Increased AGE Cross-Linking Reduces the Mechanical Properties of Osteons.

Unlabelled: The osteon is the primary structural component of bone, contributing significantly to its unique toughness and strength. Despite extensive research on osteonal structure, the properties of osteons have not been fully investigated, particularly within the context of bone fragility diseases like type 2 diabetes mellitus (T2DM). This study aims to isolate osteons from bovine bone, simulate the effects of increased advanced glycation end-products (AGEs) in T2DM through ribosylation, and evaluate the mechanical properties of isolated osteons.

Effect of in vitro ribosylation on the dynamic fracture behavior of mature bovine cortical bone.

In this study, the fracture behavior of ribosylated bovine cortical bone is investigated under loading conditions simulating a fall event. Single edge notched specimens, separated into a control group (n = 11) and a ribosylated group (n = 8), were extracted from the mid-diaphysis of a single bovine femur harvested from a mature cow. A seven-day ribosylation process results in the accumulation of Advanced-Glycation End Products (AGEs) cross-links and AGE adducts.

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

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.