Glycation of human serum albumin: inhibition by Diclofenac.
Glycation is a non-enzymatic modification of proteins by sugars, probably responsible for the initiation of complications in diabetes patients and aging individuals. Our in vitro experiments show an inhibition of sugar attachment in the presence of Diclofenac. The levels of advanced glycation products, measured as specific fluorescent groups, were also lowered due to Diclofenac. These results were compared with inhibition by Aspirin (acetylsalicylic acid), a known inhibitor of the glycation process. The protection by Diclofenac is based on a non-covalent interaction of the drug with serum albumin. There is evidence that Diclofenac specifically blocks at least one of the major glycation sites of human serum albumin.
van Boekel
M A
MA
Department of Biochemistry, University of Nijmegen, Netherlands.
van den Bergh
P J
PJ
Hoenders
H J
HJ
D001241:Aspirin / Q000737:chemistry; D001667:Binding, Competitive; D004008:Diclofenac / Q000737:chemistry*; D019298:Glucose-6-Phosphate; D005958:Glucosephosphates / Q000737:chemistry*; D006801:Humans; D011485:Protein Binding; D012709:Serum Albumin / Q000737:chemistry*; D013050:Spectrometry, Fluorescence
D005958:Glucosephosphates; D012709:Serum Albumin; D004008:Diclofenac; D019298:Glucose-6-Phosphate; D001241:Aspirin