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Role of heat shock protein 47 in transdifferentiation of human tenon's fibroblasts to myofibroblasts.

Authors
 Samin Hong ; Kyoungsoo Park ; Gong Je Seong ; Jong Bok Lee ; Sueng-Han Han ; Jin Hyoung Kim 
Citation
 BMC Ophthalmology, Vol.12 : 49, 2012 
Journal Title
 BMC Ophthalmology 
ISSN
 1471-2415 
Issue Date
2012
Abstract
BACKGROUND: Heat shock protein 47 (Hsp47) is a well-known molecular chaperone in collagen synthesis and maturation. The aim of this study is to investigate its putative role in the transdifferentiation of Tenon's fibroblasts to myofibroblasts. METHODS: Primary cultured human Tenon's fibroblasts were exposed to transforming growth factor-β1 (TGF-β1) for up to 48 hours. The mRNA levels of Hsp47 and α smooth muscle actin (αSMA) were determined by quantitative real time RT-PCR. After delivery of small interfering RNA (siRNA) molecules targeting Hsp47 into the cells, the expression of Hsp47 and αSMA proteins was determined by western immunoblotting. RESULTS: TGF-β1 increased the mRNA expressions of both Hsp47 and αSMA in human Tenon's fibroblasts, as determined by quantitative real time RT-PCR. However, it induced the protein expression of only αSMA but not Hsp47, as determined by western immunoblots. When siRNAs specific for Hsp47 were introduced into those cells, the TGF-β1-induced expression of αSMA was significantly attenuated on western immunoblots; after 48 hours of exposure to TGF-β1, the relative densities of immunobands were 11.58 for the TGF-β1 only group and 2.75 for the siRNA treatment group, compared with the no treatment control group (p < 0.001). CONCLUSIONS: Our data suggest that Hsp47 may be related to the TGF-β1-induced transdifferentiation of human Tenon's fibroblasts to myofibroblasts.
URI
http://ir.ymlib.yonsei.ac.kr/handle/22282913/89795
DOI
10.1186/1471-2415-12-49
Appears in Collections:
1. 연구논문 > 1. College of Medicine > Dept. of Pharmacology
1. 연구논문 > 1. College of Medicine > Dept. of Ophthalmology
Yonsei Authors
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