Matrix Metalloproteinases: The Clue to Intervertebral Disc Degeneration?
- 1 July 1998
- journal article
- review article
- Published by Wolters Kluwer Health in Spine
- Vol. 23 (14) , 1612-1626
- https://doi.org/10.1097/00007632-199807150-00021
Abstract
A review of the current literature on the role of matrix metalloproteinases in intervertebral disc degeneration. To detail the characteristics of matrix metalloproteinases (classification, structure, substrate specificity and regulation) and to report previous studies of intervertebral discs. Degeneration of the intervertebral disc, a probable prerequisite to disc herniation, is a complex phenomenon, and its physiopathologic course remains unclear. Matrix metalloproteinases probably play an important role but have received sparse attention in the literature. A systematic review of studies reporting a role of matrix metalloproteinases in intervertebral disc degeneration. In several studies, investigators have reported the presence of proteolytic enzymes from disc culture systems and disc tissue extracts in degenerated human intervertebral discs, especially collagenase-1 (MMP-1) and stromelysin-1 (MMP-3). The matrix metalloproteinases are regulated by specific inhibitors (tissue inhibitors of metalloproteinases, or TIMPS), cytokines (interleukin-1), and growth factors. This field of application is of particular interest because conventional treatments are disappointing in chronic low back pain. Clinical trials with specific inhibitors of metalloproteinases are beginning in osteoarthritis.Keywords
This publication has 135 references indexed in Scilit:
- The new collagenase, collagenase-3, is expressed and synthesized by human chondrocytes but not by synoviocytes. A role in osteoarthritis.Journal of Clinical Investigation, 1996
- Cloning, expression, and type II collagenolytic activity of matrix metalloproteinase-13 from human osteoarthritic cartilage.Journal of Clinical Investigation, 1996
- Assignment of the Human Membrane-Type Matrix Metalloproteinase (MMP14) Gene to 14q11-q12 by in Situ HybridizationGenomics, 1995
- Inhibition of interleukin-1 (IL-1) induced neutral proteases from rabbit articular chondrocytes by WY-46,135 and WY-48,989Inflammation Research, 1991
- The complex between a tissue inhibitor of metalloproteinases (TIMP‐2) and 72‐kDa progelatinase is a metalloproteinase inhibitorEuropean Journal of Biochemistry, 1991
- Imbalance between the mechanisms of activation and inhibition of metalloproteases in the early lesions of experimental osteoarthritisArthritis & Rheumatism, 1990
- Evidence for metalloproteinase and metalloproteinase inhibitor imbalance in human osteoarthritic cartilage.Journal of Clinical Investigation, 1989
- Inactivation of tissue inhibitor of metalloproteinases by neutrophil elastase and other serine proteinasesFEBS Letters, 1988
- Endogenous Activation of Latent Collagenase by Rheumatoid Synovial CellsNew England Journal of Medicine, 1977
- Characterization of Collagen and Its Precursors Synthesized by Rabbit‐Articular‐Cartilage Cells in Various Culture SystemsEuropean Journal of Biochemistry, 1976