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Metalloproteinase production by rabbit articular cartilage: comparison of the effects of interleukin-1α in vitro and in vivo (1994)

Hembry, R. M. ; Bagga, M. R. ; Dingle, J. T. ; [et al.]

Springer

Virchows Archiv 425 (1994), S. 413-424

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ISSN: 1432-2307

Keywords: Interleukin-1 ; Metalloproteinase Collagenase ; Cartilage ; Arthritis

Source: Springer Online Journal Archives 1860-2000

Topics: Medicine

Notes: Abstract To assess the effects of interleukin-1 on intact articular cartilage in vitro, explants from young and adult rabbits were cultured with interleukin-1 and the distributions of the matrix metalloproteinases and tissue inhibitor of metalloproteinases (TIMP-1) were investigated by indirect immunofluorescence microscopy. One to 2-week-old cartilage chondrocytes synthesized collagenase in response to pure or crude interleukin-1 (monocyte conditioned medium), with subarticular cells most responsive. Collagenase synthesis was not stimulated in adult articular chondrocytes when explants were treated with either pure or crude interleukin-1. Stromelysin, gelatinase and TIMP-1 could not be demonstrated within any zone of the cartilage, indicating that their synthesis was not stimulated by either pure or crude interleukin-1. The addition of fibroblast growth factors, either alone or in combination with interleukin-1, did not modify these responses. These results contrast markedly with observations on cultured chondrocyte monolayers, where interleukin-1 treatment induces near co-ordinate expression of metalloproteinases. To assess the effects of interleukin-1 in vivo, it was injected into adult rabbit knee joint spaces and the articular cartilage subsequently analysed for evidence of altered metalloproteinase production by immunocytochemistry. No significant increase in metalloproteinase or TIMP-1 synthesis by chondrocytes was detected, although the cartilage matrix showed a marked loss of toluidine blue metachromasia. We conclude that metalloproteinases are not involved in the rapid loss of proteoglycan from cartilage matrix in these situations.

Type of Medium: Electronic Resource

URL: http://dx.doi.org/10.1007/BF00189580

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The sensitivity of synthesis of human cartilage matrix to inhibition by IL-1 suggests a mechanism for the development of osteoarthritis (1991)

Dingle, J. T. ; Horner, A. ; Shield, M.

New York, NY [u.a.] : Wiley-Blackwell

Cell Biochemistry and Function 9 (1991), S. 99-102

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ISSN: 0263-6484

Keywords: Proteoglycan synthesis ; Interleukin 1 ; human articular cartilage ; Chemistry ; Biochemistry and Biotechnology

Source: Wiley InterScience Backfile Collection 1832-2000

Topics: Biology , Medicine

Notes: The damage to articular cartilage, characteristic of arthritic disease, is usually ascribed to increased degradative activity by enzymes or free radicals from locally activated cells.1-3 We propose that inhibition of matrix synthesis, and consequential impairment of the natural repair process, may be at least as important in chronic joint disease.

Additional Material: 1 Ill.