Evidence map›Paper›PMID 17114298›Full record

ArticleGut2007

Protease-activated receptor-2 protects against pancreatitis by stimulating exocrine secretion.

Vijay P Singh, Lakshmi Bhagat, Sarah Navina, Rifat Sharif, Rajinder K Dawra, Ashok K Saluja

Open access · bronzeAbstract read
In one paragraph

Article in Gut, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.

0numbers the graph read from it
0cells of the map it votes in
31citing papers in PubMed
3.2field-weighted citation impact, top 7% 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

31 citing papers in PubMed, 74 citations in OpenAlex.

  1. Trial
  2. Pathologically relevant trypsinogen activation in pancreatitis.American journal of physiology. Gastrointestinal and liver physiology · 2026
    Review
  3. Review
  4. Article
  5. PAR2: The Cornerstone of Pancreatic Diseases.Physiological research · 2022
    Review
  6. Mouse model suggests limited role for human mesotrypsin in pancreatitis.Pancreatology : official journal of the International Association of Pancreatology (IAP) ... [et al.] · 2021
    Article
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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

6 authors at 3 institutions in 1 country.

Vijay P SinghDepartment of Gastroenterology, Mayo Clinic, Rochester, Minnesota, USA.
Lakshmi Bhagat
Sarah Navina
Rifat Sharif
Rajinder K Dawra
Ashok K Saluja
University of Minnesota · USIdera Pharmaceuticals (United States) · USMayo Clinic · US

Funding

NIDDK NIH HHS DK58649
6 · The paper itself

Abstract

backgroundProtease-activated receptor-2 (PAR-2) is present in the pancreas, where it has been shown to play a protective role during pancreatitis. However, the mechanism by which it protects against pancreatitis still remains to be elucidated. Acute pancreatitis is associated with premature zymogen activation and a blockage in digestive enzyme secretion.

aimTo examine the effects of PAR-2 activation on the severity of pancreatitis, and to determine whether its protective effects are mediated by affecting either premature activation or secretory blockage, or both.

resultsThe results confirmed that PAR-2 -/- mice have more severe pancreatitis than wild-type mice. Interestingly, intrapancreatic trypsin levels in the PAR-2 knockouts remained high after 6 h of pancreatitis, whereas they reverted to normal in the wild types. During pancreatitis, PAR-2 mRNA levels were upregulated in wild-type mice in response to supramaximal caerulein administration. Further, after a single injection of supramaximal caerulein, PAR-2 mRNA levels were also elevated, reaching a peak at 3 h. Stimulating PAR-2 with trypsin or the PAR-2-activating peptide, serine-leucine-isoleucine-glycine-arginine-leucine (SLIGRL), induced significantly more secretion from the acini of these caerulein-sensitised mice compared with the controls. PAR-2 activation also reversed the inhibition of secretion observed in both the caerulein and arginine models.

conclusionsTrypsin released during the early stages of pancreatitis activates PAR-2 receptors on the acinar cells and stimulates secretion from these cells. Thus, PAR-2 activation may decrease pancreatic injury and limit the severity of pancreatitis by allowing extracellular trypsin to act as a secretagogue.

Indexed as

Acute DiseaseAmylasesAnimalsArginineCeruletideDisease Models, AnimalEnzyme ActivationMaleMiceMice, Inbred C57BLMice, KnockoutPancreas, ExocrinePancreatitisReceptor, PAR-2RNA, MessengerTissue Culture TechniquesAmylasesArginineCeruletideReceptor, PAR-2RNA, MessengerTranscription FactorsTrypsin

Identifiers

PMID17114298
PMCPMC1994368
OpenAlexW2289439614

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.