ArticleInflammatory bowel diseases2011
Matrilysin-1 (MMP7) cleaves galectin-3 and inhibits wound healing in intestinal epithelial cells.
Article in Inflammatory bowel diseases, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.
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Who cites it
35 citing papers in PubMed, 70 citations in OpenAlex.
- Review
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- Age-Related Transcriptomic Changes in the Vermiform Appendix.International journal of molecular sciences · 2025Article
- Spatiotemporal Adaptations-Driven Dynamic Thra Activation Simulates a Skin Wound Healing Response.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Article
- Novel anti-inflammatory properties of mannose oligosaccharides in the treatment of inflammatory bowel disease via LGALS3 modulation.NPJ biofilms and microbiomes · 2025Article
- Galectins in epithelial-mesenchymal transition: roles and mechanisms contributing to tissue repair, fibrosis and cancer metastasis.Biological research · 2024Review
- Article
- Integrative multi-omics deciphers the spatial characteristics of host-gut microbiota interactions in Crohn's disease.Cell reports. Medicine · 2023Article
- Matrix metalloproteinase 7 contributes to intestinal barrier dysfunction by degrading tight junction protein Claudin-7.Frontiers in immunology · 2022Article
- Roles of MicroRNA-21 in Skin Wound Healing: A Comprehensive Review.Frontiers in pharmacology · 2022Review
- Galectins in Cancer and the Microenvironment: Functional Roles, Therapeutic Developments, and Perspectives.Biomedicines · 2021Review
- Galectin-3 Identifies a Subset of Macrophages With a Potential Beneficial Role in Atherosclerosis.Arteriosclerosis, thrombosis, and vascular biology · 2020Article
- Galectin-3 Is a Potential Mediator for Atherosclerosis.Journal of immunology research · 2020Review
- Pleiotropic Effects of Modified Citrus Pectin.Nutrients · 2019Review
- Galectin-3 as a candidate upstream biomarker for quantifying risks of myocardial ageing.ESC heart failure · 2019Article
- Arecoline Promotes Migration of A549 Lung Cancer Cells through Activating the EGFR/Src/FAK Pathway.Toxins · 2019Article
- In-feed resin acids reduce matrix metalloproteinase activity in the ileal mucosa of healthy broilers without inducing major effects on the gut microbiota.Veterinary research · 2019Article
- Activation of Resolution Pathways to Prevent and Fight Chronic Inflammation: Lessons From Asthma and Inflammatory Bowel Disease.Frontiers in immunology · 2019Review
- Galectin-3: One Molecule for an Alphabet of Diseases, from A to Z.International journal of molecular sciences · 2018Review
- Quantitative proteomics reveal the anti-tumour mechanism of the carbohydrate recognition domain of Galectin-3 in Hepatocellular carcinoma.Scientific reports · 2017Article
Corrections and comments
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Authors and funding
6 authors at 3 institutions in 1 country.
Funding
Abstract
backgroundGalectin-3 is an animal lectin that has been implicated in wound healing and is decreased in inflammatory bowel disease (IBD). Matrix metalloproteinase-7 (MMP7), also known as matrilysin-1, a protease shown to cleave extracellular matrix proteins, is highly expressed in IBD tissues, especially at the leading edge of gastrointestinal ulcers. The ability of MMP7 to cleave galectin-3 and influence wound healing has not been reported previously. The aim was to determine whether MMP7 cleaves galectin-3 and modulates wound healing in intestinal epithelial cells.
methodsThe cleaved fragments of galectin-3 were identified by N-terminal sequencing and mass spectrometry. Western blotting was used to detect the cleaved galectin-3 products in a colonic epithelial cell line (T84 cells). Cell migration was studied by the in vitro scratch method.
resultsWe demonstrate for the first time that MMP7 cleaves galectin-3 in vitro, resulting in three cleaved fragments (20.2 kDa, 18.9 kDa, and 15.5 kDa). Exogenous treatment of T84 cells with recombinant MMP7 resulted in the appearance of secreted galectin-3 cleavage fragments in the supernatant. MMP7 inhibited cell migration and resulted in wound retraction and the addition of MMP7 to galectin-3 abrogated the wound healing and cell migration induced by galectin-3.
conclusionsWe have demonstrated that galectin-3 is a substrate for MMP7. Cleavage of galectin-3 may be one mechanism by which MMP7 inhibits wound healing. This study has significance in understanding delayed wound healing in chronic intestinal diseases like intestinal ulcers and IBD, where MMP7 protein expression is elevated with a decreased galectin-3 protein expression.
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