Activation of neuronal extracellular receptor kinase (ERK) in Alzheimer disease links oxidative stress to abnormal phosphorylation
Responses to increased oxidative stress may be the common mechanism responsible for the varied cytopathology of Alzheimer disease (AD). A possible link in support of this hypothesis is that one of the most striking features of AD, the abnormal accumulation of highly phosphorylated τ and neurofilamen...
Gespeichert in:
| Veröffentlicht in: | Neuroreport 1999-08, Vol.10 (11), p.2411-2415 |
|---|---|
| Hauptverfasser: | , , , , , , , , , , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 2415 |
|---|---|
| container_issue | 11 |
| container_start_page | 2411 |
| container_title | Neuroreport |
| container_volume | 10 |
| creator | Perry, George Roder, Hanno Nunomura, Akihiko Takeda, Atsushi Friedlich, Avi L Zhu, Xiongwei Raina, Arun K Holbrook, Nikki Siedlak, Sandra L Harris, Peggy L. R Smith, Mark A |
| description | Responses to increased oxidative stress may be the common mechanism responsible for the varied cytopathology of Alzheimer disease (AD). A possible link in support of this hypothesis is that one of the most striking features of AD, the abnormal accumulation of highly phosphorylated τ and neurofilament proteins, may be brought about by extracellular receptor kinase (ERK) whose activation is a common response to oxidative stress. In this study, we demonstrate that activated ERK is specifically increased in the same vulnerable neurons in AD that are the site of oxidative damage and abnormal phosphorylation. These findings suggest that ERK dysregulation, likely resulting from oxidative stress, could play an important role in the increased phosphorylation of cytoskeletal proteins observed in AD. |
| doi_str_mv | 10.1097/00001756-199908020-00035 |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_69950606</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>17382100</sourcerecordid><originalsourceid>FETCH-LOGICAL-c4825-9b3314c755bbc2ff89cc3af2d4eec844c33e5d631d28d9f20ad39620b96d39963</originalsourceid><addsrcrecordid>eNqFkl1vFCEUhomxsdvVv2C4MKa9mAoDzAyXm6Z-xCYmRhPvCMOcyeIysALTDy_95bLdbfXGSHLCCTznPeG8IIQpOadEtm9IWbQVTUWllKQjNanKCRNP0ILyllVCdN-eogWRQlZcNuIYnaT0vSCS0O4ZOqaEM1nABfq1Mtle62yDx2HEHuYYvHYYbnPUBpybnY44goFtDhFvrNcJ8Onl549n2Hq8cj_XYCeIeLAJdlfO-k3C4dYORfQacMoRUsI5YN37EKeivV2HVCLeufu-z9HRqF2CF4d9ib6-vfxy8b66-vTuw8XqqjK8q0Ule8YoN60QfW_qceykMUyP9cABTMe5YQzE0DA61N0gx5rogcmmJr1sSiIbtkSv97rbGH7MkLKabNo9UXsIc1KNlII05P8gbVlX0zLvJer2oIkhpQij2kY76XinKFE7o9SDUerRKHVvVCl9eegx9xMMfxXunSnAqwOgk9FujNobm_5wkpC25QXje-wmuAwxbdx8A1GtQbu8Vv_6J-w3ze2tGw</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>17382100</pqid></control><display><type>article</type><title>Activation of neuronal extracellular receptor kinase (ERK) in Alzheimer disease links oxidative stress to abnormal phosphorylation</title><source>MEDLINE</source><source>Journals@Ovid Complete</source><creator>Perry, George ; Roder, Hanno ; Nunomura, Akihiko ; Takeda, Atsushi ; Friedlich, Avi L ; Zhu, Xiongwei ; Raina, Arun K ; Holbrook, Nikki ; Siedlak, Sandra L ; Harris, Peggy L. R ; Smith, Mark A</creator><creatorcontrib>Perry, George ; Roder, Hanno ; Nunomura, Akihiko ; Takeda, Atsushi ; Friedlich, Avi L ; Zhu, Xiongwei ; Raina, Arun K ; Holbrook, Nikki ; Siedlak, Sandra L ; Harris, Peggy L. R ; Smith, Mark A</creatorcontrib><description>Responses to increased oxidative stress may be the common mechanism responsible for the varied cytopathology of Alzheimer disease (AD). A possible link in support of this hypothesis is that one of the most striking features of AD, the abnormal accumulation of highly phosphorylated τ and neurofilament proteins, may be brought about by extracellular receptor kinase (ERK) whose activation is a common response to oxidative stress. In this study, we demonstrate that activated ERK is specifically increased in the same vulnerable neurons in AD that are the site of oxidative damage and abnormal phosphorylation. These findings suggest that ERK dysregulation, likely resulting from oxidative stress, could play an important role in the increased phosphorylation of cytoskeletal proteins observed in AD.