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Lysine Hydroxylation and Cross-Linking of Collagen

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Post-Translational Modification of Proteins

Part of the book series: Methods in Molecular Biology ((MIMB,volume 1934))

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Abstract

Collagens represent a large family of structurally related proteins containing a unique triple-helical structure. Among them, the fibril-forming collagens are the most abundant in vertebrates providing tissues with form and stability. One of the characteristics of the fibrillar collagens is its sequential posttranslational modifications of specific lysine residues that have major effects on molecular assembly and stability of the fibrils in the extracellular space. Hydroxylation of lysine residues is the first modification catalyzed by lysyl hydroxylases, and is critical for the following glycosylation and in determining the fate of covalent cross-linking. This chapter presents an overview of lysine hydroxylation and cross-linking of collagen, and the analytical methods we have developed.

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Acknowledgments

This study was originally supported by NIH grants DE10489 and AR052824 and NASA grant NAG2-1596.

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Authors and Affiliations

  1. Department of Oral and Craniofacial Health Sciences, School of Dentistry, University of North Carolina, Chapel Hill, NC, USA

    Mitsuo Yamauchi & Masahiko Terajima

  2. Department of Oral Science, Graduate School of Medicine, Chiba University, Chiba, Japan

    Masashi Shiiba

Authors
  1. Mitsuo Yamauchi
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  2. Masahiko Terajima
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  3. Masashi Shiiba
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Corresponding author

Correspondence to Mitsuo Yamauchi .

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Editors and Affiliations

  1. Recombinant Research and Development, Octapharma Biopharmaceuticals GmbH, Heidelberg, Germany

    Christoph Kannicht

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Yamauchi, M., Terajima, M., Shiiba, M. (2019). Lysine Hydroxylation and Cross-Linking of Collagen. In: Kannicht, C. (eds) Post-Translational Modification of Proteins. Methods in Molecular Biology, vol 1934. Humana, New York, NY. https://doi.org/10.1007/978-1-4939-9055-9_19

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  • DOI: https://doi.org/10.1007/978-1-4939-9055-9_19

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  • Publisher Name: Humana, New York, NY

  • Print ISBN: 978-1-4939-9053-5

  • Online ISBN: 978-1-4939-9055-9

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