Glycoproteomics in neurodegenerative diseases
Identifieur interne : 000700 ( Main/Exploration ); précédent : 000699; suivant : 000701Glycoproteomics in neurodegenerative diseases
Auteurs : Hyejin Hwang [États-Unis] ; Jianpeng Zhang [États-Unis] ; Kathryn A. Chung [États-Unis] ; James B. Leverenz [États-Unis] ; Cyrus P. Zabetian [États-Unis] ; Elaine R. Peskind [États-Unis] ; Joseph Jankovic [États-Unis] ; Zhen Su [États-Unis] ; Aneeka M. Hancock [États-Unis] ; Catherine Pan [États-Unis] ; Thomas J. Montine [États-Unis] ; Sheng Pan [États-Unis] ; John Nutt [États-Unis] ; Roger Albin [États-Unis] ; Marla Gearing [États-Unis] ; Richard P. Beyer [États-Unis] ; Min Shi [États-Unis] ; Jing Zhang [États-Unis]Source :
- Mass Spectrometry Reviews [ 0277-7037 ] ; 2010-01.
English descriptors
- KwdEn :
Abstract
Protein glycosylation regulates protein function and cellular distribution. Additionally, aberrant protein glycosylations have been recognized to play major roles in human disorders, including neurodegenerative diseases. Glycoproteomics, a branch of proteomics that catalogs and quantifies glycoproteins, provides a powerful means to systematically profile the glycopeptides or glycoproteins of a complex mixture that are highly enriched in body fluids, and therefore, carry great potential to be diagnostic and/or prognostic markers. Application of this mass spectrometry‐based technology to the study of neurodegenerative disorders (e.g., Alzheimer's disease and Parkinson's disease) is relatively new, and is expected to provide insight into the biochemical pathogenesis of neurodegeneration, as well as biomarker discovery. In this review, we have summarized the current understanding of glycoproteins in biology and neurodegenerative disease, and have discussed existing proteomic technologies that are utilized to characterize glycoproteins. Some of the ongoing studies, where glycoproteins isolated from cerebrospinal fluid and human brain are being characterized in Parkinson's disease at different stages versus controls, are presented, along with future applications of targeted validation of brain specific glycoproteins in body fluids. © 2009 Wiley Periodicals, Inc., Mass Spec Rev 29:79–125, 2010
Url:
DOI: 10.1002/mas.20221
Affiliations:
- États-Unis
- Géorgie (États-Unis), Michigan, Oregon, Texas, Washington (État)
- Houston
- Baylor College of Medicine
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Beyer</name><affiliation wicri:level="2"><country xml:lang="fr">États-Unis</country><placeName><region type="state">Washington (État)</region></placeName><wicri:cityArea>Department of Environmental & Occupational Health Sciences, University of Washington School of Medicine, Seattle</wicri:cityArea></affiliation></author><author><name sortKey="Shi, Min" sort="Shi, Min" uniqKey="Shi M" first="Min" last="Shi">Min Shi</name><affiliation wicri:level="2"><country xml:lang="fr">États-Unis</country><placeName><region type="state">Washington (État)</region></placeName><wicri:cityArea>Department of Pathology, University of Washington, Seattle</wicri:cityArea></affiliation></author><author><name sortKey="Zhang, Jing" sort="Zhang, Jing" uniqKey="Zhang J" first="Jing" last="Zhang">Jing Zhang</name><affiliation wicri:level="2"><country xml:lang="fr">États-Unis</country><placeName><region type="state">Washington (État)</region></placeName><wicri:cityArea>Department of Pathology, University of Washington, Seattle</wicri:cityArea></affiliation></author></analytic><monogr></monogr><series><title level="j">Mass Spectrometry Reviews</title><title level="j" type="abbrev">Mass Spectrom. Rev.</title><idno type="ISSN">0277-7037</idno><idno type="eISSN">1098-2787</idno><imprint><publisher>Wiley Subscription Services, Inc., A Wiley Company</publisher><pubPlace>Hoboken</pubPlace><date type="published" when="2010-01">2010-01</date><biblScope unit="volume">29</biblScope><biblScope unit="issue">1</biblScope><biblScope unit="page" from="79">79</biblScope><biblScope unit="page" to="125">125</biblScope></imprint><idno type="ISSN">0277-7037</idno></series><idno type="istex">39E49D67A31877FB13570FF15D84333251F02047</idno><idno type="DOI">10.1002/mas.20221</idno><idno type="ArticleID">MAS20221</idno></biblStruct></sourceDesc><seriesStmt><idno type="ISSN">0277-7037</idno></seriesStmt></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Alzheimer's diseases</term><term>Parkinson's disease</term><term>biomarkers</term><term>cerebrospinal fluids</term><term>glycoproteomics</term><term>mass