Journal of Biological Chemistry p. 17326 - 17338 (2019)
Update date:2022-08-03
Topics:
Ohno, Rei-Ichi
Ichimaru, Kenta
Tanaka, Seitaro
Sugawa, Hikari
Katsuta, Nana
Sakake, Shiori
Tominaga, Yu-Ki
Ban, Ikuho
Shirakawa, Jun-Ichi
Yamaguchi, Yoshiki
Ito, Emi
Taniguchi, Naoyuki
Nagai, Ryoji
Prolonged hyperglycemia generates advanced glycation endproducts (AGEs), which are believed to be involved in the pathogenesis of diabetic complications. In the present study, we developed a polyclonal antibody against fructose-modified proteins (Fru-P antibody) and identified its epitope as glucoselysine (GL) by NMR and LC-electrospray ionization (ESI)- quadrupole TOF (QTOF) analyses and evaluated its potential role in diabetes sequelae. Although the molecular weight of GL was identical to that of fructoselysine (FL), GL was distinguishable from FL because GL was resistant to acid hydrolysis, which converted all of the FLs to furosine. We also detected GL in vitro when reduced BSA was incubated with fructose for 1 day. However, when we incubated reduced BSA with glucose, galactose, or mannose for 14 days, we did not detect GL, suggesting that GL is dominantly generated from fructose. LC-ESI-MS/MS experiments with synthesized [13C6]GL indicated that the GL levels in the rat eye lens time-dependently increase after streptozotocininduced diabetes. We observed a 31.3-fold increase in GL 8 weeks after the induction compared with nondiabetic rats, and N∈-(carboxymethyl)lysine and furosine increased by 1.7- and 21.5-fold, respectively, under the same condition. In contrast, sorbitol in the lens levelled off at 2 weeks after diabetes induction. We conclude that GL may be a useful biological marker to monitor and elucidate the mechanism of protein degeneration during progression of diabetes.
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