schliessen

Filtern

 

Bibliotheken

Discrimination of Isomers of Released N- and O-Glycans Using Diagnostic Product Ions in Negative Ion PGC-LC-ESI-MS/MS

Profiling cellular protein glycosylation is challenging due to the presence of highly similar glycan structures that play diverse roles in cellular physiology. As the anomericity and the exact linkage type of a single glycosidic bond can influence glycan function, there is a demand for improved and... Full description

Journal Title: Journal of the American Society for Mass Spectrometry 2018-03-30, Vol.29 (6), p.1194-1209
Main Author: Ashwood, Christopher
Other Authors: Lin, Chi-Hung , Thaysen-Andersen, Morten , Packer, Nicolle H
Format: Electronic Article Electronic Article
Language: English
Subjects:
Publisher: New York: Springer US
ID: ISSN: 1044-0305
Link: https://www.ncbi.nlm.nih.gov/pubmed/29603058
Zum Text:
SendSend as email Add to Book BagAdd to Book Bag
Staff View
recordid: cdi_proquest_miscellaneous_2020490688
title: Discrimination of Isomers of Released N- and O-Glycans Using Diagnostic Product Ions in Negative Ion PGC-LC-ESI-MS/MS
format: Article
creator:
  • Ashwood, Christopher
  • Lin, Chi-Hung
  • Thaysen-Andersen, Morten
  • Packer, Nicolle H
subjects:
  • Analytical Chemistry
  • Animals
  • Automation
  • Bioinformatics
  • Biotechnology
  • Cell Line
  • Cellular structure
  • Chemistry
  • Chemistry and Materials Science
  • Chromatography, Liquid - methods
  • Diagnostic software
  • Diagnostic systems
  • Discrimination
  • Focus: Mass Spectrometry in Glycobiology and Related Fields: Research Article
  • Fragmentation
  • Glycan
  • Glycomics - methods
  • Glycoproteins
  • Glycoproteins - chemistry
  • Glycosylation
  • Graphite - chemistry
  • Graphitization
  • Ions - analysis
  • Isomerism
  • Isomers
  • Mass spectrometers
  • Mice
  • Organic Chemistry
  • Physiological aspects
  • Polysaccharides
  • Polysaccharides - analysis
  • Porosity
  • Proteomics
  • Sialic Acids - analysis
  • Spectrometers
  • Spectrometry, Mass, Electrospray Ionization - methods
  • Tandem Mass Spectrometry - methods
  • Workflow
ispartof: Journal of the American Society for Mass Spectrometry, 2018-03-30, Vol.29 (6), p.1194-1209
description: Profiling cellular protein glycosylation is challenging due to the presence of highly similar glycan structures that play diverse roles in cellular physiology. As the anomericity and the exact linkage type of a single glycosidic bond can influence glycan function, there is a demand for improved and automated methods to confirm detailed structural features and to discriminate between structurally similar isomers, overcoming a significant bottleneck in the analysis of data generated by glycomics experiments. We used porous graphitized carbon-LC-ESI-MS/MS to separate and detect released N - and O -glycan isomers from mammalian model glycoproteins using negative mode resonance activation CID-MS/MS. By interrogating similar fragment spectra from closely related glycan isomers that differ only in arm position and sialyl linkage, product fragment ions for discrimination between these features were discovered. Using the Skyline software, at least two diagnostic fragment ions of high specificity were validated for automated discrimination of sialylation and arm position in N -glycan structures, and sialylation in O -glycan structures, complementing existing structural diagnostic ions. These diagnostic ions were shown to be useful for isomer discrimination using both linear and 3D ion trap mass spectrometers when analyzing complex glycan mixtures from cell lysates. Skyline was found to serve as a useful tool for automated assessment of glycan isomer discrimination. This platform-independent workflow can potentially be extended to automate the characterization and quantitation of other challenging glycan isomers. Graphical Abstract ᅟ
