Evidence map›Paper›PMID 28072855›Full record

ArticlePloS one2017

SDF-1α/CXCR4 Signaling in Lipid Rafts Induces Platelet Aggregation via PI3 Kinase-Dependent Akt Phosphorylation.

Hiroko Ohtsuka, Tomohiro Iguchi, Moyuru Hayashi, Mizuho Kaneda, Kazuko Iida, Motoyuki Shimonaka, Takahiko Hara, Morio Arai, Yuichi Koike, Naomasa Yamamoto and 1 more

Abstract read
In one paragraph

Article in PloS one, 2017. 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
–field-weighted citation impact
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.

  1. Cyclomulberrin fromRSC advances · 2026
    Article
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  4. Article
  5. Review
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  7. Article
  8. Review
  9. Article
  10. Review
  11. Article
  12. Review
  13. Function of Platelet Glycosphingolipid Microdomains/Lipid Rafts.International journal of molecular sciences · 2020
    Review
  14. Article
  15. Article
  16. Arhgef1 Plays a Vital Role in Platelet Function and Thrombogenesis.Journal of the American Heart Association · 2019
    Article
  17. 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

11 authors.

Hiroko OhtsukaLaboratory of Biomembrane, Tokyo Metropolitan Institute of Medical Science, Tokyo, Japan.
Tomohiro IguchiLaboratory of Biomembrane, Tokyo Metropolitan Institute of Medical Science, Tokyo, Japan.
Moyuru HayashiLaboratory of Biomembrane, Tokyo Metropolitan Institute of Medical Science, Tokyo, Japan.
Mizuho KanedaLaboratory of Biomembrane, Tokyo Metropolitan Institute of Medical Science, Tokyo, Japan.
Kazuko IidaLaboratory of Biomembrane, Tokyo Metropolitan Institute of Medical Science, Tokyo, Japan.
Motoyuki ShimonakaDepartment of Chemistry, Tokyo University of Science, Tokyo, Japan.
Takahiko HaraStem Cell Project, Tokyo Metropolitan Institute of Medical Science, Tokyo, Japan.
Morio AraiBaxalta Japan Ltd., Tokyo, Japan.
Yuichi KoikeDepartment of Drug Metabolism and Clinical Pharmacokinetics, School of Pharmaceutical Sciences, Ohu University, Fukushima, Japan.
Naomasa YamamotoDepartment of Biochemistry, School of Pharmaceutical Sciences, Ohu University, Fukushima, Japan.
Kohji KasaharaLaboratory of Biomembrane, Tokyo Metropolitan Institute of Medical Science, Tokyo, Japan.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Stromal cell-derived factor-1α (SDF-1α)-induced platelet aggregation is mediated through its G protein-coupled receptor CXCR4 and phosphatidylinositol 3 kinase (PI3K). Here, we demonstrate that SDF-1α induces phosphorylation of Akt at Thr308 and Ser473 in human platelets. SDF-1α-induced platelet aggregation and Akt phosphorylation are inhibited by pretreatment with the CXCR4 antagonist AMD3100 or the PI3K inhibitor LY294002. SDF-1α also induces the phosphorylation of PDK1 at Ser241 (an upstream activator of Akt), GSK3β at Ser9 (a downstream substrate of Akt), and myosin light chain at Ser19 (a downstream element of the Akt signaling pathway). SDF-1α-induced platelet aggregation is inhibited by pretreatment with the Akt inhibitor MK-2206 in a dose-dependent manner. Furthermore, SDF-1α-induced platelet aggregation and Akt phosphorylation are inhibited by pretreatment with the raft-disrupting agent methyl-β-cyclodextrin. Sucrose density gradient analysis shows that 35% of CXCR4, 93% of the heterotrimeric G proteins Gαi-1, 91% of Gαi-2, 50% of Gβ and 4.0% of PI3Kβ, and 4.5% of Akt2 are localized in the detergent-resistant membrane raft fraction. These findings suggest that SDF-1α/CXCR4 signaling in lipid rafts induces platelet aggregation via PI3K-dependent Akt phosphorylation.

Indexed as

Platelet AggregationBlood PlateletsChemokine CXCL12HumansMembrane MicrodomainsPhosphatidylinositol 3-KinasesPhosphorylationProto-Oncogene Proteins c-aktReceptors, CXCR4Chemokine CXCL12CXCL12 protein, humanPhosphatidylinositol 3-KinasesProto-Oncogene Proteins c-aktReceptors, CXCR4

Identifiers

PMID28072855
PMCPMC5224795

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Registered trials

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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.