Evidence map›Paper›PMID 32022992›Full record

ArticleJournal of thrombosis and haemostasis : JTH2020

Pharmacologic dissection of the overlapping impact of heat shock protein family members on platelet function.

Joseph W Jackson, Genesis M Rivera-Marquez, Kristin Beebe, Andy D Tran, Jane B Trepel, Jason E Gestwicki, Brian S J Blagg, Shuichi Ohkubo, Leonard M Neckers

Open access · bronzeAbstract read
In one paragraph

Article in Journal of thrombosis and haemostasis : JTH, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing papers in PubMed
0.7field-weighted citation impact, top 33% 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

7 citing papers in PubMed, 11 citations in OpenAlex.

  1. The Release of Platelet DAMPs is Regulated by NINJ1-Mediated Plasma Membrane Rupture.Indian journal of hematology & blood transfusion : an official journal of Indian Society of Hematology and Blood Transfusion · 2025
    Article
  2. Article
  3. Review
  4. Review
  5. Article
  6. Genetic Deletion of HLJ1 Does Not Affect Blood Coagulation in Mice.International journal of molecular sciences · 2022
    Article
  7. 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

9 authors at 4 institutions in 2 countries.

Joseph W JacksonUrologic Oncology Branch, Center for Cancer Research, National Cancer Institute, National Institutes of Health, Bethesda, MD, USA.
Genesis M Rivera-MarquezUrologic Oncology Branch, Center for Cancer Research, National Cancer Institute, National Institutes of Health, Bethesda, MD, USA.
Kristin BeebeUrologic Oncology Branch, Center for Cancer Research, National Cancer Institute, National Institutes of Health, Bethesda, MD, USA.
Andy D TranCenter for Cancer Research, Confocal Microscopy Core Facility, National Cancer Institute, National Institutes of Health, Bethesda, MD, USA.
Jane B TrepelDevelopmental Therapeutics Branch, Center for Cancer Research, National Cancer Institute, National Institutes of Health, Bethesda, MD, USA.
Jason E GestwickiDepartment of Pharmaceutical Chemistry and the Institute for Neurodegenerative Disease, University of California at San Francisco, San Francisco, CA, USA.
Brian S J BlaggDepartment of Chemistry and Biochemistry, The University of Notre Dame, Notre Dame, IN, USA.
Shuichi OhkuboTsukuba Research Center, Taiho Pharmaceutical Co., Ltd., Tsukuba, Japan.ORCID 0000-0001-9554-4534
Leonard M NeckersUrologic Oncology Branch, Center for Cancer Research, National Cancer Institute, National Institutes of Health, Bethesda, MD, USA.
National Institutes of Health · USTaiho Pharmaceutical (Japan) · JPUniversity of California, San Francisco · USUniversity of Notre Dame · US

Funding

CCR Microscopy CoreZICBC010858 · NCI · DIVISION OF BASIC SCIENCES - NCI · PI KRUHLAK, MICHAEL · 2009 to 2025
$14.8M
Signal Transduction Events and the Regulation of Cell GrowthZICSC006743 · NCI · DIVISION OF CLINICAL SCIENCES - NCI · PI TREPEL, JANE B · 2009 to 2023
$13.8M
Role of HSP90 Family Chaperone Proteins in Cellular Signal TransductionZIASC010074 · NCI · DIVISION OF CLINICAL SCIENCES - NCI · PI NECKERS, LEONARD · 2009 to 2025
$13.3M
Molecular Chaperones and Small MoleculesR01NS059690 · NINDS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI Jason E Gestwicki · 2008 to 2026
$7.9M
Intramural NIH HHS ZIA SC010074NINDS NIH HHS R01 NS059690
6 · The paper itself

Abstract

backgroundPlatelets play a pivotal role in hemostasis, wound healing, and inflammation, and are thus implicated in a variety of diseases, including cancer. Platelet function is associated with release of granule content, cellular shape change, and upregulation of receptors that promote establishment of a thrombus and maintenance of hemostasis.

objectivesThe role of heat shock proteins (Hsps) in modulating platelet function has been studied for a number of years, but comparative roles of individual Hsps have not been thoroughly examined.

methodsWe utilized a panel of specific inhibitors of Hsp40, Hsp70, Hsp90, and Grp94 (the endoplasmic reticulum homolog of Hsp90) to assess their impact on several aspects of platelet function.

resultsInhibition of each of the aforementioned Hsps reduced alpha granule release. In contrast, there was some selectivity in impacts on dense granule release. Thromboxane synthesis was impaired after exposure to inhibitors of Hsp40, Hsp90, and Grp94, but not after inhibition of Hsp70. Both expression of active glycoprotein IIb/IIIa (GPIIb/IIIa) and fibrinogen-induced platelet shape change were diminished by our inhibitors. In contrast, aggregation was selectively abrogated after inhibition of Hsp40 or Hsp90. Lastly, activated platelet-cancer cell interactions were reduced by inhibition of both Hsp70 and Grp94.

conclusionsThese data suggest the importance of Hsp networks in regulating platelet activity.

Indexed as

Heat-Shock ProteinsPlatelet Glycoprotein GPIIb-IIIa ComplexBlood PlateletsHemostasisHumansPlatelet AggregationPlatelet Aggregation InhibitorsHeat-Shock ProteinsPlatelet Aggregation InhibitorsPlatelet Glycoprotein GPIIb-IIIa Complexantiplatelet agentscancerheat shock proteinshemostasisplatelets

Identifiers

PMID32022992
PMCPMC7497839
OpenAlexW3005277510

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.