Latvian Institute of Organic Synthesis, Aizkraukles Str. 21, Riga, LV1006, Latvia.
J Physiol Sci. 2012 Nov;62(6):469-78. doi: 10.1007/s12576-012-0224-9. Epub 2012 Aug 15.
The glyoxalase enzymes catalyse the conversion of reactive glucose metabolites into non-toxic products as a part of the cellular defence system against glycation. This study investigated changes in glyoxalase 1 and glyoxalase 2 activities and the development of diabetic complications in experimental animal models of obesity (Zucker fa/fa rats) and type 2 diabetes mellitus (Goto-Kakizaki rats). In contrast to Zucker rats, in Goto-Kakizaki rats the glyoxalase 1 activities in brain, spinal cord and sciatic nerve tissues were significantly reduced by 10, 32 and 36 %, respectively. Lower glyoxalase 1 activity in the neuronal tissues was associated with a higher blood glucose concentration and impaired endothelium-dependent relaxation to acetylcholine in aortic rings in Goto-Kakizaki rats. This study provides evidence for disturbed neuronal glyoxalase 1 activity under conditions of hyperglycaemia in the presence of impaired endothelium-dependent relaxation and cognitive function.
该糖氧醛酸酶酶催化的反应性葡萄糖代谢物转化为无毒的产品作为细胞防御系统的一部分对糖化。本研究探讨了糖氧醛酸酶 1 和糖氧醛酸酶 2 的活性变化和糖尿病并发症的发展在肥胖的实验动物模型( Zucker fa/fa 大鼠)和 2 型糖尿病( Goto-Kakizaki 大鼠)。与 Zucker 大鼠相反,在 Goto-Kakizaki 大鼠的脑中糖氧醛酸酶 1 活性分别显著降低 10%、32%和 36%,脊髓和坐骨神经组织。神经元组织中较低的糖氧醛酸酶 1 活性与较高的血糖浓度和受损的内皮依赖性松弛有关乙酰胆碱在 Goto-Kakizaki 大鼠的主动脉环中。本研究为在存在受损的内皮依赖性松弛和认知功能的情况下,高血糖条件下神经元糖氧醛酸酶 1 活性紊乱提供了证据。