN SCHOOL OF MEDICINE AT MOUNT SINAI · PI Zhenyu Yue · 2008 to 2026
$9.2M
MOLECULAR MECHANISMS OF PLATELET EXOCYTOSISR01HL056652 · NHLBI · UNIVERSITY OF KENTUCKY · PI WHITEHEART, SIDNEY WALDO · 1996 to 2019
$5.2M
Center for Biomedical Research Excellence in the Molecular Basis of Human DiseaseP20GM103486 · NIGMS · UNIVERSITY OF KENTUCKY · PI LOUIS HERSH, LOUIS HERSH LOUIS HERSH · 2012 to 2013
$4.2M
Structure/Function Determinants of Platelet Granule SecretionR01HL119393 · NHLBI · UNIV OF ARKANSAS FOR MED SCIS · PI STORRIE, BRIAN · 2013 to 2016
$1.4M
The Platelet Secretory MachineryR01HL091893 · NHLBI · UNIVERSITY OF KENTUCKY · PI WHITEHEART, SIDNEY WALDO · 2008 to 2011
$1.2M
NHLBI NIH HHS HL091893NHLBI NIH HHS HL56652NHLBI NIH HHS R01 HL056652NHLBI NIH HHS R01 HL091893NHLBI NIH HHS R01 HL119393NHLBI NIH HHS R01HL119393NIGMS NIH HHS P20 GM103486NIGMS NIH HHS P20GM103486NINDS NIH HHS R01 NS060123NINDS NIH HHS R01NS060123
6 · The paper itself

Abstract

Autophagy is important for maintaining cellular homeostasis, and thus its deficiency is implicated in a broad spectrum of human diseases. Its role in platelet function has only recently been examined. Our biochemical and imaging studies demonstrate that the core autophagy machinery exists in platelets, and that autophagy is constitutively active in resting platelets. Moreover, autophagy is induced upon platelet activation, as indicated by agonist-induced loss of the autophagy marker LC3II. Additional experiments, using inhibitors of platelet activation, proteases, and lysosomal acidification, as well as platelets from knockout mouse strains, show that agonist-induced LC3II loss is a consequence of platelet signaling cascades and requires proteases, acidic compartments, and membrane fusion. To assess the physiological role of platelet autophagy, we generated a mouse strain with a megakaryocyte- and platelet-specific deletion of Atg7, an enzyme required for LC3II production. Ex vivo analysis of platelets from these mice shows modest defects in aggregation and granule cargo packaging. Although these mice have normal platelet numbers and size distributions, they exhibit a robust bleeding diathesis in the tail-bleeding assay and a prolonged occlusion time in the FeCl3-induced carotid injury model. Our results demonstrate that autophagy occurs in platelets and is important for hemostasis and thrombosis.

Indexed as

AnimalsAutophagyBlood PlateletsBlotting, WesternCells, CulturedHemostasisHumansMiceMice, Mutant StrainsPlatelet ActivationThrombosis

Identifiers

PMID26209658
PMCPMC4559933
OpenAlexW1738348680

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.