Advanced glycation end products inhibit the expression of collagens type I and III by XXXX gingival fibroblasts.

@entity1 @entity6 @entity2348 @entity98 @entity2521 @entity413
BACKGROUND: It is evident that @entity6 are closely interrelated. Accumulation of advanced glycation end products (AGEs), coupled with exaggerated host responses to @entity2348 , may account for the increased periodontal destruction observed in @entity1 with uncontrolled @entity6 . The present study investigated the effects of AGEs on the viability of @entity1 gingival fibroblasts (HGFs) and the expression of types I and III collagen in HGFs. METHODS: The cell viability of HGFs was examined by @entity98 assay, whereas the expression of types I and III collagen message and protein was detected by real-time quantitative reverse transcription-polymerase chain reaction and sandwich enzyme-linked immunosorbent assay, respectively. RESULTS: AGEs significantly suppressed the cell viability of HGFs from 24 to 72 hours (P <0.01). A high concentration of @entity413 (25 mmol/l) in the culture media exaggerated the inhibition of the survival rate of HGFs (P <0.01). The expression of collagen types I and III messages and proteins was significantly downregulated at 72 hours by AGEs in a concentration-dependent manner (P <0.05). Moreover, the synthesis of intracellular types I and III collagen protein was markedly inhibited by AGEs (P <0.05). CONCLUSIONS: AGEs may suppress the cell viability of HGFs and downregulate the expression of types I and III collagen by the cells. Further investigations are warranted to clarify the molecular mechanisms of AGEs in the regulation of cell function and collagen metabolism in @entity1 with @entity6 and @entity2521 .
