Biochemical evidence for altered subchondral bone collagen metabolism in osteoarthritis of the hip.

Osteoarthritis (OA) of the hip is invariably viewed as a disease primarily affecting the articular cartilage. Data presented in this report, however, demonstrate changes in the metabolic activity of the underlying trabecular bone tissue, the processes of which may represent a significant factor in the pathogenesis of hip OA. Trabecular bone tissue from OA subjects expressed significantly more matrix metalloproteinase (MMP)-2 (gelatinase A, 72 kDa type IV collagenase) when compared to age-matched osteoporotic (OP) and normal bone tissue. Alkaline phosphatase was also significantly elevated in OA bone tissue. The combination of increased MMP-2 and alkaline phosphatase indicates heightened collagen turnover in the subchondral bone compartment of osteoarthritic hips. The data obtained from this study warrant a closer investigation into the significance of these changes in OA and emphasize the multifactorial elements of the whole joint in the whole joint in the overall disease process.

[1]  R. Loeser,et al.  Osteoarthritis in cynomolgus macaques: A primate model of naturally occurring disease , 1994, Journal of orthopaedic research : official publication of the Orthopaedic Research Society.

[2]  L. W. Plewes Osteo‐arthritis of the hip , 1940 .

[3]  J. Clohisy,et al.  Parathyroid hormone induces transcription of collagenase in rat osteoblastic cells by a mechanism using cyclic adenosine 3',5'-monophosphate and requiring protein synthesis. , 1992, Molecular endocrinology.

[4]  M. Seibel,et al.  Urinary hydroxy-pyridinium crosslinks provide indices of cartilage and bone involvement in arthritic diseases. , 1989, The Journal of rheumatology.

[5]  L E Lanyon,et al.  Direct transformation from quiescence to bone formation in the adult periosteum following a single brief period of bone loading , 1988, Journal of bone and mineral research : the official journal of the American Society for Bone and Mineral Research.

[6]  U. K. Laemmli,et al.  Cleavage of structural proteins during , 1970 .

[7]  James P. Quigley,et al.  Matrix Metalloproteinase-2 Is an Interstitial Collagenase , 1995, The Journal of Biological Chemistry.

[8]  J. Reynolds,et al.  Mouse osteoblasts synthesize collagenase in response to bone resorbing agents. , 1984, Biochimica et biophysica acta.

[9]  L. Avioli,et al.  Expression of metalloproteinases and tissue inhibitors of metalloproteinases in human osteoblast-like cells: differentiation is associated with repression of metalloproteinase biosynthesis. , 1994, Endocrinology.

[10]  R. Baron,et al.  (Pro)collagenase (matrix metalloproteinase-1) is present in rodent osteoclasts and in the underlying bone-resorbing compartment. , 1993, Journal of cell science.

[11]  P Young,et al.  Prediction of the progression of joint space narrowing in osteoarthritis of the knee by bone scintigraphy. , 1993, Annals of the rheumatic diseases.

[12]  J. Kalinowski,et al.  Production of both 92- and 72-kDa gelatinases by bone cells. , 1992, Matrix.

[13]  N. Forest,et al.  Microcinematographic and autoradiographic kinetic studies of bone cell differentiation in vitro: matrix formation and mineralization. , 1989, Bone.

[14]  J. Quigley,et al.  Matrix metalloproteinase-2 is an interstitial collagenase. Inhibitor-free enzyme catalyzes the cleavage of collagen fibrils and soluble native type I collagen generating the specific 3/4- and 1/4-length fragments. , 1995, The Journal of biological chemistry.

[15]  R. Rose,et al.  The role of bone changes in the degeneration of articular cartilage in osteoarthrosis. , 1978, Acta orthopaedica Belgica.

[16]  J. Delaisse,et al.  Direct extraction and assay of bone tissue collagenase and its relation to parathyroid-hormone-induced bone resorption. , 1986, The Biochemical journal.

[17]  A. Bailey,et al.  The Continuous Elongation Technique for Severe Dupuytren’s Disease , 1994, Journal of hand surgery.

[18]  R. Hembry,et al.  The effects of selective inhibitors of matrix metalloproteinases (MMPs) on bone resorption and the identification of MMPs and TIMP-1 in isolated osteoclasts. , 1994, Journal of cell science.