Are advanced glycation end-product-modified proteins of pathogenetic importance in fibromyalgia?

被引:28
作者
Hein, G [1 ]
Franke, S [1 ]
机构
[1] Univ Jena, Dept Internal Med Rheumatol & Osteol 4, D-07740 Jena, Germany
关键词
fibromyalgia; advanced glycation end-product; pentosidine; collagen cross-linking; pain;
D O I
10.1093/rheumatology/41.10.1163
中图分类号
R5 [内科学];
学科分类号
1002 [临床医学]; 100201 [内科学];
摘要
Objective. To quantify the serum levels of the advanced glycation end-product (AGE) pentosidine in 41 patients with fibromyalgia (FM) and 46 healthy controls. The formation of pentosidine is closely related to oxidative stress. Methods. Pentosidine was measured by reverse-phased high-performance liquid chromatography with gradient separation on a RP-18 column. Results. Patients with FM have significantly higher pentosidine serum levels than healthy subjects. Conclusion. AGE modification of proteins leads to reduced solubility and high resistance to proteolytic digestion of such altered proteins (e.g. AGE-modified collagens). AGES are also able to stimulate different kinds of cells via activation of the NFkappaB, mediated by specific receptors of AGES (e.g. RAGE) on the cell surface. Both mechanisms may contribute to the development, perpetuation and spreading of pain phenomena in FM patients.
引用
收藏
页码:1163 / 1167
页数:5
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