Evidence map›Paper›PMID 33120983›Full record

ArticleNutrients2020

Opposing Effect of Naringenin and Quercetin on the Junctional Compartment of MDCK II Cells to Modulate the Tight Junction.

Mio Nakashima, Misaki Hisada, Natsuko Goda, Takeshi Tenno, Ayaka Kotake, Yuko Inotsume, Ikuo Kameoka, Hidekazu Hiroaki

Open access · goldAbstract read
In one paragraph

Article in Nutrients, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
1.5field-weighted citation impact, top 17% 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

11 citing papers in PubMed, 25 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Article
  6. Quercetin improves and protects Calu-3 airway epithelial barrier function.Frontiers in cell and developmental biology · 2023
    Article
  7. Article
  8. Article
  9. Article
  10. Review
  11. 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

8 authors at 1 institution in 1 country.

Mio NakashimaGraduate School of Pharmaceutical Sciences, Nagoya University, Furocho, Chikusa, Nagoya, Aichi 464-8601, Japan.
Misaki HisadaGraduate School of Pharmaceutical Sciences, Nagoya University, Furocho, Chikusa, Nagoya, Aichi 464-8601, Japan.
Natsuko GodaGraduate School of Pharmaceutical Sciences, Nagoya University, Furocho, Chikusa, Nagoya, Aichi 464-8601, Japan.
Takeshi TennoGraduate School of Pharmaceutical Sciences, Nagoya University, Furocho, Chikusa, Nagoya, Aichi 464-8601, Japan.
Ayaka KotakeCosmetics Research Department, Nicca Chemical Co. Ltd., Fukui 910-8670, Japan.
Yuko InotsumeCosmetics Research Department, Nicca Chemical Co. Ltd., Fukui 910-8670, Japan.
Ikuo KameokaCosmetics Research Department, Nicca Chemical Co. Ltd., Fukui 910-8670, Japan.
Hidekazu HiroakiGraduate School of Pharmaceutical Sciences, Nagoya University, Furocho, Chikusa, Nagoya, Aichi 464-8601, Japan.ORCID 0000-0003-1621-5893
Nagoya University · JP

Funding

KOSÉ Cosmetology Research Foundation 27-597The Japan Food Chemical Research Foundation H31-006
6 · The paper itself

Abstract

Maintaining tight junction (TJ) integrity is important for epithelial cell barriers. Previously, the enhancement of TJ integrity, induced by citrus-derived flavonoids, naringin (NRG) and hesperidin (HSD), was demonstrated, but the effects of their aglycones naringenin (NAR) and hesperetin (HST), and the mechanisms, have not been systematically investigated. Here we compared three series of flavonoids related to NAR, HST, quercetin (QUE) and their glycosides with the Madin-Darby canine kidney (MDCK) II cell monolayers. The effect of flavonoids on the protein expression level of claudin (CLD)-2 and its subcellular localization were investigated. NAR, NRG, and HSD increased the CLD-2 localization at the TJ compartment, and its protein expression level. QUE and HST showed TJ-mitigating activity. Narirutin (NRT), neohesperidin (NHD) and rutin (RUT) did not affect the TJ. In addition, NAR and QUE induced an increase or decrease of the transepithelial electrical resistance (TEER) values of the MDCK II monolayers. Two known signaling pathways, phosphatidyl-inositol-3 kinase (PI3K) and 5'-AMP-activated protein kinase (AMPK), were further compared with NAR. Two-dimensional polyacrylamide electrophoresis (2D PAGE) analysis of whole-cell proteins treated with NAR, AICA-riboside (AMPK activator) and LY294002 (PI3K inhibitor) showed in both a distinct pattern. This suggests the target of NAR's CLD-2 or zonula occludens-1 (ZO-1) modulation was unique.

Indexed as

AMP-Activated Protein KinasesAnimalsClaudin-2DogsEpithelial CellsFlavanonesKidneyMadin Darby Canine Kidney CellsPhosphatidylinositol 3-KinasesQuercetinSignal TransductionTight JunctionsZonula Occludens-1 ProteinAMP-Activated Protein KinasesClaudin-2FlavanonesnaringeninPhosphatidylinositol 3-KinasesQuercetinZonula Occludens-1 Protein5′ adenosine monophosphate (AMP)-activated protein kinasedynamic equilibrium of tight junctionepithelial barrier enhancerflavonoidsphosphatidylinositol-3-phosphate kinasetight junction integrity

Identifiers

PMID33120983
PMCPMC7693399
OpenAlexW3097736133

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.