Synthesis, Processing, and Function of N-Glycans in N-Glycoproteins.

Autor:	Bieberich E; Department of Physiology, University of Kentucky College of Medicine, Lexington, KY, USA. Erhard.bieberich@uky.edu.; Veteran Affairs Medical Center, Lexington, KY, USA. Erhard.bieberich@uky.edu.
Jazyk:	angličtina
Zdroj:	Advances in neurobiology [Adv Neurobiol] 2023; Vol. 29, pp. 65-93.
DOI:	10.1007/978-3-031-12390-0_3
Abstrakt:	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. (© 2023. The Author(s), under exclusive license to Springer Nature Switzerland AG.)
Databáze:	MEDLINE
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