Advanced Glycation End Products, Diabetes, and Bone Strength

被引：164

作者：

Yamamoto, Masahiro ^{[1
]}

Sugimoto, Toshitsugu ^{[1
]}

机构：

[1] Shimane Univ, Internal Med 1, Fac Med, 89-1 Enya Cho, Izumo, Shimane 6938501, Japan

来源：

CURRENT OSTEOPOROSIS REPORTS | 2016年 / 14卷 / 06期

关键词：

Fracture; Bone quality; Material properties; Pentosidine; Crosslink; Receptor for advanced glycation end products (RAGE); COLLAGEN CROSS-LINKS; MESENCHYMAL STEM-CELLS; STROMAL ST2 CELLS; MINERAL DENSITY; FRACTURE RISK; POSTMENOPAUSAL WOMEN; NONENZYMATIC GLYCATION; MECHANICAL-PROPERTIES; VERTEBRAL FRACTURES; TRABECULAR BONE;

D O I：

10.1007/s11914-016-0332-1

中图分类号：

R5 [内科学];

学科分类号：

1002 ; 100201 ;

摘要：

Diabetic patients have a higher fracture risk than expected by their bone mineral density (BMD). Poor bone quality is the most suitable and explainable cause for the elevated fracture risk in this population. Advanced glycation end products (AGEs), which are diverse compounds generated via a non-enzymatic reaction between reducing sugars and amine residues, physically affect the properties of the bone material, one of a component of bone quality, through their accumulation in the bone collagen fibers. On the other hand, these compounds biologically act as agonists for these receptors for AGEs (RAGE) and suppress bone metabolism. The concentrations of AGEs and endogenous secretory RAGE, which acts as a "decoy receptor" that inhibits the AGEs-RAGE signaling axis, are associated with fracture risk in a BMD-independent manner. AGEs are closely associated with the pathogenesis of this unique clinical manifestation through physical and biological mechanisms in patients with diabetes mellitus.

引用

页码：320 / 326

页数：7

共 77 条

[61] Differential expression of human lysyl hydroxylase genes, lysine hydroxylation, and cross-linking of type I collagen during osteoblastic differentiation in vitro [J].