Cell biology of osteoarthritis: The chondrocyte’s response to injury

被引:63
作者
Fukui N. [1 ]
Purple C.R. [1 ]
Sandell L.J. [1 ]
机构
[1] Department of Orthopaedic Surgery, Washington University School of Medicine, Barnes-Jewish Hospital, Mail Stop 90-34-674, 216 South Kingshighway, St. Louis, 63110, MO
关键词
Articular Cartilage; Articular Chondrocytes; Cartilage Oligomeric Matrix Protein; Nitric Oxide; Osteoarthritis Cartilage;
D O I
10.1007/s11926-001-0064-8
中图分类号
学科分类号
摘要
Cartilage is comprised of a large amount of functional extracellular matrix that is made and maintained by a small number of chondrocytes, the sole resident cell type. Normal cartilage exists in a relatively steady state: that is, the anabolic processes (those that result in the synthesis of cartilage matrix components) are in equilibrium with the catabolic processes (those that result in the normal turnover of matrix molecules). If the functional extracellular matrix is disturbed by physical or molecular means, the cells respond in an attempt to repair the matrix. This stimulated activity does not result in repair due to the extent and complexity of the extracellular matrix. Eventually, the newly synthesized and activated catabolic enzymes degrade the matrix components. This review presents the cellular and molecular mechanisms that account for this activity and provides some possible solutions. © 2001, Current Science Inc.
引用
收藏
页码:496 / 505
页数:9
相关论文
共 72 条
[1]  
Sandell L.J., Aigner T., Articular cartilage and changes in arthritis. An introduction: cell biology of osteoarthritis, Arthritis Res, 3, pp. 107-113, (2001)
[2]  
Aigner T., Zhu Y., Chansky H.H., Et al., Reexpression of type IIA procollagen by adult articular chondrocytes in osteoarthritic cartilage, Arthritis Rheum, 42, pp. 1443-1450, (1999)
[3]  
Salminen H., Vuorio E., Saamanen A.M., Expression of Sox9 and type IIA procollagen during attempted repair of articular cartilage damage in a transgenic mouse model of osteoarthritis, Arthritis Rheum, 44, pp. 947-955, (2001)
[4]  
Boos N., Nerlich A.G., Wiest I., Et al., Immunohistochemical analysis of type-X-collagen expression in osteoarthritis of the hip joint, J Orthop Res, 17, pp. 495-502, (1999)
[5]  
van Meurs J.B., van Lent P.L., Holthuysen A.E., Et al., Kinetics of aggrecanase-and metalloproteinase-induced neoepitopes in various stages of cartilage destruction in murine arthritis, Arthritis Rheum, 42, pp. 1128-1139, (1999)
[6]  
Tortorella M.D., Burn T.C., Pratta M.A., Et al., Purification and cloning of aggrecanase-1: a member of the ADAMTS family of proteins, Science, 284, pp. 1664-1666, (1999)
[7]  
Abbaszade I., Liu R.Q., Yang F., Et al., Cloning and characterization of ADAMTS11, and aggrecanase from the ADAMTS family, J Biol Chem, 274, pp. 318-322, (1999)
[8]  
Flannery C.R., Little C.B., Hughes C.E., Caterson B., Expression of ADAMTS homologues in articular cartilage, Biochem Biophys Res Commun, 260, pp. 318-322, (1999)
[9]  
Sandy J.D., Verscharen C., Analysis of aggrecan in human knee cartilage and synovial fluid indicates that aggrecanase (ADAMTS) activity is responsible for the catabolic turnover and loss of whole aggrecan whereas other protease activity is required for C-terminal processing in vivo, Biochem J, 358, pp. 615-626, (2001)
[10]  
Moos V., Fickert S., Muller B., Weber U., Sieper J., Immunohistological analysis of cytokine expression in human osteoarthritic and healthy cartilage, J Rheumatol, 26, pp. 870-879, (1999)