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Rheumatology 2003; 42: 336-342
© 2003 British Society for Rheumatology

The G1 domain of aggrecan released from porcine articular cartilage forms stable complexes with hyaluronan/link protein

T. Yasumoto2, J. L. E. Bird2, K. Sugimoto3, R. M. Mason1 and M. T. Bayliss2,

1 Molecular Pathology Section, Division of Biomedical Sciences, Imperial College School of Medicine, South Kensington, London SW7 2AZ,
2 Royal Veterinary College, Royal College Street, London NW1 0TU, UK and
3 Sankyo Co., Ltd, Tokyo, Japan

Objective. To raise peptide antibodies recognizing the C-terminal amino acid sequence in the G1 domain of porcine aggrecan, generated by the action of either aggrecanase or neutral metalloproteinase(s), in rabbits and to use them to investigate the release of aggrecan from porcine articular cartilage.

Method. An explant culture system was used to investigate the release of the G1 domain of aggrecan from porcine articular cartilage treated with retinoic acid or interleukin 1ß and to study how the activity of these agents is modified by the proteinase inhibitor, batimastat (BB94).

Results. Retinoic acid and interleukin 1ß induced both enzyme activities and the release of the G1 domain into the culture medium. Proteinase activity was significantly reduced when the tissue was incubated in the presence of BB94. The functional properties of the enzyme-generated G1 domain were studied using large-pore, agarose/polyacrylamide gel electrophoresis, and it was shown to interact with hyaluronan and link protein.

Conclusions. The results show that there must be a mechanism for removing a functional G1 domain from aggrecan during tissue turnover using this culture system.

KEY WORDS: Cartilage, Aggrecanase, Metalloproteinase, Aggrecan, Neo-epitopes.

Correspondence to: R. M. Mason, Imperial College, South Kensington, London SW7 2AZ, UK. E-mail: roger.mason{at}imperial.ac.uk


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