1. Cyclosporine A inhibits TGF-β2-induced myofibroblasts of primary cultured human pterygium fibroblasts
- Author
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Gum, Sang Il, Kim, Yeoun-Hee, Jung, Jae-Chang, Kim, Im Gyu, Lee, Jun Seok, Lee, Kyoo Won, and Park, Young Jeung
- Subjects
Male ,0301 basic medicine ,Oligonucleotides ,Biophysics ,Inflammation ,Pterygium ,Biochemistry ,Transforming Growth Factor beta2 ,03 medical and health sciences ,0302 clinical medicine ,Downregulation and upregulation ,Laminin ,Humans ,Medicine ,Myofibroblasts ,Molecular Biology ,Cells, Cultured ,Messenger RNA ,biology ,business.industry ,Cell Differentiation ,Muscle, Smooth ,Cell Biology ,Fibroblasts ,Actins ,eye diseases ,Fibronectins ,Fibronectin ,030104 developmental biology ,Microscopy, Fluorescence ,Immunology ,Cyclosporine ,030221 ophthalmology & optometry ,Cancer research ,biology.protein ,Female ,sense organs ,medicine.symptom ,business ,Myofibroblast ,Immunosuppressive Agents ,Software ,Intracellular ,Signal Transduction ,Transforming growth factor - Abstract
Cyclosporine A (CsA), an immunomodulatory drug, and is increasingly used to treat moderate dry eye syndrome and ocular surface inflammation. However, any inhibitory effect on differentiation of fibroblasts to myofibroblasts remains unclear. Here, we show that the inhibitory effect of CsA on transforming growth factor-beta2 (TGF-β2)-induced myofibroblasts in primary cultured human pterygium fibroblasts. CsA significantly decreased mRNA and protein expression of myofibroblast-related markers including α-SMA, laminin, and fibronectin. These findings were supported by the results from immunofluorescence staining. Taken together, these results indicate the therapeutic potential of CsA against pterygium progression. Further studies are necessary to elucidate the precise intracellular signal mechanism responsible for CsA-induced downregulation of myofibroblast markers in pterygium fibroblasts.
- Published
- 2017