Open Access

VIEWPOINT

Effect of non-enzymatic glycation on collagen nanoscale mechanisms in diabetic and age-related bone fragility

by JAMES L. ROSENBERG¹, WILLIAM WOOLLEY¹, IHSAN ELNUNU¹, JULIA KAMML², DAVID S. KAMMER², CLAIRE ACEVEDO^1,3,*

1 Department of Mechanical Engineering, University of Utah, Salt Lake City, 84112, USA
2 Institute for Building Materials, ETH Zurich, Zurich, Switzerland
3 Department of Biomedical Engineering, University of Utah, Salt Lake City, 84112, USA

* Corresponding Author: CLAIRE ACEVEDO. Email:

BIOCELL 2023, 47(7), 1651-1659. https://doi.org/10.32604/biocell.2023.028014

Received 26 November 2022; Accepted 20 March 2023; Issue published 21 June 2023

Abstract

Age and diabetes have long been known to induce an oxidative reaction between glucose and collagen, leading to the accumulation of advanced glycation end-products (AGEs) cross-links in collagenous tissues. More recently, AGEs content has been related to loss of bone quality, independent of bone mass, and increased fracture risk with aging and diabetes. Loss of bone quality is mostly attributed to changes in material properties, structural organization, or cellular remodeling. Though all these factors play a role in bone fragility disease, some common recurring patterns can be found between diabetic and age-related bone fragility. The main pattern we will discuss in this viewpoint is the increase of fibrillar collagen stiffness and loss of collagen-induced plasticity with AGE accumulation. This study focused on recent related experimental studies and discusses the correlation between fluorescent AGEs content at the molecular and fibrillar scales, collagen deformation mechanisms at the nanoscale, and resistance to bone fracture at the macroscale.

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