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Aggrecanases are considered to play a key role in the destruction of articular cartilage during the progression of arthritis. Here we report that the N-terminal inhibitory domain of tissue inhibitor of metalloproteinases 3 (N-TIMP-3), but not TIMP-1 or TIMP-2, inhibits glycosaminoglycan release from bovine nasal and porcine articular cartilage explants stimulated with interleukin-1alpha or retinoic acid in a dose-dependent manner. This inhibition is due to the blocking of aggrecanase activity induced by the catabolic factors. Little apoptosis of primary porcine chondrocytes is observed at an effective concentration of N-TIMP-3. These results suggest that TIMP-3 may be a candidate agent for use against cartilage degradation.

Original publication

DOI

10.1016/s0014-5793(03)01295-x

Type

Journal article

Journal

FEBS letters

Publication Date

12/2003

Volume

555

Pages

431 - 436

Addresses

Kennedy Institute of Rheumatology Division, Imperial College London, 1 Aspenlea Road, W6 8LH, London, UK.

Keywords

Cartilage, Articular, Cell Line, Chondrocytes, Animals, Cattle, Swine, Humans, Tretinoin, Endopeptidases, Glycosaminoglycans, Proteoglycans, Lectins, C-Type, Recombinant Proteins, Extracellular Matrix Proteins, Tissue Inhibitor of Metalloproteinase-3, Interleukin-1, Protease Inhibitors, Culture Techniques, Apoptosis, Protein Structure, Tertiary, Aggrecans