ArticleProceedings of the National Academy of Sciences of the United States of America1997
Luminal trypsin may regulate enterocytes through proteinase-activated receptor 2.
Article in Proceedings of the National Academy of Sciences of the United States of America, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 91 papers.
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Who cites it
91 citing papers in PubMed, 319 citations in OpenAlex.
- Assessment of the interaction between sodium dodecyl sulfate and trypsin enzyme through micellization and thermodynamic analysis.RSC advances · 2026Article
- Feedback Regulation of Pancreatic Juice Secretion in Pigs.Biomolecules · 2026Article
- Modulation of Nociceptive Ion Channels by Protease-Activated Receptor-2 in Inflammatory Pain: Molecular Mechanisms and Therapeutic Potential.International journal of molecular sciences · 2026Review
- Hereditary α-tryptasemia; a review of mechanisms linking α-tryptase gene dosage to intestinal homeostasis and immunopathology.Frontiers in allergy · 2026Review
- An update on mechanisms of pruritus and their potential treatment in primary cutaneous T-cell lymphoma.Clinical and experimental medicine · 2023Review
- Protease-activated receptors in health and disease.Physiological reviews · 2023Review
- Inflammation and Impaired Gut Physiology in Post-operative Ileus: Mechanisms and the Treatment Options.Journal of neurogastroenterology and motility · 2022Review
- Mice expressing fluorescent PARProceedings of the National Academy of Sciences of the United States of America · 2022Article
- The Transmembrane Protease TMPRSS2 as a Therapeutic Target for COVID-19 Treatment.International journal of molecular sciences · 2022Review
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- 3D printed personalized magnetic micromachines from patient blood-derived biomaterials.Science advances · 2021Article
- Protease Activated Receptors and Arthritis.International journal of molecular sciences · 2021Review
- Hydroelectrolytic Disorder in COVID-19 patients: Evidence Supporting the Involvement of Subfornical Organ and Paraventricular Nucleus of the Hypothalamus.Neuroscience and biobehavioral reviews · 2021Review
- The Immature Gut Barrier and Its Importance in Establishing Immunity in Newborn Mammals.Frontiers in immunology · 2020Review
- TRPV1 activity and substance P release are required for corneal cold nociception.Nature communications · 2019Article
- Effects of probiotic supplementation on post-infectious irritable bowel syndrome in rodent model.BMC complementary and alternative medicine · 2019Article
- G-Protein-Coupled Receptors Are Dynamic Regulators of Digestion and Targets for Digestive Diseases.Gastroenterology · 2019Review
- Protease Activated Receptor-2 Induces Immune Activation and Visceral Hypersensitivity in Post-infectious Irritable Bowel Syndrome Mice.Digestive diseases and sciences · 2019Article
- Protease-Activated Receptors in the Intestine: Focus on Inflammation and Cancer.Frontiers in endocrinology · 2019Review
- Responses of rainbow trout intestinal epithelial cells to different kinds of nutritional deprivation.Fish physiology and biochemistry · 2018Article
31 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
7 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Proteinase-activated receptor 2 (PAR-2) is a recently characterized G-protein coupled receptor that is cleaved and activated by pancreatic trypsin. Trypsin is usually considered a digestive enzyme in the intestinal lumen. We examined the hypothesis that trypsin, at concentrations normally present in the lumen of the small intestine, is also a signaling molecule that specifically regulates enterocytes by activating PAR-2. PAR-2 mRNA was highly expressed in the mucosa of the small intestine and in an enterocyte cell line. Immunoreactive PAR-2 was detected at the apical membrane of enterocytes, where it could be cleaved by luminal trypsin. Physiological concentrations of pancreatic trypsin and a peptide corresponding to the tethered ligand of PAR-2, which is exposed by trypsin cleavage, stimulated generation of inositol 1,4,5-trisphosphate, arachidonic acid release, and secretion of prostaglandin E2 and F1alpha from enterocytes and a transfected cell line. Application of trypsin to the apical membrane of enterocytes and to the mucosal surface of everted sacs of jejunum also stimulated prostaglandin E2 secretion. Thus, luminal trypsin activates PAR-2 at the apical membrane of enterocytes to stimulate secretion of eicosanoids, which regulate multiple cell types in a paracrine and autocrine manner. We conclude that trypsin is a signaling molecule that specifically regulates enterocytes by triggering PAR-2.
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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.