糖蛋白
聚糖
糖基化
内质网
高尔基体
生物化学
岩藻糖
内质网相关蛋白降解
天冬酰胺
化学
N-连接糖基化
生物
细胞生物学
氨基酸
未折叠蛋白反应
出处
期刊:Advances in neurobiology
日期:2022-10-19
卷期号:: 65-93
被引量:4
标识
DOI:10.1007/978-3-031-12390-0_3
摘要
Many membrane-resident and secreted proteins, including growth factors and their receptors are N-glycosylated. The initial N-glycan structure is synthesized in the endoplasmic reticulum (ER) as a branched structure on a lipid anchor (dolicholpyrophosphate) and then co-translationally, "en bloc" transferred and linked via N-acetylglucosamine to asparagine within a specific N-glycosylation acceptor sequence of the nascent recipient protein. In the ER and then the Golgi apparatus, the N-linked glycan structure is modified by hydrolytic removal of sugar residues ("trimming") followed by re-glycosylation with additional sugar residues ("processing") such as galactose, fucose or sialic acid to form complex N-glycoproteins. While the sequence of the reactions leading to biosynthesis, "en bloc" transfer and processing of N-glycans is well investigated, it is still not completely understood how N-glycans affect the biological fate and function of N-glycoproteins. This review will discuss the biology of N-glycoprotein synthesis, processing and function with specific reference to the physiology and pathophysiology of the immune and nervous system, as well as infectious diseases such as Covid-19.
科研通智能强力驱动
Strongly Powered by AbleSci AI