Interplay between protein glycosylation pathways in Alzheimer's disease
Deviations from the normal nucleoplasmic protein O-GlcNAcylation, as well as from normal protein sialylation and N-glycosylation in the secretory pathway, have been reported in Alzheimer's disease (AD). However, the interplay between the cytoplasmic protein -GlcNAcylation and the secretory N-/O...
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| Veröffentlicht in: | Science advances 2017-09, Vol.3 (9), p.e1601576-e1601576 |
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| container_title | Science advances |
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| creator | Frenkel-Pinter, Moran Shmueli, Merav Daniel Raz, Chen Yanku, Michaela Zilberzwige, Shai Gazit, Ehud Segal, Daniel |
| description | Deviations from the normal nucleoplasmic protein O-GlcNAcylation, as well as from normal protein sialylation and N-glycosylation in the secretory pathway, have been reported in Alzheimer's disease (AD). However, the interplay between the cytoplasmic protein
-GlcNAcylation and the secretory N-/O-glycosylation in AD has not been described. We present a comprehensive analysis of the N-, O-, and
-GlcNAc-glycomes in AD-affected brain regions as well as in AD patient serum. We detected marked differences in levels of glycan involved in both protein
-GlcNAcylation and N-/O-glycosylation between patients and healthy individuals and revealed brain region-specific glycosylation-related pathology in patients. These alterations are not general for other neurodegenerative conditions, such as frontotemporal dementia and corticobasal degeneration. The alterations in the AD glycome in the serum could potentially lead to novel glyco-based biomarkers for AD progression. Strikingly, negative interrelationship was found between the pathways of protein
-GlcNAcylation and N-/O-glycosylation, suggesting a novel intracellular cross-talk. |
| doi_str_mv | 10.1126/sciadv.1601576 |
| format | Article |
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-GlcNAcylation and the secretory N-/O-glycosylation in AD has not been described. We present a comprehensive analysis of the N-, O-, and
-GlcNAc-glycomes in AD-affected brain regions as well as in AD patient serum. We detected marked differences in levels of glycan involved in both protein
-GlcNAcylation and N-/O-glycosylation between patients and healthy individuals and revealed brain region-specific glycosylation-related pathology in patients. These alterations are not general for other neurodegenerative conditions, such as frontotemporal dementia and corticobasal degeneration. The alterations in the AD glycome in the serum could potentially lead to novel glyco-based biomarkers for AD progression. Strikingly, negative interrelationship was found between the pathways of protein
-GlcNAcylation and N-/O-glycosylation, suggesting a novel intracellular cross-talk.</description><identifier>ISSN: 2375-2548</identifier><identifier>EISSN: 2375-2548</identifier><identifier>DOI: 10.1126/sciadv.1601576</identifier><identifier>PMID: 28929132</identifier><language>eng</language><publisher>United States: American Association for the Advancement of Science</publisher><subject>Aged ; Aged, 80 and over ; Alzheimer Disease - blood ; Alzheimer Disease - metabolism ; Alzheimer Disease - pathology ; Biomarkers ; Brain - metabolism ; Brain - pathology ; Case-Control Studies ; Female ; Glycobiology ; Glycosylation ; Humans ; Male ; Middle Aged ; Neuroscience ; Protein Processing, Post-Translational ; Proteome ; Proteomics - methods ; SciAdv r-articles ; Signal Transduction</subject><ispartof>Science advances, 2017-09, Vol.3 (9), p.e1601576-e1601576</ispartof><rights>Copyright © 2017 The Authors, some rights reserved; exclusive licensee American Association for the Advancement of Science. No claim to original U.S. Government Works. Distributed under a Creative Commons Attribution NonCommercial License 4.0 (CC BY-NC). 