Resveratrol Prevents Dendritic Cell Maturation in Response to Advanced Glycation End Products
Figure 1
Molecular characterization of glycated albumin. (a) Structural analysis of the amino acid sequence of albumin. The analysis indicates that 22 (in bold) out of 60 lysine residues (K) are potential glycation sites. (b) Fluorescent AGE formation in an albumin solution incubated in the presence of D-glucose or D-mannitol (250 mM) after 10, 30, or 60 days. Data are expressed as means of arbitrary unit/mg of proteins ± SD (). *; †‡. The black star indicates the moderately modified AGE-albumin used in the subsequent cellular studies. (c) SDS-PAGE analysis of albumin preparations (50 μg per lane) incubated or not with 250 mM glucose for the reported times, followed by Coomassie staining, according to standard protocol. (d) Size exclusion chromatography of albumin and AGE-albumin. Albumin was incubated for 30 days with 250 mM D-mannitol (albumin) or D-glucose (AGE-albumin). One representative experiment out of three is reported.