language: eng
source:
identifier: ISSN: 1044-0305
fulltext: no_fulltext
issn:
  • 1044-0305
  • 1879-1123
url: Link


@attributes
NO1
SEARCH_ENGINEprimo_central_multiple_fe
SEARCH_ENGINE_TYPEPrimo Central Search Engine
RANK2.364641
LOCALfalse
PrimoNMBib
record
control
sourceidgale_proqu
recordidTN_cdi_proquest_miscellaneous_2020490688
sourceformatXML
sourcesystemPC
galeidA542977482
sourcerecordidA542977482
originalsourceidFETCH-LOGICAL-1459t-afe13ea4378d8bed7ac032fff4173e27cd9d8399a3002697fc49408536bc0b230
addsrcrecordideNp9UVtrFDEYDaLYuvoDfJGAL76kzW0nyWPZ1nVhe8G1zyGbSYaUmaQmM0L76806VaGg5CEfJ-cczpcDwHuCTwjG4rQQxhqCMJGIKEbR4wtwTKRQiBDKXtYZc44ww8sj8KaUO4yJwEq8BkdUNQdYHoPpPBSbwxCiGUOKMHm4KWlwuRzGr653prgWXiFoYguv0bp_sCYWeFtC7OB5MF1MZQwW3uTUTnaEm1RfQ4RXrquOP9wBgDfrFdqu0MVugy53p5e7t-CVN31x757uBbj9fPFt9QVtr9eb1dkWEb5UIzLeEeYMZ0K2cu9aYSxm1HvPiWCOCtuqVjKlDMOYNkp4yxXHcsmavcV7yvACfJp973P6Prky6qGu6_reRJemoimmmCvcSFmpH59R79KUY01XWUQp3tDKXICTmdWZ3ukQfRqzsfW0bgg2RedDxc-WnCohuKRVQGaBzamU7Ly-r79t8oMmWB9K1HOJupaoDyXqx6r58BRl2g-u_aP43VoliGemNoy_-qtpQv9fazorSzWNnct_t_y36CdAzrZZ
sourcetypeAggregation Database
isCDItrue
recordtypearticle
pqid2019946249
display
typearticle
titleDiscrimination of Isomers of Released N- and O-Glycans Using Diagnostic Product Ions in Negative Ion PGC-LC-ESI-MS/MS
creatorAshwood, Christopher ; Lin, Chi-Hung ; Thaysen-Andersen, Morten ; Packer, Nicolle H
creatorcontribAshwood, Christopher ; Lin, Chi-Hung ; Thaysen-Andersen, Morten ; Packer, Nicolle H
descriptionProfiling cellular protein glycosylation is challenging due to the presence of highly similar glycan structures that play diverse roles in cellular physiology. As the anomericity and the exact linkage type of a single glycosidic bond can influence glycan function, there is a demand for improved and automated methods to confirm detailed structural features and to discriminate between structurally similar isomers, overcoming a significant bottleneck in the analysis of data generated by glycomics experiments. We used porous graphitized carbon-LC-ESI-MS/MS to separate and detect released N - and O -glycan isomers from mammalian model glycoproteins using negative mode resonance activation CID-MS/MS. By interrogating similar fragment spectra from closely related glycan isomers that differ only in arm position and sialyl linkage, product fragment ions for discrimination between these features were discovered. Using the Skyline software, at least two diagnostic fragment ions of high specificity were validated for automated discrimination of sialylation and arm position in N -glycan structures, and sialylation in O -glycan structures, complementing existing structural diagnostic ions. These diagnostic ions were shown to be useful for isomer discrimination using both linear and 3D ion trap mass spectrometers when analyzing complex glycan mixtures from cell lysates. Skyline was found to serve as a useful tool for automated assessment of glycan isomer discrimination. This platform-independent workflow can potentially be extended to automate the characterization and quantitation of other challenging glycan isomers. Graphical Abstract ᅟ