2017 The Authors</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c456t-4d0b8ba317d86c1215caed6e57f5d1b06d48355821a33bc6646cff7e4f111d2d3</citedby><cites>FETCH-LOGICAL-c456t-4d0b8ba317d86c1215caed6e57f5d1b06d48355821a33bc6646cff7e4f111d2d3</cites><orcidid>0000-0002-6777-505X ; 0000-0001-5764-1720</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC5600531/pdf/$$EPDF$$P50$$Gpubmedcentral$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC5600531/$$EHTML$$P50$$Gpubmedcentral$$Hfree_for_read</linktohtml><link.rule.ids>230,314,723,776,780,860,881,27901,27902,53766,53768</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/28929132$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Frenkel-Pinter, Moran</creatorcontrib><creatorcontrib>Shmueli, Merav Daniel</creatorcontrib><creatorcontrib>Raz, Chen</creatorcontrib><creatorcontrib>Yanku, Michaela</creatorcontrib><creatorcontrib>Zilberzwige, Shai</creatorcontrib><creatorcontrib>Gazit, Ehud</creatorcontrib><creatorcontrib>Segal, Daniel</creatorcontrib><title>Interplay between protein glycosylation pathways in Alzheimer's disease</title><title>Science advances</title><addtitle>Sci Adv</addtitle><description>Deviations from the normal nucleoplasmic protein O-GlcNAcylation, as well as from normal protein sialylation and N-glycosylation in the secretory pathway, have been reported in Alzheimer's disease (AD). However, the interplay between the cytoplasmic protein
-GlcNAcylation and the secretory N-/O-glycosylation in AD has not been described. We present a comprehensive analysis of the N-, O-, and
-GlcNAc-glycomes in AD-affected brain regions as well as in AD patient serum. We detected marked differences in levels of glycan involved in both protein
-GlcNAcylation and N-/O-glycosylation between patients and healthy individuals and revealed brain region-specific glycosylation-related pathology in patients. These alterations are not general for other neurodegenerative conditions, such as frontotemporal dementia and corticobasal degeneration. The alterations in the AD glycome in the serum could potentially lead to novel glyco-based biomarkers for AD progression. Strikingly, negative interrelationship was found between the pathways of protein
-GlcNAcylation and N-/O-glycosylation, suggesting a novel intracellular cross-talk.</description><subject>Aged</subject><subject>Aged, 80 and over</subject><subject>Alzheimer Disease - blood</subject><subject>Alzheimer Disease - metabolism</subject><subject>Alzheimer Disease - pathology</subject><subject>Biomarkers</subject><subject>Brain - metabolism</subject><subject>Brain - pathology</subject><subject>Case-Control Studies</subject><subject>Female</subject><subject>Glycobiology</subject><subject>Glycosylation</subject><subject>Humans</subject><subject>Male</subject><subject>Middle Aged</subject><subject>Neuroscience</subject><subject>Protein Processing, Post-Translational</subject><subject>Proteome</subject><subject>Proteomics - methods</subject><subject>SciAdv r-articles</subject><subject>Signal Transduction</subject><issn>2375-2548</issn><issn>2375-2548</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2017</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpVUcFOAjEQbYxGCHL1aPamF7DTbru7FxNCFElIvOi56bazULPsYrtA1q93DUjwNJN5b96bzCPkFugYgMnHYJy2uzFICiKRF6TPeCJGTMTp5VnfI8MQPimlEEspILsmPZZmLAPO-mQ2rxr0m1K3UY7NHrGKNr5u0FXRsmxNHdpSN67uprpZ7XUbog6ZlN8rdGv09yGyLqAOeEOuCl0GHB7rgHy8PL9PX0eLt9l8OlmMTCxkM4otzdNcc0hsKg0wEEajlSiSQljIqbRxyoVIGWjOcyNlLE1RJBgXAGCZ5QPydNDdbPM1WoNV43WpNt6ttW9VrZ36j1RupZb1TglJqeDQCTwcBXz9tcXQqLULBstSV1hvg4IsBprRRKQddXygGl-H4LE42QBVvwGoQwDqGEC3cHd-3In-927-A1WDhE0</recordid><startdate>20170901</startdate><enddate>20170901</enddate><creator>Frenkel-Pinter, Moran</creator><creator>Shmueli, Merav Daniel</creator><creator>Raz, Chen</creator><creator>Yanku, Michaela</creator><creator>Zilberzwige, Shai</creator><creator>Gazit, Ehud</creator><creator>Segal, Daniel</creator><general>American Association for the Advancement of Science</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope><scope>5PM</scope><orcidid>https://orcid.org/0000-0002-6777-505X</orcidid><orcidid>https://orcid.org/0000-0001-5764-1720</orcidid></search><sort><creationdate>20170901</creationdate><title>Interplay between protein glycosylation pathways in Alzheimer's