Biol. Chem. Hoppe-Seyler Vol. 374, pp. 497-500, July 1993 Vladimir PODRAZKY, Jitka STOVI'CKOV , Jana NOVOTN and KarelTRNAVSKY Institute of Rheumatology, Prague, Czech Republic (Received 20 April / 28 May 1993) Summary: Bovine intervertebral disc- and articular cartilage extracts contain a metalloproteinase system capable of degrading type XI collagen. The collagendegrading activity is rather low in unmodified extracts but increases considerably on metalloproteinase activation. The similartiy between intervertebral disc and articular cartilage in their patterns of (casein-degrading) metalloproteinases and type XI and type II collagen degradation is believed to suggest a similarity in the events underlying the degradative disorders of articular cartilage and intervertebral disc. Key terms: Intervertebral disc, articular cartilage, type XI collagen, collagen-degrading activity. The matrix of cartilage contains a variety of fibrillar and amorphous macromolecular substances. The most abundant fibrillar component is collagen type II which forms a three-dimensional network of fibers thought to be responsible for the mechanical strength of cartilage. Apart from this major collagen type, several other collagens participate in the cartilage matrix structure. Of special interest is type XI collagen described originally as la, 2a, 3a collagen111. Type XI collagen resembles type II collagen in that it is a fiberforming collagen
Biological Chemistry Hoppe-Seyler – de Gruyter
Published: Jan 1, 1993
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