Post-Translational Modifications in Collagen Biosynthesis
Summary
Collagen biosynthesis is orchestrated through a series of co- and post-translational modifications that transform nascent procollagen chains into robust extracellular fibres. Key among these are the hydroxylation of specific proline and lysine residues by prolyl and lysyl hydroxylases, which respectively confer thermal stability and establish sites for subsequent glycosylation. Hydroxylysines may be galactosylated and glucosylgalactosylated by dedicated glycosyltransferases, fine-tuning intermolecular cross-linking patterns that dictate fibril diameter, tensile strength and enzymatic susceptibility. Procollagen trimers further undergo proteolytic cleavage of N- and C-propeptides and the formation of covalent bonds via lysyl oxidase, culminating in insoluble collagen networks. This intricate sequence of modifications underlies tissue-specific mechanical properties and is modulated by oxygen tension, cellular chaperones and metabolic signals. Disruption of any step can give rise to connective tissue disorders, fibrotic disease and altered tumour microenvironments, highlighting the clinical relevance of these enzymatic processes for both pathology and biomaterials design.
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Post-Translational Modifications in Collagen Biosynthesis publication trend
The graph below shows the total number of articles in post-translational modifications in collagen biosynthesis across all publications each year (not limited to Nature Index journals).
Technical terms
Prolyl 4-hydroxylation: Enzymatic addition of a hydroxyl group to a proline residue, essential for collagen triple-helix stability.
Hydroxylysine O-glycosylation: Attachment of galactose or glucosylgalactose to hydroxylysine, influencing cross-link formation.
Lysyl hydroxylase: Enzyme catalysing the hydroxylation of lysine residues in procollagen.
Glycosyltransferase: Enzyme that transfers sugar moieties onto hydroxylysine residues.
Cross-linking: Formation of covalent bonds between collagen molecules, enhancing fibre strength and stability.
Triple helix: Three collagen polypeptide chains wound into a right-handed supercoil, forming the structural core of collagen.
References
- Collagen prolyl 4-hydroxylase isoenzymes I and II have sequence specificity towards different X-Pro-Gly triplets. Matrix Biology (2023).
- Identification of Regulatory Molecular “Hot Spots” for LH/PLOD Collagen Glycosyltransferase Activity. International Journal of Molecular Sciences (2023).
- Glycosylation and Cross-linking in Bone Type I Collagen*. Journal of Biological Chemistry (2014).
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