N-glycosylation proteome of endoplasmic reticulum in mouse liver by ConA affinity chromatography coupled with LTQ-FT mass spectrometry

doi:10.1007/s11426-010-0133-9

	N-glycosylation proteome of endoplasmic reticulum in mouse liver by ConA affinity chromatography coupled with LTQ-FT mass spectrometry
	Song LiNa 1; Wang JingLan 1; Liu JinFeng 1; Lu Zhuang 1,3; Sui ShaoHui 1; Jia Wei 1; Yang Bing 1; Chi Hao 2; Wang LeHeng 2; He SiMin 2; Yu WenFeng 1; Meng LingYan 1; Chen Shuo 1; Peng Xu 1; Liang Yimin 1; Cai Yun 1; Qian XiaoHong 1
	2010-04-01
发表期刊	SCIENCE CHINA-CHEMISTRY
ISSN	1674-7291
卷号	53 期号:4 页码:768-777
摘要	Glycosylation is the most versatile and one of the most significant protein post-translational modifications. It is generally classified into three categories according to the amino acid to which the glycan is attached: N-glycosylation, O-glycosylation and C-glycosylation. Synthesis of N-glycoproteins occurs in the rough endoplasmic reticulum (rER), and all N-glycoproteins synthesized in rER have uniform glycan endings with mannose (Man) and glucose (Glc). A systematic strategy was developed to comprehensively profile N-glycoproteins in complex biological samples. The lectin Concanvalin A (ConA), which has a high affinity for glycans ending with Man, was used to extract the N-glycoproteins synthesized or located in the rER, and identified the N-glycoproteins and their glycosylation sites by LTQ-FT MS. The analysis was repeated three times at both the biological sample and mass spectrometry levels. In total, 323 glycosylation sites on 212 N-glycoproteins were identified in the mouse liver. Of these, 131 were known N-glycoproteins in the Swissprot database. The identified N-glycoproteins were classified according to their cell location by the Swissprot database and GO software. The identified N-glycoproteins in this study would serve as a good complement to the N-glycoprotein database for the mouse liver.
关键词	glycosylation rER lectin affinity chromatography ConA LTQ-FT MS
DOI	10.1007/s11426-010-0133-9
收录类别	SCI
语种	英语
资助项目	National Natural Science Foundation of China[30621063] ; National Natural Science Foundation of China[20635010] ; National Natural Science Foundation of China[20735005] ; China National Key Program for Basic Research[2006CB910801] ; China National Key Program for Basic Research[2007CB914104] ; China National Key Program for Basic Research[2002CB713807] ; National High Technology Research and Development Program of China[2006AA02A308] ; National High Technology Research and Development Program of China[2007AA02Z315] ; National High Technology Research and Development Program of China[2007AA02Z326]
WOS研究方向	Chemistry
WOS类目	Chemistry, Multidisciplinary
WOS记录号	WOS:000278263400010
出版者	SCIENCE CHINA PRESS
引用统计	被引频次：2[WOS] [WOS记录] [WOS相关记录]
文献类型	期刊论文
条目标识符	http://119.78.100.204/handle/2XEOYT63/12053
专题	中国科学院计算技术研究所期刊论文_英文
通讯作者	Qian XiaoHong
作者单位	1.Beijing Inst Radiat Med, Beijing Proteome Res Ctr, State Key Lab Prote, Beijing 102206, Peoples R China 2.Chinese Acad Sci, Inst Comp Technol, Beijing 100190, Peoples R China 3.Beijing Inst Biotechnol, Beijing 100081, Peoples R China
推荐引用方式 GB/T 7714	Song LiNa,Wang JingLan,Liu JinFeng,et al. N-glycosylation proteome of endoplasmic reticulum in mouse liver by ConA affinity chromatography coupled with LTQ-FT mass spectrometry[J]. SCIENCE CHINA-CHEMISTRY,2010,53(4):768-777.
APA	Song LiNa.,Wang JingLan.,Liu JinFeng.,Lu Zhuang.,Sui ShaoHui.,...&Qian XiaoHong.(2010).N-glycosylation proteome of endoplasmic reticulum in mouse liver by ConA affinity chromatography coupled with LTQ-FT mass spectrometry.SCIENCE CHINA-CHEMISTRY,53(4),768-777.
MLA	Song LiNa,et al."N-glycosylation proteome of endoplasmic reticulum in mouse liver by ConA affinity chromatography coupled with LTQ-FT mass spectrometry".SCIENCE CHINA-CHEMISTRY 53.4(2010):768-777.