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. 2007 Feb 7:1:61-76.

Collagen biomarkers for arthritis applications

Affiliations

Collagen biomarkers for arthritis applications

James D Birmingham et al. Biomark Insights. .
No abstract available

Keywords: ankylosing spondylitis; biomarkers; osteoarthritis; rheumatoid arthritis; type II collagen.

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Figures

Figure 1a
Figure 1a
Amino acid sequence in α1(II) chain of human procollagen type IIB (COL2A1_HUMAN, P02458, UniProtKB/Swiss). Numbering of amino acids in this figure (and throughout the whole text of this review) is consistent with numbering in the source given above and may not correspond to numbering in a particular reference. Numbering used here includes N-terminal signal peptide and N-propeptide, and does not include the alternatively spliced block of 69 amino acids in the N-propeptide (which is shown in Figure 1b). Each number corresponds to the last one of ten amino acids under it. - Tandems Proline/Hydroxyproline and Lysine/Hydroxylysine are not distinguished and are represented by the same letter (P and K, respectively). - Positions of cross-links are color-coded and underlined (K121, 239, 1061, and 1162). - The telopeptides (in red lettering) and epitopes discussed in this review is as follows: 113–131 N-terminal non-helical domain (N-terminal telopeptide) 1146–1172 C-terminal non-helical domain (C-terminal telopeptide) 132–1145 Triple-helical domain 1173–1418 Carboxy-terminal propeptide domain 26–112 Amino-terminal propeptide domain
Figure 1b
Figure 1b
Amino acid sequence of α1(II) chain of human procollagen type IIA (UniProtKB/TrEMBL entry Q14047) 29–97 The alternatively spliced 69 amino acids of the amino-terminal propeptide domain.
Figure 2
Figure 2
The sequence of the cross-linked Col2CTx epitope. The crosslinked structure of this telopeptide biomarker, indicative of type II collagen degradation, enables it to survive to urine. The cross-link designated as Hyl-Hyl-Hyl is hydroxylysylpyridinoline.

References

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