Evidence map›Paper›PMID 25510899›Full record

ArticleJournal of natural medicines2015

The TLR2 agonist in polysaccharide-K is a structurally distinct lipid which acts synergistically with the protein-bound β-glucan.

Kenneth Quayle, Catherine Coy, Leanna Standish, Hailing Lu

Abstract read
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In one paragraph

Article in Journal of natural medicines, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
0.4field-weighted citation impact, top 39% 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

14 citing papers in PubMed, 17 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Review
  5. COVID-19 and Cancer Diseases-The Potential ofInternational journal of molecular sciences · 2023
    Review
  6. Review
  7. Characterization of aInternational journal of molecular sciences · 2022
    Article
  8. Article
  9. TheFrontiers in molecular biosciences · 2021
    Article
  10. Biomedicines · 2020
    Review
  11. Article
  12. Review
  13. A Proinflammatory Effect of theMediators of inflammation · 2017
    Article
  14. 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

4 authors at 3 institutions in 1 country.

Kenneth QuayleTumor Vaccine Group, Department of Medicine, University of Washington, 850 Republican Street, Seattle, WA, 98109, USA, quaylek@uw.edu.
Catherine Coy
Leanna Standish
Hailing Lu
Bastyr University · USSeattle University · USUniversity of Washington · US

Funding

Enhancing innate immunity by combining PSK with docetaxel in/C.Higano/C.WennerU19AT006028 · NCCIH · BASTYR UNIVERSITY · PI DISIS, MARY L., STANDISH, LEANNA J · 2010 to 2013
$4.0M
NCCIH NIH HHS 3U19AT006028-02S1
6 · The paper itself

Abstract

Protein-bound polysaccharide-K (Krestin; PSK) is a hot-water extract of Trametes versicolor with immune stimulatory activity. It has been used for the past 30 years and has demonstrated anti-tumor efficacy in multiple types of cancer. The ability of PSK to activate dendritic cells and T cells is dependent on its ability to stimulate Toll-like receptor 2 (TLR2), yet it remains unknown which structural component within PSK activates TLR2. The purpose of this study was to identify the TLR2 agonist within PSK and understand its role in the overall mechanism of PSK's immunogenic activity. TLR2 activity was eliminated by treatment with lipoprotein lipase but not by trypsin or lyticase. Rapid centrifugation of PSK can separate the fraction with TLR2 agonist activity from the soluble β-glucan fraction. To study the potential interaction between the β-glucan component and the lipid component, we labeled the soluble β-glucan with fluorescein. Uptake of the labeled β-glucan by J774A macrophages and JAWSII dendritic cells was inhibited by anti-Dectin-1 antibody but not by anti-TLR2 antibody, confirming that Dectin-1 is the receptor for β-glucan. Interestingly, pre-treatment of JAWSII cells with the TLR2-active lipid fraction significantly enhanced the uptake of the soluble β-glucan, indicating the synergy between the TLR2 agonist component and the β-glucan component. Altogether, these results present evidence that PSK has two active components-the well-characterized protein-bound β-glucan and a previously unreported lipid-which work synergistically via the Dectin-1 and TLR2 receptors.

Indexed as

Adjuvants, ImmunologicAnimalsAntineoplastic Agentsbeta-GlucansBiological ProductsDectin-1Dendritic CellsDrug SynergismHumansLectins, C-TypeLipidsMacrophagesMiceProteoglycansT-LymphocytesToll-Like Receptor 2Adjuvants, ImmunologicAntineoplastic Agentsbeta-GlucansBiological ProductsDectin-1Lectins, C-TypeLipidspolysaccharide-KProteoglycansToll-Like Receptor 2

Identifiers

PMID25510899
OpenAlexW1986558147

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.