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Lysine post-translational modifications of collagen

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Yamauchi, Mitsuo, Sricholpech, Marnisa·2012·Essays in Biochemistry
DOI 10.1042/bse0520113
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Abstract

Type I collagen is the most abundant structural protein in vertebrates. It is a heterotrimeric molecule composed of two α1 chains and one α2 chain, forming a long uninterrupted triple helical structure with short non-triple helical telopeptides at both the N- and C-termini. During biosynthesis, collagen acquires a number of post-translational modifications, including lysine modifications, that are critical to the structure and biological functions of this protein. Lysine modifications of collagen are highly complicated sequential processes catalysed by several groups of enzymes leading to the final step of biosynthesis, covalent intermolecular cross-linking. In the cell, specific lysine residues are hydroxylated to form hydroxylysine. Then specific hydroxylysine residues located in the helical domain of the molecule are glycosylated by the addition of galactose or glucose-galactose. Outside the cell, lysine and hydroxylysine residues in the N- and C-telopeptides can be oxidatively deaminated to produce reactive aldehydes that undergo a series of non-enzymatic condensation reactions to form covalent intra- and inter-molecular cross-links. Owing to the recent advances in molecular and cellular biology, and analytical technologies, the biological significance and molecular mechanisms of these modifications have been gradually elucidated. This chapter provides an overview on these enzymatic lysine modifications and subsequent cross-linking.

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Metadata

Authors
Yamauchi, M., & Sricholpech, M.
Venue
Essays in Biochemistry
Publisher
Portland Press Ltd.
Published
2012-05-25
Volume
52
Pages
113-133
ISSN
  • 0071-1365 (ISSN-L)
  • 1744-1358
DOI
10.1042/bse0520113
OpenAlex
W1978262131
Cited by
626
References
4
FWCI
6.85
Type
journal article
Language
en
Open access
green

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