摘要
O位N-乙酰葡糖胺(O-GlcNAc)修饰普遍存在于许多胞浆蛋白与核蛋白中,并且与磷酸化体系竞争相同的丝氨酸/苏氨酸残基位点,进而调节细胞内重要的生理过程。胰岛素抵抗是指胰岛素刺激肌肉和脂肪细胞摄取和利用葡萄糖的能力降低。高血糖能提高细胞内己糖胺通路的活性,使参与信号转导的蛋白质的O-GlcNAc修饰水平异常升高,打破了O-GlcNAc修饰与磷酸化的动态平衡,诱导胰岛素抵抗。本文就近年来有关O-GlcNAc修饰异常与胰岛素抵抗的相互关系做一综述。
O-linked a-N-acetylglucosamine glycosylation （O-GlcNAc） exists universally in many nucleocytoplasmic proteins, and it competes directly with phosphorylation for the same serine/threonine residues sites, thereby modulating important intracellular physiological processes in cells. Insulin resistance is defined as that muscle and adipocytes have reduced ability to uptake and use glucose stimulated by insulin. Hyperglycemia can elevate the activity of hexosamine biosynthesis pathway, making the level of O-GIcNAc posttranslational modifications on proteins involved in signal transduction unusual increase, so the dynamic balance between O-GlcNAc modification and phosphorylation is broken, which induces insulin resistance. This paper aims to review the relationship between aberrant O-GlcNAcylation and insulin resistance.
出处
《生命的化学》
CAS
CSCD
北大核心
2009年第3期365-369,共5页
Chemistry of Life
