|M.Sc Student||Karin Kertesz Rosenfeld|
|Subject||The Influence of Advanced Glycation End Products (AGEs) on|
Cells in Culture
|Department||Department of Biotechnology and Food Engineering||Supervisors||Professor Emeritus Yannai Shmuel (Deceased)|
|Mr. Werman Moshe|
The non-enzymatic glycation, also named the Maillard reaction, is a posttranslational modification of proteins, caused by the condensation with reducing sugars. It includes an array of spontaneous complex chain reactions, which produces a heterogeneous group of irreversible adducts, called Advanced Glycation End Products (AGEs).
Another mechanism, termed glycoxidation, includes an oxidation reaction of a free sugar and/or protein-bound sugars produced as a result of glycation, in the presence of metallic ions.
The objectives of this study were to prepare and characterize AGEs formed from different reducing sugars (glucose, fructose and glyceraldehyde) and to investigate the influence of AGEs on the normal rat kidney (NRK) epithelial cell line originating from its proximal tubules.
The results indicate that browning rate, typical AGE fluorescence, typical pentosidine fluorescence, carbonyl level and cross-linking, characterized by SDS-PAGE assay, were compatible with the sugar reactivity. Different sugars produce different or similar AGE compositions at different time intervals.
AGEs elicited a significant inhibitory effect (p<0.05) on the viability of the cell line, in a kind of sugar- and dose- dependent manner.
The effect of oxidative stress on the cells, caused by exposure to AGEs, was reflected in an increase in carbonyl level in the cells and a decrease in glutathione peroxidase activity.