</description><identifier>ISSN: 0959-4965</identifier><identifier>EISSN: 1473-558X</identifier><identifier>DOI: 10.1097/00001756-199908020-00035</identifier><identifier>PMID: 10439473</identifier><language>eng</language><publisher>Hagerstown, MD: Lippincott Williams & Wilkins, Inc</publisher><subject>Adult ; Aged ; Alzheimer Disease - enzymology ; Alzheimer Disease - metabolism ; Alzheimer Disease - pathology ; Biological and medical sciences ; Brain - enzymology ; Brain - metabolism ; Brain - pathology ; Calcium-Calmodulin-Dependent Protein Kinases - metabolism ; Degenerative and inherited degenerative diseases of the nervous system. Leukodystrophies. Prion diseases ; Enzyme Activation - physiology ; extracellular signal-regulated kinase ; Humans ; Medical sciences ; Middle Aged ; Neurology ; Neurons - enzymology ; Neurons - metabolism ; Oxidative Stress - physiology ; Phosphorylation ; tau Proteins - metabolism</subject><ispartof>Neuroreport, 1999-08, Vol.10 (11), p.2411-2415</ispartof><rights>1999 Lippincott Williams & Wilkins, Inc.</rights><rights>1999 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c4825-9b3314c755bbc2ff89cc3af2d4eec844c33e5d631d28d9f20ad39620b96d39963</citedby><cites>FETCH-LOGICAL-c4825-9b3314c755bbc2ff89cc3af2d4eec844c33e5d631d28d9f20ad39620b96d39963</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780,27901,27902</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=1900774$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/10439473$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Perry, George</creatorcontrib><creatorcontrib>Roder, Hanno</creatorcontrib><creatorcontrib>Nunomura, Akihiko</creatorcontrib><creatorcontrib>Takeda, Atsushi</creatorcontrib><creatorcontrib>Friedlich, Avi L</creatorcontrib><creatorcontrib>Zhu, Xiongwei</creatorcontrib><creatorcontrib>Raina, Arun K</creatorcontrib><creatorcontrib>Holbrook, Nikki</creatorcontrib><creatorcontrib>Siedlak, Sandra L</creatorcontrib><creatorcontrib>Harris, Peggy L. R</creatorcontrib><creatorcontrib>Smith, Mark A</creatorcontrib><title>Activation of neuronal extracellular receptor kinase (ERK) in Alzheimer disease links oxidative stress to abnormal phosphorylation</title><title>Neuroreport</title><addtitle>Neuroreport</addtitle><description>Responses to increased oxidative stress may be the common mechanism responsible for the varied cytopathology of Alzheimer disease (AD). A possible link in support of this hypothesis is that one of the most striking features of AD, the abnormal accumulation of highly phosphorylated τ and neurofilament proteins, may be brought about by extracellular receptor kinase (ERK) whose activation is a common response to oxidative stress. In this study, we demonstrate that activated ERK is specifically increased in the same vulnerable neurons in AD that are the site of oxidative damage and abnormal phosphorylation. These findings suggest that ERK dysregulation, likely resulting from oxidative stress, could play an important role in the increased phosphorylation of cytoskeletal proteins observed in AD.