NDLI: Elucidation of O-glycosylation structures of the ß-amyloid precursor protein by liquid chromatography - mass spectrometry using electron transfer dissociation and collision induced dissociation

Please wait, while we are loading the content...

Proteomics-determined differences in the Concanavalin-A-fractionated proteome of hippocampus and inferior parietal lobule in subjects with Alzheimer’s disease and mild cognitive impairment: Implications for progression of AD

Pancreatic Cancer Serum Detection Using A Lectin/Glyco-Antibody Array Method

Exploiting Differential Dissociation Chemistries of O-Linked Glycopeptide Ions for the Localization of Mucin-Type Protein Glycosylation

Analytical Performance of Immobilized Pronase for Glycopeptide Footprinting and Implications for Surpassing Reductionist Glycoproteomics

Identification and development of fucosylated glycoproteins as biomarkers of primary hepatocellular carcinoma

Glycoproteomics for Prostate Cancer Detection: Changes in Serum PSA Glycosylation Patterns

Glycomic Characterization of Prostate Specific Antigen and Prostatic Acid Phosphatase in Prostate Cancer and Benign Disease Seminal Plasma Fluids

Elucidation of O-glycosylation structures of the ß-amyloid precursor protein by liquid chromatography - mass spectrometry using electron transfer dissociation and collision induced dissociation

Mapping Glycans onto Specific N-Linked Glycosylation Sites of Pyrus Communis PGIP Redefines the Interface for EPG:PGIP Interactions

A Perspective on the Maillard Reaction and the Analysis of Protein Glycation by Mass Spectrometry: Probing the Pathogenesis of Chronic Disease

Mass spectrometry based targeted protein quantification: methods and applications

Phosphorylation Site Mapping of Endogenous Proteins: A Combined MS and Bioinformatics Approach

Identification and Analysis of Occludin Phosphosites: A Combined Mass Spectrometry and Bioinformatics Approach

Comparison of MS2-only, MSA, and MS2/MS3 Methodologies for Phosphopeptide Identification

Identification and Verification of Lysine Propionylation and Butyrylation in Yeast Core Histones Using PTMap Software

High-Throughput Liquid-Liquid Fractionation of Multiple Protein Post-Translational Modifications*

EVALUATION OF ARCHIVAL TIME ON SHOTGUN PROTEOMICS OF FORMALIN-FIXED AND PARAFFIN-EMBEDDED TISSUES

Proteomic Analysis and Identification of the Structural and Regulatory Proteins of the Rhodobacter capsulatus Gene Transfer Agent

Prion Disease Diagnosis by Proteomic Profiling

Absolute Quantification of C-Reactive Protein in Human Plasma Derived from Patients with Epithelial Ovarian Cancer Utilizing Protein Cleavage Isotope Dilution Mass Spectrometry

Year: 2009, Volume: 8, Issue: 1

Year: 2008, Volume: 7

Year: 2007, Volume: 6

Year: 2006, Volume: 5

Year: 2005, Volume: 4

Year: 2004, Volume: 3

Year: 2002, Volume: 1

Elucidation of O-glycosylation structures of the ß-amyloid precursor protein by liquid chromatography - mass spectrometry using electron transfer dissociation and collision induced dissociation

Content Provider	PubMed Central
Author	Perdivara, Irina Petrovich, Robert Bernadette, Alliquant Deterding, Leesa J. Tomer, Kenneth B. Przybylski, Michael
Abstract	Accumulation and deposition of ß-amyloid peptide, a major constituent in neuritic plaques are hallmarks of Alzheimer’s disease (AD) and AD-related neurodegenerative diseases. ß-Amyloid (Aß) is derived from the proteolytic cleavage of amyloid precursor protein (APP), a transmembrane protein present in three major isoforms in brain comprising 695, 751 and 770 amino acids, respectively. Among other post-translational modifications, APP is modified during maturation by N- and O- glycosylation, which are thought to be responsible for its expression and secretion. Unlike N-glycosylation, no sites of O-glycosylation of APP have previously been reported. We report here the identification of three specific O-glycosylation sites of the secreted APP695 (sAPP695) produced in CHO cells, using a combination of high performance liquid chromatography and electrospray - tandem mass spectrometry. With the use of electron transfer dissociation and collision induced dissociation (ETD and CID), we identified type, composition and structures of the Core 1 type O-linked glycans attached at the residues: Thr 291, Thr 292 and Thr 576 of the full length APP695. The glycosylations comprise multiple short glycans, containing N-acetyl galactosamine (GalNAc), Gal-GalNAc and sialic acid terminated structures. The presence of the glycopeptides in the tryptic mixture was identified using the CID-generated sugar oxonium ions. ETD proved to be valuable for the unambiguous identification of the modified sites as ETD fragmentation occurred along the peptide backbone with little or no cleavage of the glycans. Thus, the combination of the CID and ETD techniques in LC-MS is shown here, as a powerful tool for de novo identification of O-glycosylations at unknown modification sites in proteins.
Related Links	http://dx.doi.org/10.1021/pr800758g
Starting Page	631
File Format	PDF
ISSN	15353907
e-ISSN	15353907
Journal	Journal of proteome research
Issue Number	2
Volume Number	8
Language	English
Publisher Date	2009-02-01
Access Restriction	Open
Subject Keyword	Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	Chemistry Biochemistry