spectrometry</term></keywords></textClass><langUsage><language ident="en">en</language></langUsage></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Protein glycosylation regulates protein function and cellular distribution. Additionally, aberrant protein glycosylations have been recognized to play major roles in human disorders, including neurodegenerative diseases. Glycoproteomics, a branch of proteomics that catalogs and quantifies glycoproteins, provides a powerful means to systematically profile the glycopeptides or glycoproteins of a complex mixture that are highly enriched in body fluids, and therefore, carry great potential to be diagnostic and/or prognostic markers. Application of this mass spectrometry‐based technology to the study of neurodegenerative disorders (e.g., Alzheimer's disease and Parkinson's disease) is relatively new, and is expected to provide insight into the biochemical pathogenesis of neurodegeneration, as well as biomarker discovery. In this review, we have summarized the current understanding of glycoproteins in biology and neurodegenerative disease, and have discussed existing proteomic technologies that are utilized to characterize glycoproteins. Some of the ongoing studies, where glycoproteins isolated from cerebrospinal fluid and human brain are being characterized in Parkinson's disease at different stages versus controls, are presented, along with future applications of targeted validation of brain specific glycoproteins in body fluids. © 2009 Wiley Periodicals, Inc., Mass Spec Rev 29:79–125, 2010</div></front></TEI><affiliations><list><country><li>États-Unis</li></country><region><li>Géorgie (États-Unis)</li><li>Michigan</li><li>Oregon</li><li>Texas</li><li>Washington (État)</li></region><settlement><li>Houston</li></settlement><orgName><li>Baylor College of Medicine</li></orgName></list><tree><country name="États-Unis"><region name="Washington (État)"><name sortKey="Hwang, Hyejin" sort="Hwang, Hyejin" uniqKey="Hwang H" first="Hyejin" last="Hwang">Hyejin Hwang</name></region><name sortKey="Albin, Roger" sort="Albin, Roger" uniqKey="Albin R" first="Roger" last="Albin">Roger Albin</name><name sortKey="Beyer, Richard P" sort="Beyer, Richard P" uniqKey="Beyer R" first="Richard P." last="Beyer">Richard P. Beyer</name><name sortKey="Chung, Kathryn A" sort="Chung, Kathryn A" uniqKey="Chung K" first="Kathryn A." last="Chung">Kathryn A. Chung</name><name sortKey="Gearing, Marla" sort="Gearing, Marla" uniqKey="Gearing M" first="Marla" last="Gearing">Marla Gearing</name><name sortKey="Hancock, Aneeka M" sort="Hancock, Aneeka M" uniqKey="Hancock A" first="Aneeka M." last="Hancock">Aneeka M. Hancock</name><name sortKey="Jankovic, Joseph" sort="Jankovic, Joseph" uniqKey="Jankovic J" first="Joseph" last="Jankovic">Joseph Jankovic</name><name sortKey="Leverenz, James B" sort="Leverenz, James B" uniqKey="Leverenz J" first="James B." last="Leverenz">James B. Leverenz</name><name sortKey="Leverenz, James B" sort="Leverenz, James B" uniqKey="Leverenz J" first="James B." last="Leverenz">James B. Leverenz</name><name sortKey="Montine, Thomas J" sort="Montine, Thomas J" uniqKey="Montine T" first="Thomas J." last="Montine">Thomas J. Montine</name><name sortKey="Nutt, John" sort="Nutt, John" uniqKey="Nutt J" first="John" last="Nutt">John Nutt</name><name sortKey="Pan, Catherine" sort="Pan, Catherine" uniqKey="Pan C" first="Catherine" last="Pan">Catherine Pan</name><name sortKey="Pan, Sheng" sort="Pan, Sheng" uniqKey="Pan S" first="Sheng" last="Pan">Sheng Pan</name><name sortKey="Peskind, Elaine R" sort="Peskind, Elaine R" uniqKey="Peskind E" first="Elaine R." last="Peskind">Elaine R. Peskind</name><name sortKey="Peskind, Elaine R" sort="Peskind, Elaine R" uniqKey="Peskind E" first="Elaine R." last="Peskind">Elaine R. Peskind</name><name sortKey="Shi, Min" sort="Shi, Min" uniqKey="Shi M" first="Min" last="Shi">Min Shi</name><name sortKey="Su, Zhen" sort="Su, Zhen" uniqKey="Su Z" first="Zhen" last="Su">Zhen Su</name><name sortKey="Zabetian, Cyrus P" sort="Zabetian, Cyrus P" uniqKey="Zabetian C" first="Cyrus P." last="Zabetian">Cyrus P. Zabetian</name><name sortKey="Zhang, Jianpeng" sort="Zhang, Jianpeng" uniqKey="Zhang J" first="Jianpeng" last="Zhang">Jianpeng Zhang</name><name sortKey="Zhang, Jing" sort="Zhang, Jing" uniqKey="Zhang J" first="Jing" last="Zhang">Jing Zhang</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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