</description><subject>Adult</subject><subject>Aged</subject><subject>Alzheimer Disease - enzymology</subject><subject>Alzheimer Disease - metabolism</subject><subject>Alzheimer Disease - pathology</subject><subject>Biological and medical sciences</subject><subject>Brain - enzymology</subject><subject>Brain - metabolism</subject><subject>Brain - pathology</subject><subject>Calcium-Calmodulin-Dependent Protein Kinases - metabolism</subject><subject>Degenerative and inherited degenerative diseases of the nervous system. Leukodystrophies. Prion diseases</subject><subject>Enzyme Activation - physiology</subject><subject>extracellular signal-regulated kinase</subject><subject>Humans</subject><subject>Medical sciences</subject><subject>Middle Aged</subject><subject>Neurology</subject><subject>Neurons - enzymology</subject><subject>Neurons - metabolism</subject><subject>Oxidative Stress - physiology</subject><subject>Phosphorylation</subject><subject>tau Proteins - metabolism</subject><issn>0959-4965</issn><issn>1473-558X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1999</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkl1vFCEUhomxsdvVv2C4MKa9mAoDzAyXm6Z-xCYmRhPvCMOcyeIysALTDy_95bLdbfXGSHLCCTznPeG8IIQpOadEtm9IWbQVTUWllKQjNanKCRNP0ILyllVCdN-eogWRQlZcNuIYnaT0vSCS0O4ZOqaEM1nABfq1Mtle62yDx2HEHuYYvHYYbnPUBpybnY44goFtDhFvrNcJ8Onl549n2Hq8cj_XYCeIeLAJdlfO-k3C4dYORfQacMoRUsI5YN37EKeivV2HVCLeufu-z9HRqF2CF4d9ib6-vfxy8b66-vTuw8XqqjK8q0Ule8YoN60QfW_qceykMUyP9cABTMe5YQzE0DA61N0gx5rogcmmJr1sSiIbtkSv97rbGH7MkLKabNo9UXsIc1KNlII05P8gbVlX0zLvJer2oIkhpQij2kY76XinKFE7o9SDUerRKHVvVCl9eegx9xMMfxXunSnAqwOgk9FujNobm_5wkpC25QXje-wmuAwxbdx8A1GtQbu8Vv_6J-w3ze2tGw</recordid><startdate>19990802</startdate><enddate>19990802</enddate><creator>Perry, George</creator><creator>Roder, Hanno</creator><creator>Nunomura, Akihiko</creator><creator>Takeda, Atsushi</creator><creator>Friedlich, Avi L</creator><creator>Zhu, Xiongwei</creator><creator>Raina, Arun K</creator><creator>Holbrook, Nikki</creator><creator>Siedlak, Sandra L</creator><creator>Harris, Peggy L. R</creator><creator>Smith, Mark A</creator><general>Lippincott Williams & Wilkins, Inc</general><general>Lippincott Williams and Wilkins</general><scope>IQODW</scope><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>7TK</scope><scope>7X8</scope></search><sort><creationdate>19990802</creationdate><title>Activation of neuronal extracellular receptor kinase (ERK) in Alzheimer disease links oxidative stress to abnormal phosphorylation</title><author>Perry, George ; Roder, Hanno ; Nunomura, Akihiko ; Takeda, Atsushi ; Friedlich, Avi L ; Zhu, Xiongwei ; Raina, Arun K ; Holbrook, Nikki ; Siedlak, Sandra L ; Harris, Peggy L. R ; Smith, Mark A</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4825-9b3314c755bbc2ff89cc3af2d4eec844c33e5d631d28d9f20ad39620b96d39963</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1999</creationdate><topic>Adult</topic><topic>Aged</topic><topic>Alzheimer Disease - enzymology</topic><topic>Alzheimer Disease - metabolism</topic><topic>Alzheimer Disease - pathology</topic><topic>Biological and medical sciences</topic><topic>Brain - enzymology</topic><topic>Brain - metabolism</topic><topic>Brain - pathology</topic><topic>Calcium-Calmodulin-Dependent Protein Kinases - metabolism</topic><topic>Degenerative and inherited degenerative diseases of the nervous system. Leukodystrophies. Prion diseases</topic><topic>Enzyme Activation - physiology</topic><topic>extracellular signal-regulated kinase</topic><topic>Humans</topic><topic>Medical sciences</topic><topic>Middle Aged</topic><topic>Neurology</topic><topic>Neurons - enzymology</topic><topic>Neurons - metabolism</topic><topic>Oxidative Stress - physiology</topic><topic>Phosphorylation</topic><topic>tau Proteins - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Perry, George</creatorcontrib><creatorcontrib>Roder, Hanno</creatorcontrib><creatorcontrib>Nunomura, Akihiko</creatorcontrib><creatorcontrib>Takeda, Atsushi</creatorcontrib><creatorcontrib>Friedlich, Avi L</creatorcontrib><creatorcontrib>Zhu, Xiongwei</creatorcontrib><creatorcontrib>Raina, Arun