title: Advances in collagen cross-link analysis.
abstract: 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.
authors.affiliation: Orthopaedic Research Labs, Department of Orthopaedics & Sports Medicine, University of Washington, 1959 NE Pacific Street, Seattle, WA 98195-6500, USA. deyre@u.washington.edu
authors.forename: David R
authors.initials: DR
authors.lastname: Eyre
authors.forename: Mary Ann
authors.initials: MA
authors.lastname: Weis
authors.forename: Jiann-Jiu
authors.initials: JJ
authors.lastname: Wu
mesh_terms: 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
chemical_list: D000596:Amino Acids; D024161:Collagen Type XI; C015484:pyridinoline; D003094:Collagen; D008239:Lysine