Advances in collagen cross-link analysis.
The combined application of ion-trap mass spectrometry and peptide-specific antibodies for the isolation and structural analysis of collagen cross-linking domains is illustrated with examples of results from various types of collagen with the emphasis on bone and cartilage. We highlight the potential of such methods to advance knowledge on the importance of post-translational modifications (e.g., degrees of lysine hydroxylation and glycosylation) and preferred intermolecular binding partners for telopeptide and helical cross-linking domains in regulating cross-link type and placement.
Eyre
David R
DR
Orthopaedic Research Labs, Department of Orthopaedics & Sports Medicine, University of Washington, 1959 NE Pacific Street, Seattle, WA 98195-6500, USA. deyre@u.washington.edu
Weis
Mary Ann
MA
Wu
Jiann-Jiu
JJ
D000595:Amino Acid Sequence; D000596:Amino Acids / Q000737:chemistry; D000818:Animals; D003094:Collagen / Q000737:chemistry* / Q000378:metabolism; D024161:Collagen Type XI / Q000737:chemistry; D006031:Glycosylation; D006801:Humans; D006900:Hydroxylation; D008239:Lysine / Q000737:chemistry; D008954:Models, Biological; D008969:Molecular Sequence Data; D011499:Protein Processing, Post-Translational; D021241:Spectrometry, Mass, Electrospray Ionization
D000596:Amino Acids; D024161:Collagen Type XI; C015484:pyridinoline; D003094:Collagen; D008239:Lysine