人关节滑膜细胞晚期糖基化终产物结合蛋白的表达及其调节

EXPRESSION AND REGULATION OF THE BINDING PROTEINS FOR ADVANCED GLYCATION END PRODUCTS ON HUMAN JOINT SYNOVIAL CELLS

为探讨人关节滑膜细胞是否表达晚期糖基化终产物 (AGEs)结合蛋白 ,并研究其表达的调节因素 ,分离、培养正常人关节A型和B型滑膜细胞 ,用放射性配体 受体结合法检测滑膜细胞表面AGEs结合蛋白 ,并观测TNF α、IL 1β和AGE修饰的白蛋白 (AGE HSA)对滑膜细胞AGEs结合蛋白表达的影响。结果显示 ,滑膜细胞表面存在AGEs结合蛋白 ,A型细胞Kd =(1.2 7± 0 .19)× 10 -6M ,B型细胞Kd =(1.38± 0 .16 )× 10 -7M。TNF α、IL 1β和AGE HSA能上调滑膜细胞AGEs结合蛋白的表达。提示人类关节滑膜细胞可表达对AGEs特异的结合蛋白 。

The study was performed to detect the binding proteins for advanced glycation end products (AGEs) on human joint synovial cells (HSCs). Normal human synovial cells (type A and type B cells) were isolated and cultured in vitro. Binding assay was performed with radiolabeled human serum albumin modified by AGE (AGE HSA). Specific binding was defined as total binding minus binding in the presence of excess unlabeled AGE HSA. The result showed that: specific dose dependent binding of 125 I AGE HSA to immobilized HSCs was observed with R=4.90 0.75 10 4 /cell , Kd = 1.27 0.19 10 -6 M in type A HSCs , and R= 3.48 0.32 10 5 /cell, Kd= 1.38±0.16 10 -7 M in type B HSCs. TNF α,IL 1β and AGE HSA upregulated the expression of AGE binding proteins on HSCs. Normal HSCs express specific AGE binding proteins. TNF α, IL 1β and AGE HSA upregulate the expression of these proteins, suggesting that joint resident cells may be involved in the pathogenesis of dialysis related amyloidosis.