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PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
2009-7-21
pubmed:abstractText
The interaction of fibroblast growth factor-inducible 14 (Fn14) and, its ligand tumor necrosis factor-like weak inducer of apoptosis (TWEAK) is known to be important in wound healing of tissues. However, to our knowledge, expression and function of Fn14 in corneal myofibroblasts, which have a crucial role in wound healing of corneal stroma, has not been investigated. In this study, we investigated the expression and function of Fn14 in corneal myofibroblasts. Expression of Fn14 protein was assessed by flow cytometry. Corneal myofibroblasts showed strong expression of Fn14 protein, while keratocytes did not. TGF-beta(1) promoted the differentiation of keratocytes into corneal myofibroblasts, and induced Fn14 expression. These data reveal that keratocytes phenotype determines the level of Fn14 expression. ELISA was used to detect chemokines and matrix metalloproteinases in the supernatant of corneal myofibroblasts cultured with or without stimulation by TWEAK and/or TGF-beta(1). TWEAK increased the production of IL-8, MCP-1, and RANTES by corneal myofibroblasts via Fn14. TGF-beta(1) augmented the TWEAK-induced production of these chemokines. TWEAK also increased the production of MMP-1 and -3 by corneal myofibroblasts via Fn14, while TGF-beta(1) inhibited this effect of TWEAK on MMP production. TWEAK-induced phosphorylation of NF-kappaB and MAP kinase in corneal myofibroblasts. Furthermore, TWEAK partially inhibited the differentiation of keratocytes into corneal myofibroblasts promoted by TGF-beta(1). These data suggest that the Fn14/TWEAK system may have several roles in wound healing by corneal myofibroblasts. In the future, modulation of the TWEAK/Fn14 system may become a novel approach for control corneal wound healing.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/Actins, http://linkedlifedata.com/resource/pubmed/chemical/Chemokines, http://linkedlifedata.com/resource/pubmed/chemical/Eye Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Fibroblast Growth Factors, http://linkedlifedata.com/resource/pubmed/chemical/Matrix Metalloproteinase 1, http://linkedlifedata.com/resource/pubmed/chemical/Matrix Metalloproteinase 2, http://linkedlifedata.com/resource/pubmed/chemical/Mitogen-Activated Protein Kinases, http://linkedlifedata.com/resource/pubmed/chemical/NF-kappa B, http://linkedlifedata.com/resource/pubmed/chemical/TNFSF12 protein, human, http://linkedlifedata.com/resource/pubmed/chemical/Transforming Growth Factor beta1, http://linkedlifedata.com/resource/pubmed/chemical/Tumor Necrosis Factors, http://linkedlifedata.com/resource/pubmed/chemical/fibroblast growth factor 14
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
1096-0007
pubmed:author
pubmed:issnType
Electronic
pubmed:volume
89
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
256-62
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed-meshheading:19344712-Actins, pubmed-meshheading:19344712-Aged, pubmed-meshheading:19344712-Cell Differentiation, pubmed-meshheading:19344712-Cells, Cultured, pubmed-meshheading:19344712-Chemokines, pubmed-meshheading:19344712-Cornea, pubmed-meshheading:19344712-Drug Interactions, pubmed-meshheading:19344712-Eye Proteins, pubmed-meshheading:19344712-Fibroblast Growth Factors, pubmed-meshheading:19344712-Fibroblasts, pubmed-meshheading:19344712-Humans, pubmed-meshheading:19344712-Matrix Metalloproteinase 1, pubmed-meshheading:19344712-Matrix Metalloproteinase 2, pubmed-meshheading:19344712-Middle Aged, pubmed-meshheading:19344712-Mitogen-Activated Protein Kinases, pubmed-meshheading:19344712-NF-kappa B, pubmed-meshheading:19344712-Phosphorylation, pubmed-meshheading:19344712-Transforming Growth Factor beta1, pubmed-meshheading:19344712-Tumor Necrosis Factors, pubmed-meshheading:19344712-Wound Healing
pubmed:year
2009
pubmed:articleTitle
Expression and function of fibroblast growth factor-inducible 14 in human corneal myofibroblasts.
pubmed:affiliation
Department of Ophthalmology, Juntendo University School of Medicine, Tokyo 113-8431, Japan. ebihara@juntendo.ac.jp
pubmed:publicationType
Journal Article