identifier
0ISSN: 1044-0305
1EISSN: 1879-1123
2DOI: 10.1007/s13361-018-1932-z
3PMID: 29603058
languageeng
publisherNew York: Springer US
subjectAnalytical Chemistry ; Animals ; Automation ; Bioinformatics ; Biotechnology ; Cell Line ; Cellular structure ; Chemistry ; Chemistry and Materials Science ; Chromatography, Liquid - methods ; Diagnostic software ; Diagnostic systems ; Discrimination ; Focus: Mass Spectrometry in Glycobiology and Related Fields: Research Article ; Fragmentation ; Glycan ; Glycomics - methods ; Glycoproteins ; Glycoproteins - chemistry ; Glycosylation ; Graphite - chemistry ; Graphitization ; Ions - analysis ; Isomerism ; Isomers ; Mass spectrometers ; Mice ; Organic Chemistry ; Physiological aspects ; Polysaccharides ; Polysaccharides - analysis ; Porosity ; Proteomics ; Sialic Acids - analysis ; Spectrometers ; Spectrometry, Mass, Electrospray Ionization - methods ; Tandem Mass Spectrometry - methods ; Workflow
ispartofJournal of the American Society for Mass Spectrometry, 2018-03-30, Vol.29 (6), p.1194-1209
rights
0American Society for Mass Spectrometry 2018
1COPYRIGHT 2018 Springer
citedbyFETCH-LOGICAL-1459t-afe13ea4378d8bed7ac032fff4173e27cd9d8399a3002697fc49408536bc0b230
citesFETCH-LOGICAL-1459t-afe13ea4378d8bed7ac032fff4173e27cd9d8399a3002697fc49408536bc0b230
orcidid0000-0002-7532-4021
links
openurl$$Topenurl_article
thumbnail$$Usyndetics_thumb_exl
backlink$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/29603058$$D View this record in MEDLINE/PubMed
search
creatorcontrib
0Ashwood, Christopher
1Lin, Chi-Hung
2Thaysen-Andersen, Morten
3Packer, Nicolle H
title
0Discrimination of Isomers of Released N- and O-Glycans Using Diagnostic Product Ions in Negative Ion PGC-LC-ESI-MS/MS
1Journal of the American Society for Mass Spectrometry
addtitle
0J. Am. Soc. Mass Spectrom
1J Am Soc Mass Spectrom
descriptionProfiling cellular protein glycosylation is challenging due to the presence of highly similar glycan structures that play diverse roles in cellular physiology. As the anomericity and the exact linkage type of a single glycosidic bond can influence glycan function, there is a demand for improved and automated methods to confirm detailed structural features and to discriminate between structurally similar isomers, overcoming a significant bottleneck in the analysis of data generated by glycomics experiments. We used porous graphitized carbon-LC-ESI-MS/MS to separate and detect released N - and O -glycan isomers from mammalian model glycoproteins using negative mode resonance activation CID-MS/MS. By interrogating similar fragment spectra from closely related glycan isomers that differ only in arm position and sialyl linkage, product fragment ions for discrimination between these features were discovered. Using the Skyline software, at least two diagnostic fragment ions of high specificity were validated for automated discrimination of sialylation and arm position in N -glycan structures, and sialylation in O -glycan structures, complementing existing structural diagnostic ions. These diagnostic ions were shown to be useful for isomer discrimination using both linear and 3D ion trap mass spectrometers when analyzing complex glycan mixtures from cell lysates. Skyline was found to serve as a useful tool for automated assessment of glycan isomer discrimination. This platform-independent workflow can potentially be extended to automate the characterization and quantitation of other challenging glycan isomers. Graphical Abstract ᅟ
