Structural role of osteocalcin and its modification in bone fracture.
Journal
Applied physics reviews
ISSN: 1931-9401
Titre abrégé: Appl Phys Rev
Pays: United States
ID NLM: 101634369
Informations de publication
Date de publication:
Mar 2023
Mar 2023
Historique:
received:
13
06
2022
accepted:
10
02
2023
pmc-release:
10
03
2024
entrez:
14
3
2023
pubmed:
15
3
2023
medline:
15
3
2023
Statut:
ppublish
Résumé
Osteocalcin (OC), an abundant non-collagenous protein in bone extracellular matrix, plays a vital role in both its biological and mechanical function. OC undergoes post-translational modification, such as glycation; however, it remains unknown whether glycation of OC affects bone's resistance to fracture. Here, for the first time, we demonstrate the formation of pentosidine, an advanced glycation end-product (AGE) cross-link on mouse OC analyzed by ultra-performance liquid chromatography. Next, we establish that the presence of OC in mouse bone matrix is associated with lower interlamellar separation (distance) and thicker bridges spanning the lamellae, both of which are critical for maintaining bone's structural integrity. Furthermore, to determine the impact of modification of OC by glycation on bone toughness, we glycated bone samples
Identifiants
pubmed: 36915902
doi: 10.1063/5.0102897
pii: 5.0102897
pmc: PMC9999293
doi:
Types de publication
Journal Article
Langues
eng
Pagination
011410Subventions
Organisme : NIAMS NIH HHS
ID : R01 AR049635
Pays : United States
Informations de copyright
© 2023 Author(s).
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