On the Role of the Glycosylation of Type I Collagen in Bone.

Advanced glycation end-products Collagen Glycation Glycosylation Hydration Mineralization

Journal

Journal of structural biology
ISSN: 1095-8657
Titre abrégé: J Struct Biol
Pays: United States
ID NLM: 9011206

Informations de publication

Date de publication:
22 Oct 2024
Historique:
medline: 25 10 2024
pubmed: 25 10 2024
entrez: 24 10 2024
Statut: aheadofprint

Résumé

Glycan-protein interactions play a crucial role in biology, providing additional functions capable of inducing biochemical and cellular responses. In the extracellular matrix of bone, this type of interactions is ubiquitous. During the synthesis of the collagen molecule, glycans are post-translationally added to specific lysine residues through an enzymatically catalysed hydroxylation and subsequent glycosylation. During and after fibril assembly, proteoglycans are essential for maintaining tissue structure, porosity, and integrity. Glycosaminoglycans (GAGs), the carbohydrate chains attached to interstitial proteoglycans, are known to be involved in mineralization. They can attract and retain water, which is critical for the mechanical properties of bone. In addition, like other long-lived proteins, collagen is susceptible to glycation. Prolonged exposure of the amine group to glucose eventually leads to the formation of advanced glycation end-products (AGEs). Changes in the degree of glycosylation and glycation have been identified in bone pathologies such as osteogenesis imperfecta and diabetes and appear to be associated with a reduction in bone quality. However, how these changes affect mineralisation is not well understood. Based on the literature review, we hypothesize that the covalently attached carbohydrates may have a water-attracting function similar to that of GAGs, but at different lengths and timescales in the bone formation process. Glycosylation potentially increases the hydration around the collagen triple helix, leading to increased mineralization (hypermineralization) after water has been replaced by mineral. Meanwhile, glycation leads to the formation of crosslinking AGEs, which are associated with a decrease in hydration levels, reducing the mechanical properties of bone.

Identifiants

pubmed: 39447940
pii: S1047-8477(24)00085-6
doi: 10.1016/j.jsb.2024.108145
pii:
doi:

Types de publication

Journal Article Review

Langues

eng

Sous-ensembles de citation

IM

Pagination

108145

Informations de copyright

Copyright © 2024. Published by Elsevier Inc.

Déclaration de conflit d'intérêts

Declaration of competing interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper.

Auteurs

Luco Rutten (L)

Electron Microscopy Center, Radboud Technology Center Microscopy, Radboud University Medical Center, Geert Grooteplein Noord 29, 6525 EZ Nijmegen, Netherlands; Department of Medical BioSciences, Research Institute for Medical Innovations, Radboud University Medical Center, Geert Grooteplein Zuid 28, 6525 GA Nijmegen, Netherlands.

Elena Macías-Sánchez (E)

Electron Microscopy Center, Radboud Technology Center Microscopy, Radboud University Medical Center, Geert Grooteplein Noord 29, 6525 EZ Nijmegen, Netherlands; Department of Medical BioSciences, Research Institute for Medical Innovations, Radboud University Medical Center, Geert Grooteplein Zuid 28, 6525 GA Nijmegen, Netherlands; Department of Stratigraphy and Palaeontolgy, University of Granada, Avenida Fuente Nueva s/n, 18071 Granada, Spain. Electronic address: elena.macias@ugr.es.

Nico Sommerdijk (N)

Electron Microscopy Center, Radboud Technology Center Microscopy, Radboud University Medical Center, Geert Grooteplein Noord 29, 6525 EZ Nijmegen, Netherlands; Department of Medical BioSciences, Research Institute for Medical Innovations, Radboud University Medical Center, Geert Grooteplein Zuid 28, 6525 GA Nijmegen, Netherlands. Electronic address: nico.sommerdijk@radboudumc.nl.

Classifications MeSH