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• W2162912395 abstract "Glucokinase, the enzyme that catalyses the conversion of glucose to G-6-P, plays a key role in glucose metabolism. AGEs are implicated in diabetic complications. A previous study reported that AGEs decreased β-cell function through inhibition of cytochrome c oxidase and adenosine triphosphate synthesis. This study investigated the effects of AGEs on glucokinase and islet function.Six-month-old male C57BL6 mice were divided into bovine serum albumin (BSA) and AGE-BSA groups. BSA (200 µg/g) and AGE-BSA (60 U/g) were administered intraperitoneally twice daily. After 2 weeks, serum AGE levels were measured, oral glucose tolerance test was performed, and insulin levels during the oral glucose tolerance test were determined. Glucokinase protein expression level and activity were measured in pancreatic islets.We observed that the normal mice (C57/BL6) treated for 2 weeks with AGE-BSA showed impaired glucose tolerance and decrease in acute insulin release. Glucokinase activity in islets from the AGE-BSA-treated mice was significantly inhibited and accompanied by blunted response of islets to high glucose stimulation. Moreover, in vitro experiments showed that glucokinase protein expression was decreased, its activity was inhibited, and islet function was decreased. GKA partially restored glucokinase activity and islet function caused by AGEs.We concluded that AGEs inhibited glucokinase activity, leading to islet dysfunction in mouse pancreatic islets." @default.
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• W2162912395 date "2011-09-01" @default.
• W2162912395 modified "2023-09-23" @default.
• W2162912395 title "Advanced glycation end products downregulate glucokinase in mice" @default.
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• W2162912395 doi "https://doi.org/10.1002/dmrr.1208" @default.
• W2162912395 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/21538775" @default.
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