subject
0Analytical Chemistry
1Animals
2Automation
3Bioinformatics
4Biotechnology
5Cell Line
6Cellular structure
7Chemistry
8Chemistry and Materials Science
9Chromatography, Liquid - methods
10Diagnostic software
11Diagnostic systems
12Discrimination
13Focus: Mass Spectrometry in Glycobiology and Related Fields: Research Article
14Fragmentation
15Glycan
16Glycomics - methods
17Glycoproteins
18Glycoproteins - chemistry
19Glycosylation
20Graphite - chemistry
21Graphitization
22Ions - analysis
23Isomerism
24Isomers
25Mass spectrometers
26Mice
27Organic Chemistry
28Physiological aspects
29Polysaccharides
30Polysaccharides - analysis
31Porosity
32Proteomics
33Sialic Acids - analysis
34Spectrometers
35Spectrometry, Mass, Electrospray Ionization - methods
36Tandem Mass Spectrometry - methods
37Workflow
issn
01044-0305
11879-1123
fulltextfalse
rsrctypearticle
creationdate2018
recordtypearticle
recordideNp9UVtrFDEYDaLYuvoDfJGAL76kzW0nyWPZ1nVhe8G1zyGbSYaUmaQmM0L76806VaGg5CEfJ-cczpcDwHuCTwjG4rQQxhqCMJGIKEbR4wtwTKRQiBDKXtYZc44ww8sj8KaUO4yJwEq8BkdUNQdYHoPpPBSbwxCiGUOKMHm4KWlwuRzGr653prgWXiFoYguv0bp_sCYWeFtC7OB5MF1MZQwW3uTUTnaEm1RfQ4RXrquOP9wBgDfrFdqu0MVugy53p5e7t-CVN31x757uBbj9fPFt9QVtr9eb1dkWEb5UIzLeEeYMZ0K2cu9aYSxm1HvPiWCOCtuqVjKlDMOYNkp4yxXHcsmavcV7yvACfJp973P6Prky6qGu6_reRJemoimmmCvcSFmpH59R79KUY01XWUQp3tDKXICTmdWZ3ukQfRqzsfW0bgg2RedDxc-WnCohuKRVQGaBzamU7Ly-r79t8oMmWB9K1HOJupaoDyXqx6r58BRl2g-u_aP43VoliGemNoy_-qtpQv9fazorSzWNnct_t_y36CdAzrZZ
startdate20180330
enddate20180330
creator
0Ashwood, Christopher
1Lin, Chi-Hung
2Thaysen-Andersen, Morten
3Packer, Nicolle H
general
0Springer US
1Springer
2Springer Nature B.V
scope
0CGR
1CUY
2CVF
3ECM
4EIF
5NPM
6AAYXX
7CITATION
8BSHEE
93V.
107X7
117XB
1288E
138FE
148FG
158FI
168FJ
178FK
188G5
19ABUWG
20ARAPS
21AZQEC
22BENPR
23BGLVJ
24DWQXO
25FYUFA
26GHDGH
27GNUQQ
28GUQSH
29HCIFZ
30K9.
31M0S
32M1P
33M2O
34MBDVC
35P5Z
36P62
37PADUT
38PQEST
39PQQKQ
40PQUKI
41PRINS
42Q9U
437X8
orcididhttps://orcid.org/0000-0002-7532-4021
sort
creationdate20180330
titleDiscrimination of Isomers of Released N- and O-Glycans Using Diagnostic Product Ions in Negative Ion PGC-LC-ESI-MS/MS
authorAshwood, Christopher ; Lin, Chi-Hung ; Thaysen-Andersen, Morten ; Packer, Nicolle H
facets
frbrtype5
frbrgroupidcdi_FETCH-LOGICAL-1459t-afe13ea4378d8bed7ac032fff4173e27cd9d8399a3002697fc49408536bc0b230
rsrctypearticles
prefilterarticles
languageeng
creationdate2018
topic
0Analytical Chemistry
1Animals
2Automation
3Bioinformatics
4Biotechnology
5Cell Line
6Cellular structure
7Chemistry
8Chemistry and Materials Science
9Chromatography, Liquid - methods
10Diagnostic software
11Diagnostic systems
12Discrimination
13Focus: Mass Spectrometry in Glycobiology and Related Fields: Research Article
14Fragmentation
15Glycan
16Glycomics - methods
17Glycoproteins
18Glycoproteins - chemistry
19Glycosylation
20Graphite - chemistry
21Graphitization
22Ions - analysis
23Isomerism
24Isomers
25Mass spectrometers
26Mice
27Organic Chemistry
28Physiological aspects
29Polysaccharides
30Polysaccharides - analysis
31Porosity
32Proteomics
33Sialic Acids - analysis
34Spectrometers
35Spectrometry, Mass, Electrospray Ionization - methods
36Tandem Mass Spectrometry - methods
37Workflow
creatorcontrib
0Ashwood, Christopher
1Lin, Chi-Hung
2Thaysen-Andersen, Morten
3Packer, Nicolle H
collection
0Medline
1MEDLINE
2MEDLINE (Ovid)
3MEDLINE
4MEDLINE
5PubMed
6CrossRef
7Academic OneFile (A&I only)
8ProQuest Central (Corporate)
9Health & Medical Collection
