Glycoproteomic analysis of the changes in protein N-glycosylation during neuronal differentiation in human-induced pluripotent stem cells and derived neuronal cells

Abstract N-glycosylation of glycoproteins, a major post-translational modification, plays a crucial role in various biological phenomena. In central nervous systems, N-glycosylation is thought to be associated with differentiation and regeneration; however, the state and role of N-glycosylation in n...

Descripción completa

Guardado en:

Detalles Bibliográficos
Autores principales:	Kazumasa Kimura, Takumi Koizumi, Takaya Urasawa, Yuki Ohta, Daisuke Takakura, Nana Kawasaki
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2021
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/1b5fad1276fc47159531affe4d74a5f9
Etiquetas:	Agregar Etiqueta Sin Etiquetas, Sea el primero en etiquetar este registro!

id	oai:doaj.org-article:1b5fad1276fc47159531affe4d74a5f9
record_format	dspace
spelling	oai:doaj.org-article:1b5fad1276fc47159531affe4d74a5f92021-12-02T15:49:31ZGlycoproteomic analysis of the changes in protein N-glycosylation during neuronal differentiation in human-induced pluripotent stem cells and derived neuronal cells10.1038/s41598-021-90102-z2045-2322https://doaj.org/article/1b5fad1276fc47159531affe4d74a5f92021-05-01T00:00:00Zhttps://doi.org/10.1038/s41598-021-90102-zhttps://doaj.org/toc/2045-2322Abstract N-glycosylation of glycoproteins, a major post-translational modification, plays a crucial role in various biological phenomena. In central nervous systems, N-glycosylation is thought to be associated with differentiation and regeneration; however, the state and role of N-glycosylation in neuronal differentiation remain unclear. Here, we conducted sequential LC/MS/MS analyses of tryptic digest, enriched glycopeptides, and deglycosylated peptides of proteins derived from human-induced pluripotent stem cells (iPSCs) and iPSC-derived neuronal cells, which were used as a model of neuronal differentiation. We demonstrate that the production profiles of many glycoproteins and their glycoforms were altered during neuronal differentiation. Particularly, the levels of glycoproteins modified with an N-glycan, consisting of five N-acetylhexosamines, three hexoses, and a fucose (HN5H3F), increased in dopaminergic neuron-rich cells (DAs). The N-glycan was deduced to be a fucosylated and bisected biantennary glycan based on product ion spectra. Interestingly, the HN5H3F-modified proteins were predicted to be functionally involved in neural cell adhesion, axon guidance, and the semaphorin-plexin signaling pathway, and protein modifications were site-selective and DA-selective regardless of protein production levels. Our integrated method for glycoproteome analysis and resultant profiles of glycoproteins and their glycoforms provide valuable information for further understanding the role of N-glycosylation in neuronal differentiation and neural regeneration.Kazumasa KimuraTakumi KoizumiTakaya UrasawaYuki OhtaDaisuke TakakuraNana KawasakiNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 11, Iss 1, Pp 1-12 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Kazumasa Kimura Takumi Koizumi Takaya Urasawa Yuki Ohta Daisuke Takakura Nana Kawasaki Glycoproteomic analysis of the changes in protein N-glycosylation during neuronal differentiation in human-induced pluripotent stem cells and derived neuronal cells
description	Abstract N-glycosylation of glycoproteins, a major post-translational modification, plays a crucial role in various biological phenomena. In central nervous systems, N-glycosylation is thought to be associated with differentiation and regeneration; however, the state and role of N-glycosylation in neuronal differentiation remain unclear. Here, we conducted sequential LC/MS/MS analyses of tryptic digest, enriched glycopeptides, and deglycosylated peptides of proteins derived from human-induced pluripotent stem cells (iPSCs) and iPSC-derived neuronal cells, which were used as a model of neuronal differentiation. We demonstrate that the production profiles of many glycoproteins and their glycoforms were altered during neuronal differentiation. Particularly, the levels of glycoproteins modified with an N-glycan, consisting of five N-acetylhexosamines, three hexoses, and a fucose (HN5H3F), increased in dopaminergic neuron-rich cells (DAs). The N-glycan was deduced to be a fucosylated and bisected biantennary glycan based on product ion spectra. Interestingly, the HN5H3F-modified proteins were predicted to be functionally involved in neural cell adhesion, axon guidance, and the semaphorin-plexin signaling pathway, and protein modifications were site-selective and DA-selective regardless of protein production levels. Our integrated method for glycoproteome analysis and resultant profiles of glycoproteins and their glycoforms provide valuable information for further understanding the role of N-glycosylation in neuronal differentiation and neural regeneration.
format	article
author	Kazumasa Kimura Takumi Koizumi Takaya Urasawa Yuki Ohta Daisuke Takakura Nana Kawasaki
author_facet	Kazumasa Kimura Takumi Koizumi Takaya Urasawa Yuki Ohta Daisuke Takakura Nana Kawasaki
author_sort	Kazumasa Kimura
title	Glycoproteomic analysis of the changes in protein N-glycosylation during neuronal differentiation in human-induced pluripotent stem cells and derived neuronal cells
title_short	Glycoproteomic analysis of the changes in protein N-glycosylation during neuronal differentiation in human-induced pluripotent stem cells and derived neuronal cells
title_full	Glycoproteomic analysis of the changes in protein N-glycosylation during neuronal differentiation in human-induced pluripotent stem cells and derived neuronal cells
title_fullStr	Glycoproteomic analysis of the changes in protein N-glycosylation during neuronal differentiation in human-induced pluripotent stem cells and derived neuronal cells
title_full_unstemmed	Glycoproteomic analysis of the changes in protein N-glycosylation during neuronal differentiation in human-induced pluripotent stem cells and derived neuronal cells
title_sort	glycoproteomic analysis of the changes in protein n-glycosylation during neuronal differentiation in human-induced pluripotent stem cells and derived neuronal cells
publisher	Nature Portfolio
publishDate	2021
url	https://doaj.org/article/1b5fad1276fc47159531affe4d74a5f9
work_keys_str_mv	AT kazumasakimura glycoproteomicanalysisofthechangesinproteinnglycosylationduringneuronaldifferentiationinhumaninducedpluripotentstemcellsandderivedneuronalcells AT takumikoizumi glycoproteomicanalysisofthechangesinproteinnglycosylationduringneuronaldifferentiationinhumaninducedpluripotentstemcellsandderivedneuronalcells AT takayaurasawa glycoproteomicanalysisofthechangesinproteinnglycosylationduringneuronaldifferentiationinhumaninducedpluripotentstemcellsandderivedneuronalcells AT yukiohta glycoproteomicanalysisofthechangesinproteinnglycosylationduringneuronaldifferentiationinhumaninducedpluripotentstemcellsandderivedneuronalcells AT daisuketakakura glycoproteomicanalysisofthechangesinproteinnglycosylationduringneuronaldifferentiationinhumaninducedpluripotentstemcellsandderivedneuronalcells AT nanakawasaki glycoproteomicanalysisofthechangesinproteinnglycosylationduringneuronaldifferentiationinhumaninducedpluripotentstemcellsandderivedneuronalcells
_version_	1718385675860967424

Glycoproteomic analysis of the changes in protein N-glycosylation during neuronal differentiation in human-induced pluripotent stem cells and derived neuronal cells

Ejemplares similares