Evidence map›Paper›PMID 35269499›Full record

ArticleCells2022

Modulation of Intestinal Epithelial Permeability via Protease-Activated Receptor-2-Induced Autophagy.

Yuju Kim, Yunna Lee, Gwangbeom Heo, Sihyun Jeong, Soyeong Park, Jin-Wook Yoo, Yunjin Jung, Eunok Im

Open access · goldAbstract read
In one paragraph

Article in Cells, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
2.8field-weighted citation impact, top 9% 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

12 citing papers in PubMed, 18 citations in OpenAlex.

  1. Article
  2. Proteases in intestinal health and disease.Nature reviews. Gastroenterology & hepatology · 2026
    Review
  3. Review
  4. Tryptophan Indole Derivatives: Key Players in Type 2 Diabetes Mellitus.Diabetes, metabolic syndrome and obesity : targets and therapy · 2025
    Review
  5. Article
  6. Review
  7. Review
  8. Review
  9. Review
  10. Molecules (Basel, Switzerland) · 2023
    Article
  11. Review
  12. 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

8 authors at 1 institution in 1 country.

Yuju KimDepartment of Pharmacy, College of Pharmacy, Pusan National University, Busan 46241, Korea.
Yunna LeeDepartment of Pharmacy, College of Pharmacy, Pusan National University, Busan 46241, Korea.
Gwangbeom HeoDepartment of Pharmacy, College of Pharmacy, Pusan National University, Busan 46241, Korea.
Sihyun JeongDepartment of Pharmacy, College of Pharmacy, Pusan National University, Busan 46241, Korea.
Soyeong ParkDepartment of Pharmacy, College of Pharmacy, Pusan National University, Busan 46241, Korea.
Jin-Wook YooDepartment of Manufacturing Pharmacy, College of Pharmacy, Pusan National University, Busan 46241, Korea.ORCID 0000-0001-5216-5518
Yunjin JungDepartment of Manufacturing Pharmacy, College of Pharmacy, Pusan National University, Busan 46241, Korea.
Eunok ImDepartment of Pharmacy, College of Pharmacy, Pusan National University, Busan 46241, Korea.ORCID 0000-0002-9949-8819
Pusan National University · KR

Funding

National Research Foundation of Korea 2019R1A2C1010536
6 · The paper itself

Abstract

Protease-activated receptor 2 (PAR2) alleviates intestinal inflammation by upregulating autophagy. PAR2 also modulates tight junctions through β-arrestin signaling. Therefore, we investigated the effect of PAR2-induced autophagy on intestinal epithelial tight junctions and permeability. RT-PCR, Western blot analysis, and immunoprecipitation were performed to investigate the underlying molecular mechanisms by which PAR2 regulates autophagy and intestinal epithelial tight junctions. Inhibition of PAR2 by GB83, a PAR2 antagonist, decreased the expression of autophagy-related and tight-junction-related factors in Caco-2 cells. Moreover, inhibition of PAR2 decreased intestinal transepithelial electrical resistance. When PAR2 was activated, intestinal permeability was maintained, but when autophagy was suppressed by chloroquine, intestinal permeability was significantly increased. In addition, the prolongation of ERK1/2 phosphorylation by PAR2-ERK1/2-β-arrestin assembly was reduced under autophagy inhibition conditions. Therefore, PAR2 induces autophagy to regulate intestinal epithelial permeability, suggesting that it is related to the β-arrestin-ERK1/2 pathway. In conclusion, regulating intestinal epithelial permeability through PAR2-induced autophagy can help maintain mucosal barrier integrity. Therefore, these findings suggest that the regulation of PAR2 can be a suitable strategy to treat intestinal diseases caused by permeability dysfunction.

Indexed as

Autophagybeta-ArrestinsCaco-2 CellsHumansPermeabilityReceptor, PAR-2beta-ArrestinsF2RL1 protein, humanReceptor, PAR-2autophagyPAR2permeabilitytight junctionβ-arrestin

Identifiers

PMID35269499
PMCPMC8909592
OpenAlexW4214873617

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.