title: Cyanidin-3-rutinoside attenuates methylglyoxal-induced protein glycation and DNA damage via carbonyl trapping ability and scavenging reactive oxygen species.
abstract: BACKGROUND
  Advanced glycation end-products (AGEs) play a significant role in the development and progression of vascular complication in diabetes. Anthocyanin has been recently reported to possess antiglycating activity. This study aimed to determine whether a naturally occurring anthocyanin, cyanidin-3-rutinoside (C3R) inhibits methylglyoxal (MG) induced protein glycation and oxidative protein and DNA damage.
  
  
  METHODS
  C3R (0.125-1 mM) was incubated with bovine serum albumin and MG (1 mM) for 2 weeks. The formation of fluorescent AGEs was measured by using spectrofluorometer and thiol group content were used to detect protein oxidative damage. Gel electrophoresis was used to determine whether C3R (0.125-1 mM) reduced DNA strand breakage in a glycation model comprising lysine, MG and/or Cu(2+). The generation of superoxide anions and hydroxyl radicals were detected by the cytochrome c reduction assay and the thiobarbituric acid reactive substances assay. MG-trapping capacity was assessed by high performance liquid chromatography (HPLC).
  
  
  RESULTS
  C3R (0.25-1 mM) reduced the formation of fluorescent AGEs and depleted protein thiol groups in bovine serum albumin mediated by MG. At 1 mM C3R inhibited oxidative DNA damage in the glycation model (p < 0.05) and at 0.5-1 mM prevented Cu(2+) induced DNA strand breakage in the presence of lysine and MG. The findings showed that C3R reduced the formation of superoxide anion and hydroxyl radicals during the glycation reaction of MG with lysine. C3R directly trapped MG in a concentration and time dependent manner (both p < 0.001).
  
  
  CONCLUSIONS
  These findings suggest that C3R protects against MG-induced protein glycation and oxidative damage to protein and DNA by scavenging free radicals and trapping MG.
authors.affiliation: Program in Biomedical Sciences, Graduate School, Chulalongkorn University, Bangkok, 10330, Thailand.
authors.forename: Thavaree
authors.initials: T
authors.lastname: Thilavech
authors.affiliation: Department of Nutrition and Dietetics, Faculty of Allied Health Sciences, Chulalongkorn University, Bangkok, 10330, Thailand.
authors.forename: Sathaporn
authors.initials: S
authors.lastname: Ngamukote
authors.affiliation: CSIRO Food and Nutrition, Adelaide, SA, 5000, Australia.
authors.forename: Damien
authors.initials: D
authors.lastname: Belobrajdic
authors.affiliation: CSIRO Food and Nutrition, Adelaide, SA, 5000, Australia.
authors.forename: Mahinda
authors.initials: M
authors.lastname: Abeywardena
authors.affiliation: Department of Nutrition and Dietetics, Faculty of Allied Health Sciences, Chulalongkorn University, Bangkok, 10330, Thailand. sirichai.a@chula.ac.th.
authors.forename: Sirichai
authors.initials: S
authors.lastname: Adisakwattana
mesh_terms: D000818:Animals; D000872:Anthocyanins / Q000494:pharmacology*; D002417:Cattle; D004249:DNA Damage / Q000187:drug effects*; D005609:Free Radicals / Q000378:metabolism; D017127:Glycation End Products, Advanced / Q000378:metabolism*; D066298:In Vitro Techniques; D010084:Oxidation-Reduction; D011765:Pyruvaldehyde / Q000037:antagonists & inhibitors*; D017382:Reactive Oxygen Species / Q000378:metabolism*; D012710:Serum Albumin, Bovine; D013438:Sulfhydryl Compounds / Q000378:metabolism
chemical_list: D000872:Anthocyanins; D005609:Free Radicals; D017127:Glycation End Products, Advanced; D017382:Reactive Oxygen Species; D013438:Sulfhydryl Compounds; D012710:Serum Albumin, Bovine; D011765:Pyruvaldehyde; C428983:cyanidin 3-rutinoside
keywords: Cyanidin-3-rutinoside; Methylglyoxal; Oxidative DNA damage; Protein glycation