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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Kwak, Ji-sun Chun, Churl-hong Won, Yoonkyung Lee, Minju Kim, Jin-hong Lee, Gyuseok Chun, Jang-soo |
| Description | Author Affiliation: Kim JH ( School of Life Sciences, Cell Dynamics and Integrative Aging Research Centers, Gwangju Institute of Science and Technology, Gwangju 500-712, Korea); Lee G ( School of Life Sciences, Cell Dynamics and Integrative Aging Research Centers, Gwangju Institute of Science and Technology, Gwangju 500-712, Korea); Won Y ( School of Life Sciences, Cell Dynamics and Integrative Aging Research Centers, Gwangju Institute of Science and Technology, Gwangju 500-712, Korea); Lee M ( School of Life Sciences, Cell Dynamics and Integrative Aging Research Centers, Gwangju Institute of Science and Technology, Gwangju 500-712, Korea); Kwak JS ( School of Life Sciences, Cell Dynamics and Integrative Aging Research Centers, Gwangju Institute of Science and Technology, Gwangju 500-712, Korea); Chun CH ( Department of Orthopedic Surgery, Wonkwang University School of Medicine, Iksan 570-711, Korea.); Chun JS ( School of Life Sciences, Cell Dynamics and Integrative Aging Research Centers, Gwangju Institute of Science and Technology, Gwangju 500-712, Korea); |
| Abstract | Osteoarthritis (OA) is characterized by impairment of the load-bearing function of articular cartilage. OA cartilage matrix undergoes extensive biophysical remodeling characterized by decreased compliance. In this study, we elucidate the mechanistic origin of matrix remodeling and the downstream mechanotransduction pathway and further demonstrate an active role of this mechanism in OA pathogenesis. Aging and mechanical stress, the two major risk factors of OA, promote cartilage matrix stiffening through the accumulation of advanced glycation end-products and up-regulation of the collagen cross-linking enzyme lysyl oxidase, respectively. Increasing matrix stiffness substantially disrupts the homeostatic balance between chondrocyte catabolism and anabolism via the Rho-Rho kinase-myosin light chain axis, consequently eliciting OA pathogenesis in mice. Experimental enhancement of nonenzymatic or enzymatic matrix cross-linking augments surgically induced OA pathogenesis in mice, and suppressing these events effectively inhibits OA with concomitant modulation of matrix degrading enzymes. Based on these findings, we propose a central role of matrix-mediated mechanotransduction in OA pathogenesis. |
| ISSN | 00278424 |
| e-ISSN | 10916490 |
| Journal | Proceedings of the National Academy of Sciences of the United States of America |
| Issue Number | 30 |
| Volume Number | 112 |
| Language | English |
| Publisher | National Academy of Sciences |
| Publisher Date | 2015-07-01 |
| Publisher Place | United States |
| Access Restriction | Open |
| Subject Keyword | Cartilage, Articular Pathology Mechanotransduction, Cellular Osteoarthritis Acrylic Resins Chemistry Animals Basic Helix-Loop-Helix Transcription Factors Metabolism Chondrocytes Cytology Collagen Cross-Linking Reagents Genes, Reporter Glycosylation End Products, Advanced Mice Mice, Inbred C57BL Microscopy, Fluorescence Protein-Lysine 6-Oxidase Risk Factors Signal Transduction Stress, Mechanical Research Support, Non-U.S. Gov't Multidisciplinary |
| Content Type | Text |
| Resource Type | Article |
| Subject | Multidisciplinary |
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