INTRACELLULAR MODIFICATIONS OF HUMAN APOLIPOPROTEIN E

人载脂蛋白 E 的细胞内修饰

• 批准号: 7723008
• 负责人: VASSILIS I ZANNIS
• 金额: $ 0.13万
• 依托单位: BOSTON UNIVERSITY MEDICAL CAMPUS
• 依托单位国家: 美国
• 财政年份: 2008
• 资助国家: 美国
• 起止时间: 2008-06-01 至 2009-05-31
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/7723008
• 关键词: Alzheimer' s Disease; Apolipoprotein E; Apolipoproteins; Cells; Computer Retrieval of Information on Scientific Projects Database; Disease; Funding; Glycopeptides; Grant; Homologous Gene; Human; Hyperlipoproteinemia Type III; Institution; Lectin; Lipoproteins; Mass Spectrum Analysis; Modification; Plasma; Polysaccharides; Positioning Attribute; Research; Research Personnel; Resources; Sialic Acids; Site; Source; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization; Standards of Weights and Measures; United States National Institutes of Health; glycosylation

This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. The subproject and investigator (PI) may have received primary funding from another NIH source, and thus could be represented in other CRISP entries. The institution listed is for the Center, which is not necessarily the institution for the investigator. Human plasma apolipoprotein E (apoE) is responsible for the clearance of lipoprotein remnants and has been implicated in diseases like familial type III hyperlipoproteinemia and Alzheimer's disease. It is known to be initially sialylated after synthesis and later desialylated in the plasma. Studies of synthesis and intracellular modification of apoE by HepG2 cells have shown modified apoE isoproteins corresponding to the sialo apoE forms with two, four or six sialic acid residues. The expected O-glycosylation site needs to be confirmed and the kind of modification to be characterized by mass spectrometry. From a tryptic digest of apoE, one disialylated glycan could be detected at the expected position by LC-MS/MS, and was then also found by standard MALDI TOF MS. It is planned to isolate the glycopeptide(s) with the help of lectins. Vibrationally cooled (VC) MALDI FT-MS may help to detect higher sialylated, more instable homologs.

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