Edited by Miguel De la RosaPolyamines can presumably inhibit protein glycation, when associated with the methylglyoxal inevitably produced during glycolysis. Herein, we hypothesized a nonenzymatic interaction between putrescine and methylglyoxal in putrescine-deficient or -overexpressing Dictyostelium cells in high-glucose medium, which can control methylglyoxal production. Putrescine was essentially required for growth rescue accompanying methylglyoxal detoxification when cells underwent growth defect and cell cycle G1-arrest when supplemented with high glucose. Furthermore, methylglyoxal regulation by putrescine seemed to be a parallel pathway independent of the changes in cellular glutathione content in high-glucose medium. Consequently, we suggest that Dictyostelium cells need polyamines for normal growth and cellular methylglyoxal regulation.Keywords: Dictyostelium discoideum; glutathione; methylglyoxal; polyamines; putrescine High amounts of cellular glucose, a simple aldosic monosaccharide and a reducing sugar, can cause cellular damage that is followed by increased production of chemically reactive MG in mammals [1]. Glucose has been elucidated as a major a-dicarbonyl compound causing AGEs to form and furthermore is associated with engagement of their cellular RAGE in diabetic complications [2]. Particularly, MG has been strongly suggested to activate nonenzymatic glycation of proteins to form irreversible AGEs [3,4]. Although the biochemical origins of MG production have still not been addressed distinctly [5], MG seems to alter the intracellular content of both GSH and ROS in eukaryotes [6].To explain the biochemical roles of MG and its regulating enzymes, many types of enzyme systems have been proposed in mammals [7,8]. In microorganisms, our current study revealed that cellular MG levels altered Candida cell physiology and differentiation through their MG-consuming enzyme systems [9,10]. Additionally, we previously reported the crucial effect of MG on cell growth, cell cycle, and differentiation when MG-reducing aldose reductase (AlrA) is regulated in Dictyostelium [11]. However, nonenzymatic MG-scavenging molecules have not been sufficiently studied either in vitro or in vivo. The limited cellular MG regulation by MG-consuming enzymes is not sufficient for the nonenzymatic MG production,
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