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ORIGINAL RESEARCH ARTICLE

A BRIEF COMMUNICATION

Antiglycation Effect of Gliclazide on In Vitro AGE Formation from Glucose and Methylglyoxal

Weiguo Li^*, Kimiko Ota, Jiro Nakamura, Keiko Naruse, Eitaro Nakashima, Yutaka Oiso and Yoji Hamada^,1

^* Department of Physiology and Endocrinology Medical College of Georgia, Augusta, GA; Department of Endocrinology and Diabetes, Nagoya University Graduate School of Medicine; Department of Internal Medicine, School of Dentistry, Aichi Gakuin University; and Department of Metabolic Medicine, Nagoya University School of Medicine, Nagoya, Japan

To whom requests for reprints should be addressed at ¹ Department of Metabolic Medicine, Nagoya University School of Medicine, 65 Tsuruma-cho, Showa-ku, Nagoya 466-8550, Japan. E-mail: yhama{at}med.nagoya-u.ac.jp

Gliclazide, a sulfonylurea widely used for treatment of diabetes mellitus, is known to scavenge reactive oxygen species. To clarify whether its antioxidative ability interferes with the glycation processes, we incubated bovine serum albumin (BSA) with 1 M glucose or 1 mM methylglyoxal, in the presence or absence of gliclazide, and observed the formation of advanced glycation end products (AGEs). AGE production was assessed by AGE-specific fluorescence, an enzyme-linked immunosorbent assay (ELISA), and Western blotting. The fluorescence at excitation/emission wavelengths of 320/383 nm and 335/385 nm was definitely increased by incubating BSA with 1 M glucose or 1 mM methylglyoxal, and 1 mM gliclazide significantly blunted the fluorescent augmentation, in both wavelengths, in a dose-dependent fashion. Gliclazide almost equaled to aminoguanidine, a putative antiglycation agent, in the inhibitory effect on the glucose-induced fluorescence, while the methylglyoxal-derived fluorescent formation was less suppressed by gliclazide than by aminoguanidine. The AGE concentrations determined by ELISA showed similar results. Incubation of BSA with 1 M glucose or 1 mM methylglyoxal yielded an apparent increase in carboxymethyllysine or argpyrimidine. Both AGEs were significantly lowered by 1 mM gliclazide and a reduction of glucose-derived carboxymethyllysine was comparable to that caused by aminoguanidine. The results of Western blotting supported the findings in ELISA. To our knowledge, the present study provides the first evidence of the antiglycation effect of gliclazide on in vitro AGE formation from glucose and methylglyoxal.

Key Words: gliclazide • oxidative stress • glycation • advanced glycation end products