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Structural role of osteocalcin and its modification in bone fracture
Stacyann Bailey, Atharva A Poundarik, Grazyna E Sroga1
1Department of Biomedical Engineering, Shirley Ann Jackson PhD Center for Biotechnology and Interdisciplinary Studies, Rensselaer Polytechnic Institute, Troy, New York 12180, USA.
Applied Physics Reviews
|March 14, 2023
Summary
Glycation of osteocalcin (OC), a bone protein, forms advanced glycation end-products (AGEs) like pentosidine. This modification significantly reduces bone fracture toughness and energy dissipation, impacting skeletal health.
Area of Science:
- Biochemistry
- Biomaterials Science
- Orthopedics
Background:
- Osteocalcin (OC) is crucial for bone's biological and mechanical functions.
- OC undergoes post-translational modifications, including glycation, but its effect on bone fracture resistance is unknown.
Purpose of the Study:
- To investigate the impact of osteocalcin glycation on bone's resistance to fracture.
- To analyze the formation of advanced glycation end-products (AGEs) on osteocalcin.
- To develop a model explaining glycation's effect on bone mechanics.
Main Methods:
- Ultra-performance liquid chromatography (UPLC) to detect pentosidine cross-links on mouse OC.
- In vitro glycation of bone samples from wild-type and osteocalcin-deficient mice.
- Measurement of fluorescent AGEs and fracture toughness in glycated and control bone samples.
Main Results:
- Glycation significantly increased AGEs in wild-type mouse bones compared to osteocalcin-deficient bones.
- Glycation led to a significant decrease in fracture toughness in wild-type mouse bones.
- A molecular model indicated a 37%-90% loss in OC's energy dissipation due to pentosidine cross-linking.
Conclusions:
- Glycation of osteocalcin, forming pentosidine cross-links, negatively impacts bone fracture toughness.
- These findings highlight the role of OC modification in bone fragility.
- Understanding these mechanisms may lead to new therapeutic strategies for skeletal health.
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