Protease inhibition as new therapeutic strategy for GI diseases
Open accessAbstract
The GI tract is the most exposed organ to proteases, both in physiological and pathophysiological conditions. For digestive purposes, the lumen of the upper GI tract contains large amounts of pancreatic proteases, but studies have also demonstrated increased proteolytic activity into mucosal tissues (both in the upper and lower GI tract), associated with pathological conditions. This review aims at outlining the evidences for dysregulated proteolytic homeostasis in GI diseases and the pathogenic mechanisms of increased proteolytic activity. The therapeutic potential of protease inhibition in GI diseases is discussed, with a particular focus on IBDs, functional GI disorders and colorectal cancer.
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Host proteases such as chymase or ELA2A are able to cleave tight and adherens junction proteins including zonula occludens-1 or E-cadherin.
“Host proteases such as chymase or ELA2A are able to cleave tight and adherens junction proteins including zonula occludens-1 or E-cadherin.22,29,130”
From The emerging roles of bacterial proteases in intestinal diseases (2023) · cites this paper as [22]
Activation of the different members of the PAR family is protease specific, tightly regulated and influences physiological functions in the gut such as motility, permeability and nociception.
“The activation of the different members of the PAR family (PAR-1, 2,3 and 4) is protease specific, tightly regulated and influences a number of physiological functions in the gut such as motility, permeability and nociception.22”
From The emerging roles of bacterial proteases in intestinal diseases (2023) · cites this paper as [22]
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Tissue Inhibitor of Metalloproteinase-3 Regulates Inflammation in Human and Mouse Intestine
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Serine proteases decrease intestinal epithelial ion permeability by activation of protein kinase Cζ
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Proteinase-activated receptors (PARs) in infection and inflammation in the gut
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Self-citationFranzè, E., Caruso, R., Stolfi, C., Sarra, M., Cupi, M. L., Ascolani, M., Sedda, S., Antenucci, C., Ruffa, A., Caprioli, F., et al. (2013) · Inflammatory Bowel Diseases · doi:10.1097/mib.0b013e31828028e8 · Cited by 29 · see citing works
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Degradomics of matrix metalloproteinases in inflammatory diseases
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Proteases/Antiproteases in Inflammatory Bowel Diseases
Motta, J., Martin, L., & Vergnolle, N. (2011) · Springer eBooks · doi:10.1007/978-3-0348-0157-7_8 · Cited by 11 · see citing works
Self-citationProteases from Inflammatory Cells: Regulation of Inflammatory Response
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Oliphant, K., & Allen-Vercoe, E. (2019) · Microbiome · doi:10.1186/s40168-019-0704-8 · Cited by 1,327 · see citing works
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Serine proteases as luminal mediators of intestinal barrier dysfunction and symptom severity in IBS
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Fecal Serine Protease Profiling in Inflammatory Bowel Diseases
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Functional Proteomic Profiling of Secreted Serine Proteases in Health and Inflammatory Bowel Disease
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Self-citationThe emerging roles of bacterial proteases in intestinal diseases
Caminero, A., Guzman, M., Libertucci, J., & Lomax, A. E. (2023) · Gut Microbes · doi:10.1080/19490976.2023.2181922 · Cited by 92 · see citing works
Zhang, Z., Tanaka, I., Pan, Z., Ernst, P. B., Kiyono, H., & Kurashima, Y. (2022) · European Journal of Immunology · doi:10.1002/eji.202149532 · Cited by 69 · see citing works
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Self-citationKriaa, A., Jablaoui, A., Rhimi, S., Soussou, S., Mkaouar, H., Mariaule, V., Gruba, N., Gargouri, A., Maguin, E., Lesner, A., et al. (2021) · Cells · doi:10.3390/cells10102658 · Cited by 16 · see citing works
- Authors
- Vergnolle, N.
- Affiliations
- Université Toulouse III - Paul Sabatier (FR)
- Corresponding author
- Vergnolle, Nathalie
- ORCID
- Vergnolle, Nathalie
- Venue
- Gut
- Publisher
- BMJ
- Published
- 2016-04-12
- Volume
- 65
- Issue
- 7
- Pages
- 1215-1224
- ISSN
- 0017-5749 (ISSN-L)
- 1468-3288
- PMC
- PMC4941139
- OpenAlex
- W2335993428
- Cited by
- 226
- References
- 105
- Citations by year
- 2026: 12 · 2025: 24 · 2024: 22 · 2023: 20 · 2022: 27 · 2021: 35 · 2020: 19 · 2019: 26 · 2018: 21 · 2017: 13 · 2016: 5 · 2015: 1
- FWCI
- 1.99
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- cc-by-nc
- Locations
- Gut (publishedVersion, cc-by-nc)
- PubMed Central (publishedVersion, cc-by-nc)
- PubMed (publishedVersion)
- HAL (submittedVersion, cc-by-nc)
- HighWire Press Open Archive (submittedVersion)
- Funders
- Agence Nationale de la Recherche (R12177BB)
- Association Francois Aupetit
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › Protease and Inhibitor Mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Inflammatory Bowel Disease
- Health Sciences › Medicine › Hematology › Blood Coagulation and Thrombosis Mechanisms
- Keywords
- protease inhibition, gastrointestinal diseases, intestinal mucosa, pancreatic proteases, inflammatory bowel disease, functional gastrointestinal disorders, colorectal cancer, treatment options
- MeSH terms
- Animals, Celiac Disease, Gastrointestinal Diseases, Humans, Peptide Hydrolases, Protease Inhibitors, Colorectal Neoplasms, Inflammatory Bowel Diseases
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
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