%0 Journal Article
%T Role of Heat Shock Protein 47 in Transdifferentiation of Human Tenon's Fibroblasts to Myofibroblasts
%A Hong Samin
%A Park Kyoungsoo
%A Kim Jin
%A Han Sueng-Han
%J BMC Ophthalmology
%D 2012
%I BioMed Central
%R 10.1186/1471-2415-12-49
%X 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-¦Â1 (TGF-¦Â1) for up to 48 hours. The mRNA levels of Hsp47 and ¦Á smooth muscle actin (¦ÁSMA) 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 ¦ÁSMA proteins was determined by western immunoblotting. Results TGF-¦Â1 increased the mRNA expressions of both Hsp47 and ¦ÁSMA in human Tenon¡¯s fibroblasts, as determined by quantitative real time RT-PCR. However, it induced the protein expression of only ¦ÁSMA but not Hsp47, as determined by western immunoblots. When siRNAs specific for Hsp47 were introduced into those cells, the TGF-¦Â1-induced expression of ¦ÁSMA was significantly attenuated on western immunoblots; after 48 hours of exposure to TGF-¦Â1, the relative densities of immunobands were 11.58 for the TGF-¦Â1 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-¦Â1-induced transdifferentiation of human Tenon¡¯s fibroblasts to myofibroblasts.
%K Fibroblast
%K Fibrosis
%K Heat shock protein
%K Myofibroblast
%K Transforming growth factor-¦Â
%U http://www.biomedcentral.com/1471-2415/12/49