Abstract
Fibrillar collagens represent the most abundant extracellular matrix proteins in vertebrates providing tissues and organs with form, stability, and connectivity. For such mechanical functions, the formation of covalent intermolecular cross-linking between molecules is essential. This process, the final posttranslational modification during collagen biosynthesis, is initiated by conversion of specific lysine and hydroxylysine residues to the respective aldehydes by the action of lysyl oxidases. This conversion triggers a series of condensation reactions with the juxtaposed lysine-aldehyde, lysine, hydroxylysine, and histidine residues within the same and neighboring molecules resulting in di-, tri-, and tetravalent cross-links. Elastin, another class of extracellular matrix protein, is also stabilized by the lysyl oxidase-mediated mechanism but involving only lysine residues leading to the formation of unique tetravalent cross-links. This chapter presents an overview of fibrillar collagen cross-linking, and the analytical methods for collagen and elastin cross-links we have developed.
Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
