Relaxin Modulates the Expression of MMPs and TIMPs in Fibroblasts of Patients with Carpal Tunnel Syndrome.
10.3349/ymj.2017.58.2.415
- Author:
Young Mi KANG
1
;
Hwan Mo LEE
;
Seong Hwan MOON
;
Ho KANG
;
Yun Rak CHOI
Author Information
1. BK21 PLUS Project for Medical Science, Yonsei University College of Medicine, Seoul, Korea.
- Publication Type:Original Article
- Keywords:
Carpal tunnel syndrome;
relaxin;
subsynovial connective tissue;
matrix metalloproteinases;
collagens
- MeSH:
Actins;
Carpal Tunnel Syndrome*;
Collagen;
Connective Tissue;
Extracellular Matrix;
Fibroblasts*;
Fibronectins;
Gene Expression;
Humans;
In Vitro Techniques;
Matrix Metalloproteinases*;
Phosphorylation;
Relaxin*;
Tissue Inhibitor of Metalloproteinases;
Transforming Growth Factor beta
- From:Yonsei Medical Journal
2017;58(2):415-422
- CountryRepublic of Korea
- Language:English
-
Abstract:
PURPOSE: The aim of this study was to investigate the anti-fibrotic effect of relaxin in subsynovial fibroblasts activated by transforming growth factor beta (TGF-β). MATERIALS AND METHODS: To test the anti-fibrotic effect of an adenovirus-relaxin construct (Ad-RLN) on subsynovial fibroblasts in vitro, cells from subsynovial connective tissue of patients with carpal tunnel syndrome were activated with TGF-β1 and exposed to Ad-RLN (as a therapeutic gene) or adenovirus-lacZ construct (as a marker gene) for four hours. Subsynovial fibroblast cultures without adenoviral exposure served as controls. RESULTS: We observed induction of gene expressions of collagen I, III and IV, as well as the abatement of alpha-smooth muscle actin (a-SMA) synthesis, Smad2 phosphorylation, and fibronectin at the protein level, in comparison to controls. In addition, protein expressions of matrix metalloproteinase (MMP) I was significantly induced, whereas the protein expressions of tissue inhibitor of metalloproteinases (TIMP) I and IV were reduced due to relaxin expression. CONCLUSION: RLN prevents excessive synthesis of extracellular matrix by reducing the expressions of its components, such as fibronectin, a-SMA, and phosphorylated Smad2, by increasing the expression of MMPs; and by decreasing the expression of TIMPs.
