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Rutin Metabolites as Powerful Inhibitors of Advanced Glycation End Products
Author(s) -
Laurean Daniel Cervantes,
Pashikanti Srinath
Publication year - 2008
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.22.1_supplement.614.12
Subject(s) - methylglyoxal , glycation , rutin , chemistry , biochemistry , pharmacology , glyoxal , enzyme , antioxidant , medicine , receptor , organic chemistry
Glycation is a non‐enzymatic reaction between reducing sugars and protein‐amino groups that through ketoamines leads to advanced glycation end products (AGEs) such as fluorescent and non‐fluorescent ( N ε ‐carboxymethyllysine, CML) protein adducts. Glycation is implicated in diabetic complications involving kidney, eye and neuron damage. Aminoguanidine (AG), a powerful AGE inhibitor, induced critical side effects when tested as anti‐diabetic drug in clinical trials. This showed a need for new and improved AGE inhibitors. Histone H1 and ADP‐ribose were used as a glycation model since it allows to distinguish true AGE inhibitors from general antioxidants. Rutin derivatives were tested as AGE inhibitors since rutin, a dietary flavonoid contained in plant‐derived products, isn't absorbed intact due to gut microflora degradation. Our data showed that 3,4‐dihydroxyphenylacetic acid and 3,4‐dihydroxytoluene were equal or better inhibitors of fluorescence, and CML‐protein adducts than AG. In contrast, homovanillic acid and 3‐hydroxyphenylacetic acid, weren't as effective AGE inhibitors. Methylglyoxal and glyoxal were used as glycating agents of histone H1 to elucidate the mechanism of AGE‐inhibition and effective AGE inhibition was observed with rutin metabolites and AG. These results present alternative effective AGE inhibitors to AG that might be recommended as supplements in the prevention of diabetes complications.