XXXX -microglobulin modified with advanced glycation end products modulates collagen synthesis by @entity1 fibroblasts.

@entity1 @entity4173 @entity2783 @entity5764 @entity924 @entity2262 @entity2263
@entity2263 -microglobulin @entity2783 (A beta 2m) is a serious complication for @entity1 undergoing long-term dialysis. @entity2262 modified with advanced glycation end products (beta 2m-AGE) is a major component of the amyloid in A beta 2m. It is not completely understood whether beta 2m-AGE plays an active role in the pathogenesis of A beta 2m, or if its presence is a secondary event of the disease. @entity2262 amyloid is mainly located in @entity924 that are rich in collagen, and local fibroblasts constitute the principal cell population in the synthesis and metabolism of collagen. Recent identification of AGE binding proteins on @entity1 fibroblasts lead to the hypothesis that the fibroblast may be a target for the biological action of beta 2m-AGE. The present study demonstrated that two @entity1 fibroblast cell lines exhibited a decrease in procollagen type I mRNA and type I collagen synthesis after exposure to beta 2m-AGE for 72 hours. Similar results were observed using AGE-modified albumin. Antibody against the @entity5764 , the receptor for AGE, attenuated this decrease in synthesis, indicating that the response was partially mediated by @entity5764 . In addition, antibody against epidermal growth factor (EGF) attenuated the decrease in @entity4173 mRNA and type I collagen induced by beta 2m-AGE, suggesting that EGF acts as an intermediate factor. These findings support the hypothesis that beta 2m-AGE actively participates in connective tissue and bone remodeling via a pathway involving fibroblast @entity5764 , and at least one interposed mediator, the growth factor EGF.
