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内分泌学中的O-连接N-乙酰葡糖胺化修饰:甜蜜的联系

O-GlcNAcylation in Endocrinology: The Sweet Link.

作者信息

Knier Adam Salm, Olivier-Van Stichelen Stephanie

机构信息

Department of Biochemistry, Medical College of Wisconsin, Milwaukee, WI 53226, USA.

Department of Neurosurgery, Medical College of Wisconsin, Milwaukee, WI 53226, USA.

出版信息

Endocrinology. 2025 Apr 22;166(6). doi: 10.1210/endocr/bqaf072.

Abstract

O-GlcNAcylation is a dynamic posttranslational modification that involves the addition of N-acetylglucosamine (GlcNAc) to the serine and threonine residues of proteins. Over the past 4 decades, this modification has become increasingly recognized as having a critical influence in the field of endocrinology. The carefully controlled hormonal input for regulating sleep, mood, response to stress, growth, development, and metabolism are often associated with O-GlcNAc-dependent signaling. As protein O-GlcNAcylation patterns are heavily dependent on environmental glucose concentrations, hormone-secreting cells sense the changes in local environmental glucose concentrations and adjust hormone secretion accordingly. This ability of cells to sense nutritional cues and fine-tune hormonal production is particularly relevant toward maintaining a functional and responsive endocrine system, therefore emphasizing the importance of O-GlcNAc in the scope and application of endocrinology. This review examines how O-GlcNAcylation participates in hormonal homeostasis in different endocrine tissues and systems, from the pineal gland to the placenta, and underscores the significance of O-GlcNAc in the field of endocrinology.

摘要

O-连接的N-乙酰葡糖胺化是一种动态的翻译后修饰,涉及将N-乙酰葡糖胺(GlcNAc)添加到蛋白质的丝氨酸和苏氨酸残基上。在过去的40年里,这种修饰在内分泌学领域的关键影响越来越受到认可。调节睡眠、情绪、应激反应、生长、发育和新陈代谢的精心控制的激素输入通常与O-连接的N-乙酰葡糖胺依赖性信号传导有关。由于蛋白质的O-连接的N-乙酰葡糖胺化模式严重依赖于环境葡萄糖浓度,分泌激素的细胞会感知局部环境葡萄糖浓度的变化,并相应地调整激素分泌。细胞感知营养信号并微调激素产生的这种能力对于维持功能性和反应性内分泌系统尤为重要,因此强调了O-连接的N-乙酰葡糖胺在内分泌学范围和应用中的重要性。本综述探讨了O-连接的N-乙酰葡糖胺化如何参与从松果体到胎盘的不同内分泌组织和系统中的激素稳态,并强调了O-连接的N-乙酰葡糖胺在内分泌学领域的重要性。

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-GlcNAcylation regulates OTX2's proteostasis.N-乙酰葡糖胺化调节OTX2的蛋白质稳态。
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