Sl.	Authority	Responsibilities	Communication Details
1	Ministry of Education (GoI), Department of Higher Education	Sanctioning Authority	https://www.education.gov.in/ict-initiatives
2	Indian Institute of Technology Kharagpur	Host Institute of the Project: The host institute of the project is responsible for providing infrastructure support and hosting the project	https://www.iitkgp.ac.in
3	National Digital Library of India Office, Indian Institute of Technology Kharagpur	The administrative and infrastructural headquarters of the project	Dr. B. Sutradhar bsutra@ndl.gov.in
4	Project PI / Joint PI	Principal Investigator and Joint Principal Investigators of the project	Dr. B. Sutradhar bsutra@ndl.gov.in Prof. Saswat Chakrabarti will be added soon
5	Website/Portal (Helpdesk)	Queries regarding NDLI and its services	support@ndl.gov.in
6	Contents and Copyright Issues	Queries related to content curation and copyright issues	content@ndl.gov.in
7	National Digital Library of India Club (NDLI Club)	Queries related to NDLI Club formation, support, user awareness program, seminar/symposium, collaboration, social media, promotion, and outreach	clubsupport@ndl.gov.in
8	Digital Preservation Centre (DPC)	Assistance with digitizing and archiving copyright-free printed books	dpc@ndl.gov.in
9	IDR Setup or Support	Queries related to establishment and support of Institutional Digital Repository (IDR) and IDR workshops	idr@ndl.gov.in

Liquid chromatography-tandem mass spectrometry-based fragmentation analysis of glycopeptides

Improved identification of O-linked glycopeptides from ETD data with optimized scoring for different charge states and cleavage specificities

Novel Glycosylation Sites Localized in Campylobacter jejuni Flagellin FlaA by Liquid Chromatography Electron Capture Dissociation Tandem Mass Spectrometry

Glycosylation profiles of epitope-specific anti-β-amyloid antibodies revealed by liquid chromatography–mass spectrometry

Defining the Disulfide Bonds of Insulin-like Growth Factor-binding Protein-5 by Tandem Mass Spectrometry with Electron Transfer Dissociation and Collision-induced Dissociation

Liquid Chromatography Electron Capture Dissociation Tandem Mass Spectrometry (LC-ECD-MS/MS) versus Liquid Chromatography Collision-induced Dissociation Tandem Mass Spectrometry (LC-CID-MS/MS) for the Identification of Proteins

Liquid chromatography electron capture dissociation tandem mass spectrometry (LC-ECD-MS/MS) versus liquid chromatography collision-induced dissociation tandem mass spectrometry (LC-CID-MS/MS) for the identification of proteins

Characterization of protein N-glycosylation by tandem mass spectrometry using complementary fragmentation techniques

4-HNE Adduct Stability Characterized by Collision-Induced Dissociation and Electron Transfer Dissociation Mass Spectrometry

Elucidation of O-glycosylation structures of the ß-amyloid precursor protein by liquid chromatography - mass spectrometry using electron transfer dissociation and collision induced dissociation

Similar Documents

Liquid chromatography-tandem mass spectrometry-based fragmentation analysis of glycopeptides

Improved identification of O-linked glycopeptides from ETD data with optimized scoring for different charge states and cleavage specificities

Novel Glycosylation Sites Localized in Campylobacter jejuni Flagellin FlaA by Liquid Chromatography Electron Capture Dissociation Tandem Mass Spectrometry

Glycosylation profiles of epitope-specific anti-β-amyloid antibodies revealed by liquid chromatography–mass spectrometry

Defining the Disulfide Bonds of Insulin-like Growth Factor-binding Protein-5 by Tandem Mass Spectrometry with Electron Transfer Dissociation and Collision-induced Dissociation

Liquid Chromatography Electron Capture Dissociation Tandem Mass Spectrometry (LC-ECD-MS/MS) versus Liquid Chromatography Collision-induced Dissociation Tandem Mass Spectrometry (LC-CID-MS/MS) for the Identification of Proteins

Liquid chromatography electron capture dissociation tandem mass spectrometry (LC-ECD-MS/MS) versus liquid chromatography collision-induced dissociation tandem mass spectrometry (LC-CID-MS/MS) for the identification of proteins

Characterization of protein N-glycosylation by tandem mass spectrometry using complementary fragmentation techniques

4-HNE Adduct Stability Characterized by Collision-Induced Dissociation and Electron Transfer Dissociation Mass Spectrometry

Elucidation of O-glycosylation structures of the ß-amyloid precursor protein by liquid chromatography - mass spectrometry using electron transfer dissociation and collision induced dissociation