Evidence map›Paper›PMID 27417293›Full record

ArticleScientific reports2016

Glycosylation enables aesculin to activate Nrf2.

Kyun Ha Kim, Hyunsu Park, Hee Jin Park, Kyoung-Hwa Choi, Ruxana T Sadikot, Jaeho Cha, Myungsoo Joo

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
0.5field-weighted citation impact, top 28% 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

10 citing papers in PubMed, 14 citations in OpenAlex.

  1. Article
  2. Article
  3. Bioactive compounds isolated from the bark ofPhytochemistry letters · 2024
    Article
  4. Review
  5. Review
  6. Coumarin Derivatives in Inflammatory Bowel Disease.Molecules (Basel, Switzerland) · 2021
    Review
  7. Review
  8. Article
  9. Coumarins as Modulators of the Keap1/Nrf2/ARE Signaling Pathway.Oxidative medicine and cellular longevity · 2020
    Review
  10. 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

7 authors at 2 institutions in 2 countries.

Kyun Ha KimSchool of Korean Medicine, Pusan National University, Yangsan 626-870, Korea.
Hyunsu ParkDepartment of Microbiology, Pusan National University, Busan 609-735, Korea.
Hee Jin ParkDepartment of Microbiology, Pusan National University, Busan 609-735, Korea.
Kyoung-Hwa ChoiDepartment of Microbiology, Pusan National University, Busan 609-735, Korea.
Ruxana T SadikotSection of Pulmonary and Critical Care Medicine, Atlanta Veterans Affairs Medical Center, Emory University, Decatur, GA30033, USA.
Jaeho ChaDepartment of Microbiology, Pusan National University, Busan 609-735, Korea.
Myungsoo JooSchool of Korean Medicine, Pusan National University, Yangsan 626-870, Korea.
Pusan National University · KREmory University · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Since aesculin, 6,7-dihydroxycoumarin-6-O-β-glucopyranoside, suppresses inflammation, we asked whether its anti-inflammatory activity is associated with the activation of nuclear factor-E2-related factor 2 (Nrf2), a key anti-inflammatory factor. Our results, however, show that aesculin marginally activated Nrf2. Since glycosylation can enhance the function of a compound, we then asked whether adding a glucose makes aesculin activate Nrf2. Our results show that the glycosylated aesculin, 3-O-β-d-glycosyl aesculin, robustly activated Nrf2, inducing the expression of Nrf2-dependent genes, such as heme oxygenase-1, glutamate-cysteine ligase catalytic subunit, and NAD(P)H quinone oxidoreductase 1 in macrophages. Mechanistically, 3-O-β-d-glycosyl aesculin suppressed ubiquitination of Nrf2, retarding degradation of Nrf2. Unlike aesculin, 3-O-β-d-glycosyl aesculin significantly suppressed neutrophilic lung inflammation, a hallmark of acute lung injury (ALI), in mice, which was not recapitulated in Nrf2 knockout mice, suggesting that the anti-inflammatory function of the compound largely acts through Nrf2. In a mouse model of sepsis, a major cause of ALI, 3-O-β-d-glycosyl aesculin significantly enhanced the survival of mice, compared with aesculin. Together, these results show that glycosylation could confer the ability to activate Nrf2 on aesculin, enhancing the anti-inflammatory function of aesculin. These results suggest that glycosylation can be a way to improve or alter the function of aesculin.

Indexed as

Acute Lung InjuryAnimalsCarbon-13 Magnetic Resonance SpectroscopyEsculinGlycosylationHEK293 CellsHumansMiceMice, Inbred C57BLMice, KnockoutNeutrophilsNF-E2-Related Factor 2PneumoniaProton Magnetic Resonance SpectroscopyRAW 264.7 CellsSepsisEsculinNF-E2-Related Factor 2

Identifiers

PMID27417293
PMCPMC4945939
OpenAlexW2467471929

What OpenQuestion holds

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LicenceCC BY
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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.