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Fig. 1 Seven cross-linking sites (lysines) have been identified in the mammalian type IX collagen molecule, which consists of three triple-helical segments interrupted by and ending in four non-collagen-helical sequences (NC1 to NC4 going from right to left in this figure). The chondroitin sulphate (CS) chain shown attached to NC3 is found on type IX collagen from some sources but not from articular cartilage (Diab et al., 1996).
Fig. 2 The collagen II/IX/XI heterofibril. (a) An interaction model between surface collagen IX molecules and the collagen II polymer that can accommodate all known IX-to-IX and IX-to-II cross-links and potential interfibrillar cross-links. (b) Known and speculated sites of peptide bond cleavage in the heteropolymer required for degradation and/or lateral growth of fibrils
Fig. 3 Immunochemical localization of type II collagen in an intact articular cartilage region from the knee joint of a 59 yr old female with familial OA. mAb 4G9 specifically sees the N-propeptide of collagen type III, which is concentrated in the surface
Fig. 4 SDS-PAGE/Western blot analysis of type III collagen from mature human and bovine (5-yr cow) articular cartilage using a type II collagen C-telopeptide-specific antibody (10F2). mAb 10F2 recognizes a pepsin-generated neoepitope in the cleaved C-telopeptide from type II collagen linked to an a1(III) chain.zone and around chondrocytes at depth.
Fig. 5 Isolation and preliminary identification of a cross-linked peptide from a site of interaction between type III collagen and type II collagen from bovine articular cartilage. The collagen III N-telopeptide is linked to the residue 930 site in type II collagen by a divalent lysyl oxidase pathway cross-link.
Fig. 6 Mass spectral confirmation of the structure of the collagen II-III cross-linked peptide after further proteolysis by bacterial collagenase.
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