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dc.contributor.author
Di Sabatino, Antonio
dc.contributor.author
Pender, Sylvia L.F.
dc.contributor.author
Jackson, Claire L.
dc.contributor.author
Prothero, Joanna D.
dc.contributor.author
Gordon, John N.
dc.contributor.author
Picariello, Lucia
dc.contributor.author
Rovedatti, Laura
dc.contributor.author
Docena, Guillermo H.
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dc.contributor.author
Monteleone, Giovanni
dc.contributor.author
Rampton, David S.
dc.contributor.author
Tonelli, Francesco
dc.contributor.author
Corazza, Gino R.
dc.contributor.author
MacDonald, Thomas T.
dc.date.available
2020-08-06T15:09:28Z
dc.date.issued
2007-07
dc.identifier.citation
Di Sabatino, Antonio; Pender, Sylvia L.F.; Jackson, Claire L.; Prothero, Joanna D.; Gordon, John N.; et al.; Functional Modulation of Crohn’s Disease Myofibroblasts by Anti-Tumor Necrosis Factor Antibodies; W B Saunders Co-Elsevier Inc; Gastroenterology; 133; 1; 7-2007; 137-149
dc.identifier.issn
0016-5085
dc.identifier.uri
http://hdl.handle.net/11336/111027
dc.description.abstract
Infliximab induces immune cell apoptosis by outside-to-inside signaling through transmembrane tumor necrosis factor-α (mTNF). However, in inflamed gut, myofibroblasts also produce TNF-α, and the affects of anti-TNF antibodies on these structural cells are unknown. We investigated the action of infliximab on apoptosis, the production of matrix metalloproteinases (MMPs) and tissue inhibitor of metalloproteinases (TIMP)-1, and migration of Crohn’s disease (CD) myofibroblasts. Methods: Colonic myofibroblasts were isolated from patients with active CD and controls. mTNF was evaluated by Western blotting and flow cytometry. Infliximab-treated myofibroblasts were analyzed for apoptosis by Annexin V staining and caspase-3. TIMP-1 and MMPs were measured by Western blotting, and fibroblast migration was assessed by using an in vitro wound-healing scratch assay. Results: CD myofibroblasts showed higher mTNF expression than control myofibroblasts. Infliximab had no effect on CD myofibroblast apoptosis, caspase-3 activation, and production of MMP-3 and MMP-12. However, infliximab induced a significant dose-dependent increase in TIMP-1 production, which was inhibited by the p38 mitogen-activated protein kinase inhibitor SB 203580. The anti-TNF agents adalimumab, etanercept, and p55 TNF-receptor–human IgG fusion protein also increased TIMP-1 production. The migration of CD myofibroblasts was enhanced significantly by infliximab and recombinant human TIMP-1, and infliximab-induced migration was inhibited by anti–TIMP-1 neutralizing antibody. Infliximab also decreased CD myofibroblast collagen production. Conclusions: Our findings show a novel therapeutic pathway for anti-TNF therapies in enhancing TIMP-1 production and myofibroblast migration, which may reduce MMP activity and facilitate the wound healing.
dc.format
application/pdf
dc.language.iso
eng
dc.publisher
W B Saunders Co-Elsevier Inc
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dc.rights
info:eu-repo/semantics/openAccess
dc.rights.uri
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.subject
IBD
dc.subject
TNF
dc.subject
INFLIXIMAB
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MYOFIBROBLAST
dc.subject.classification
Otras Ciencias de la Salud
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dc.subject.classification
Ciencias de la Salud
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dc.subject.classification
CIENCIAS MÉDICAS Y DE LA SALUD
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dc.title
Functional Modulation of Crohn’s Disease Myofibroblasts by Anti-Tumor Necrosis Factor Antibodies
dc.type
info:eu-repo/semantics/article
dc.type
info:ar-repo/semantics/artículo
dc.type
info:eu-repo/semantics/publishedVersion
dc.date.updated
2020-07-20T20:21:38Z
dc.identifier.eissn
1528-0012
dc.journal.volume
133
dc.journal.number
1
dc.journal.pagination
137-149
dc.journal.pais
Estados Unidos
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dc.journal.ciudad
Philadelphia
dc.description.fil
Fil: Di Sabatino, Antonio. Universita Degli Studi Di Pavia; Italia
dc.description.fil
Fil: Pender, Sylvia L.F.. University of Southampton; Reino Unido
dc.description.fil
Fil: Jackson, Claire L.. University of Southampton; Reino Unido
dc.description.fil
Fil: Prothero, Joanna D.. University of Southampton; Reino Unido
dc.description.fil
Fil: Gordon, John N.. Royal Hampshire County Hospital; Reino Unido
dc.description.fil
Fil: Picariello, Lucia. Università degli Studi di Firenze; Italia
dc.description.fil
Fil: Rovedatti, Laura. Universita Degli Studi Di Pavia; Italia
dc.description.fil
Fil: Docena, Guillermo H.. Provincia de Buenos Aires. Gobernación. Comisión de Investigaciones Científicas. Centro de Investigación y Desarrollo en Criotecnología de Alimentos. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Centro de Investigación y Desarrollo en Criotecnología de Alimentos. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Centro de Investigación y Desarrollo en Criotecnología de Alimentos; Argentina
dc.description.fil
Fil: Monteleone, Giovanni. Universita Tor Vergata; Italia
dc.description.fil
Fil: Rampton, David S.. The Royal London Hospital; Reino Unido
dc.description.fil
Fil: Tonelli, Francesco. Università degli Studi di Firenze; Italia
dc.description.fil
Fil: Corazza, Gino R.. Universita Degli Studi Di Pavia; Italia
dc.description.fil
Fil: MacDonald, Thomas T.. Barts and The London School of Medicine and Dentistry; Reino Unido
dc.journal.title
Gastroenterology
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dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/abs/pii/S0016508507009262
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/doi/http://dx.doi.org/10.1053/j.gastro.2007.04.069
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