EXPRESSION AND REGULATION OF THE BINDING PROTEINS FOR ADVANCED GLYCATION END PRODUCTS ON HUMAN JOINT SYNOVIAL CELLS
- VernacularTitle: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
- Author:
Junqi GUO
;
Fanfan HOU
;
Xun ZHANG
- Publication Type:Journal Article
- Keywords:
synovial cell;
glycasylation end products;
receptors;
dialysis related amyloidosis
- From:Medical Journal of Chinese People's Liberation Army
2001;0(07):-
- CountryChina
- Language:Chinese
-
Abstract:
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 ?,IL 1? and AGE HSA upregulated the expression of AGE binding proteins on HSCs. Normal HSCs express specific AGE binding proteins. TNF ?, IL 1? and AGE HSA upregulate the expression of these proteins, suggesting that joint resident cells may be involved in the pathogenesis of dialysis related amyloidosis.
