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Title: Hepatic advanced glycation endproduct binding is increased in experimental diabetes.
Austin Authors: Youssef, S;Soulis, T;Cooper, Mark E
Affiliation: Department of Medicine, University of Melbourne, Austin and Repatriation Medical Centre, West Heidelberg, Victoria, Australia
Issue Date: 1-Nov-1998
Publication information: Cellular and Molecular Biology (noisy-le-grand, France); 44(7): 1095-100
Abstract: Advanced glycation endproducts (AGEs) have been implicated in the pathogenesis of diabetic complications. However, clearance pathways for these products have not been fully delineated. This study investigates changes in AGE binding in the liver in association with experimental diabetes using in vitro and in vivo radioautography techniques. Male Sprague-Dawley rats were randomised into control and diabetic rats and sacrificed after 3 weeks. Frozen liver sections (20 microm) were incubated with 125I-AGE-BSA. To further localise the AGE binding site, in vivo radioautography was performed by injection of 15 microCi of 125I-AGE-BSA into the abdominal aorta of the rat. Specific binding sites for AGEs were detected in the liver by in vitro radioautography. There was a significant increase in 125I-AGE binding in the liver of diabetic rats. Emulsion radioautography revealed that binding was localised primarily in Küpffer and liver endothelial cells. AGE binding sites were increased in the liver after 3 weeks of experimental diabetes. It remains speculative as to whether these binding sites represent AGE clearance receptors.
Gov't Doc #: 9846891
Journal: Cellular and molecular biology (Noisy-le-Grand, France)
Type: Journal Article
Subjects: Animals
Binding Sites
Diabetes Mellitus, Experimental.metabolism
Glycosylation End Products, Advanced.metabolism
In Vitro Techniques
Kupffer Cells.metabolism
Protein Binding
Rats, Sprague-Dawley
Appears in Collections:Journal articles

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