10ProQuest Central (purchase pre-March 2016)
11Medical Database (Alumni Edition)
12ProQuest SciTech Collection
13ProQuest Technology Collection
14Hospital Premium Collection
15Hospital Premium Collection (Alumni Edition)
16ProQuest Central (Alumni) (purchase pre-March 2016)
17Research Library (Alumni Edition)
18ProQuest Central (Alumni Edition)
19Advanced Technologies & Aerospace Collection
20ProQuest Central Essentials
21ProQuest Central
22Technology Collection
23ProQuest Central Korea
24Health Research Premium Collection
25Health Research Premium Collection (Alumni)
26ProQuest Central Student
27Research Library Prep
28SciTech Premium Collection
29ProQuest Health & Medical Complete (Alumni)
30Health & Medical Collection (Alumni Edition)
31Medical Database
32Research Library
33Research Library (Corporate)
34Advanced Technologies & Aerospace Database
35ProQuest Advanced Technologies & Aerospace Collection
36Research Library China
37ProQuest One Academic Eastern Edition
38ProQuest One Academic
39ProQuest One Academic UKI Edition
40ProQuest Central China
41ProQuest Central Basic
42MEDLINE - Academic
jtitleJournal of the American Society for Mass Spectrometry
delivery
delcategoryRemote Search Resource
fulltextno_fulltext
addata
au
0Ashwood, Christopher
1Lin, Chi-Hung
2Thaysen-Andersen, Morten
3Packer, Nicolle H
formatjournal
genrearticle
ristypeJOUR
atitleDiscrimination of Isomers of Released N- and O-Glycans Using Diagnostic Product Ions in Negative Ion PGC-LC-ESI-MS/MS
jtitleJournal of the American Society for Mass Spectrometry
stitleJ. Am. Soc. Mass Spectrom
addtitleJ Am Soc Mass Spectrom
date2018-03-30
risdate2018
volume29
issue6
spage1194
epage1209
pages1194-1209
issn1044-0305
eissn1879-1123
abstractProfiling cellular protein glycosylation is challenging due to the presence of highly similar glycan structures that play diverse roles in cellular physiology. As the anomericity and the exact linkage type of a single glycosidic bond can influence glycan function, there is a demand for improved and automated methods to confirm detailed structural features and to discriminate between structurally similar isomers, overcoming a significant bottleneck in the analysis of data generated by glycomics experiments. We used porous graphitized carbon-LC-ESI-MS/MS to separate and detect released N - and O -glycan isomers from mammalian model glycoproteins using negative mode resonance activation CID-MS/MS. By interrogating similar fragment spectra from closely related glycan isomers that differ only in arm position and sialyl linkage, product fragment ions for discrimination between these features were discovered. Using the Skyline software, at least two diagnostic fragment ions of high specificity were validated for automated discrimination of sialylation and arm position in N -glycan structures, and sialylation in O -glycan structures, complementing existing structural diagnostic ions. These diagnostic ions were shown to be useful for isomer discrimination using both linear and 3D ion trap mass spectrometers when analyzing complex glycan mixtures from cell lysates. Skyline was found to serve as a useful tool for automated assessment of glycan isomer discrimination. This platform-independent workflow can potentially be extended to automate the characterization and quantitation of other challenging glycan isomers. Graphical Abstract ᅟ
copNew York
pubSpringer US
pmid29603058
doi10.1007/s13361-018-1932-z
orcididhttps://orcid.org/0000-0002-7532-4021