K</creatorcontrib><creatorcontrib>Holbrook, Nikki</creatorcontrib><creatorcontrib>Siedlak, Sandra L</creatorcontrib><creatorcontrib>Harris, Peggy L. R</creatorcontrib><creatorcontrib>Smith, Mark A</creatorcontrib><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Neurosciences Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Neuroreport</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Perry, George</au><au>Roder, Hanno</au><au>Nunomura, Akihiko</au><au>Takeda, Atsushi</au><au>Friedlich, Avi L</au><au>Zhu, Xiongwei</au><au>Raina, Arun K</au><au>Holbrook, Nikki</au><au>Siedlak, Sandra L</au><au>Harris, Peggy L. R</au><au>Smith, Mark A</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Activation of neuronal extracellular receptor kinase (ERK) in Alzheimer disease links oxidative stress to abnormal phosphorylation</atitle><jtitle>Neuroreport</jtitle><addtitle>Neuroreport</addtitle><date>1999-08-02</date><risdate>1999</risdate><volume>10</volume><issue>11</issue><spage>2411</spage><epage>2415</epage><pages>2411-2415</pages><issn>0959-4965</issn><eissn>1473-558X</eissn><abstract>Responses to increased oxidative stress may be the common mechanism responsible for the varied cytopathology of Alzheimer disease (AD). A possible link in support of this hypothesis is that one of the most striking features of AD, the abnormal accumulation of highly phosphorylated τ and neurofilament proteins, may be brought about by extracellular receptor kinase (ERK) whose activation is a common response to oxidative stress. In this study, we demonstrate that activated ERK is specifically increased in the same vulnerable neurons in AD that are the site of oxidative damage and abnormal phosphorylation. These findings suggest that ERK dysregulation, likely resulting from oxidative stress, could play an important role in the increased phosphorylation of cytoskeletal proteins observed in AD.</abstract><cop>Hagerstown, MD</cop><pub>Lippincott Williams & Wilkins, Inc</pub><pmid>10439473</pmid><doi>10.1097/00001756-199908020-00035</doi><tpages>5</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0959-4965 |
| ispartof | Neuroreport, 1999-08, Vol.10 (11), p.2411-2415 |
| issn | 0959-4965 1473-558X |
| language | eng |
| recordid | cdi_proquest_miscellaneous_69950606 |
| source | MEDLINE; Journals@Ovid Complete |
| subjects | Adult Aged Alzheimer Disease - enzymology Alzheimer Disease - metabolism Alzheimer Disease - pathology Biological and medical sciences Brain - enzymology Brain - metabolism Brain - pathology Calcium-Calmodulin-Dependent Protein Kinases - metabolism Degenerative and inherited degenerative diseases of the nervous system. Leukodystrophies. Prion diseases Enzyme Activation - physiology extracellular signal-regulated kinase Humans Medical sciences Middle Aged Neurology Neurons - enzymology Neurons - metabolism Oxidative Stress - physiology Phosphorylation tau Proteins - metabolism |
| title | Activation of neuronal extracellular receptor kinase (ERK) in Alzheimer disease links oxidative stress to abnormal phosphorylation |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-31T09%3A58%3A19IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_cross&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Activation%20of%20neuronal%20extracellular%20receptor%20kinase%20(ERK)%20in%20Alzheimer%20disease%20links%20oxidative%20stress%20to%20abnormal%20phosphorylation&rft.jtitle=Neuroreport&rft.au=Perry,%20George&rft.date=1999-08-02&rft.volume=10&rft.issue=11&rft.spage=2411&rft.epage=2415&rft.pages=2411-2415&rft.issn=0959-4965&rft.eissn=1473-558X&rft_id=info:doi/10.1097/00001756-199908020-00035&rft_dat=%3Cproquest_cross%3E17382100%3C/proquest_cross%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=17382100&rft_id=info:pmid/10439473&rfr_iscdi=true |