disease</title><author>Frenkel-Pinter, Moran ; Shmueli, Merav Daniel ; Raz, Chen ; Yanku, Michaela ; Zilberzwige, Shai ; Gazit, Ehud ; Segal, Daniel</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c456t-4d0b8ba317d86c1215caed6e57f5d1b06d48355821a33bc6646cff7e4f111d2d3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2017</creationdate><topic>Aged</topic><topic>Aged, 80 and over</topic><topic>Alzheimer Disease - blood</topic><topic>Alzheimer Disease - metabolism</topic><topic>Alzheimer Disease - pathology</topic><topic>Biomarkers</topic><topic>Brain - metabolism</topic><topic>Brain - pathology</topic><topic>Case-Control Studies</topic><topic>Female</topic><topic>Glycobiology</topic><topic>Glycosylation</topic><topic>Humans</topic><topic>Male</topic><topic>Middle Aged</topic><topic>Neuroscience</topic><topic>Protein Processing, Post-Translational</topic><topic>Proteome</topic><topic>Proteomics - methods</topic><topic>SciAdv r-articles</topic><topic>Signal Transduction</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Frenkel-Pinter, Moran</creatorcontrib><creatorcontrib>Shmueli, Merav Daniel</creatorcontrib><creatorcontrib>Raz, Chen</creatorcontrib><creatorcontrib>Yanku, Michaela</creatorcontrib><creatorcontrib>Zilberzwige, Shai</creatorcontrib><creatorcontrib>Gazit, Ehud</creatorcontrib><creatorcontrib>Segal, Daniel</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Science advances</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Frenkel-Pinter, Moran</au><au>Shmueli, Merav Daniel</au><au>Raz, Chen</au><au>Yanku, Michaela</au><au>Zilberzwige, Shai</au><au>Gazit, Ehud</au><au>Segal, Daniel</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Interplay between protein glycosylation pathways in Alzheimer's disease</atitle><jtitle>Science advances</jtitle><addtitle>Sci Adv</addtitle><date>2017-09-01</date><risdate>2017</risdate><volume>3</volume><issue>9</issue><spage>e1601576</spage><epage>e1601576</epage><pages>e1601576-e1601576</pages><issn>2375-2548</issn><eissn>2375-2548</eissn><abstract>Deviations from the normal nucleoplasmic protein O-GlcNAcylation, as well as from normal protein sialylation and N-glycosylation in the secretory pathway, have been reported in Alzheimer's disease (AD). However, the interplay between the cytoplasmic protein
-GlcNAcylation and the secretory N-/O-glycosylation in AD has not been described. We present a comprehensive analysis of the N-, O-, and
-GlcNAc-glycomes in AD-affected brain regions as well as in AD patient serum. We detected marked differences in levels of glycan involved in both protein
-GlcNAcylation and N-/O-glycosylation between patients and healthy individuals and revealed brain region-specific glycosylation-related pathology in patients. These alterations are not general for other neurodegenerative conditions, such as frontotemporal dementia and corticobasal degeneration. The alterations in the AD glycome in the serum could potentially lead to novel glyco-based biomarkers for AD progression. Strikingly, negative interrelationship was found between the pathways of protein
-GlcNAcylation and N-/O-glycosylation, suggesting a novel intracellular cross-talk.</abstract><cop>United States</cop><pub>American Association for the Advancement of Science</pub><pmid>28929132</pmid><doi>10.1126/sciadv.1601576</doi><orcidid>https://orcid.org/0000-0002-6777-505X</orcidid><orcidid>https://orcid.org/0000-0001-5764-1720</orcidid><oa>free_for_read</oa></addata></record> |
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| source | MEDLINE; DOAJ Directory of Open Access Journals; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; PubMed Central |
| subjects | Aged Aged, 80 and over Alzheimer Disease - blood Alzheimer Disease - metabolism Alzheimer Disease - pathology Biomarkers Brain - metabolism Brain - pathology Case-Control Studies Female Glycobiology Glycosylation Humans Male Middle Aged Neuroscience Protein Processing, Post-Translational Proteome Proteomics - methods SciAdv r-articles Signal Transduction |
| title | Interplay between protein glycosylation pathways in Alzheimer's disease |
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