Application of synthetic phospho- and unphospho- peptides to identify phosphorylation sites in a subregion of the tau molecule, which is modified in Alzheimer's disease
Phospho‐ and unphospho‐ peptides were used to define the essential sequence for a tau epitope, which is recognized by Tau‐1 antibody and phosphorylated in Alzheimer's disease (AD). The epitope was mapped within the amino acid residues 192–199 of tau and was phosphorylated by the p34cdc2/p58cycl...
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| Veröffentlicht in: | Journal of neuroscience research 1993-02, Vol.34 (3), p.371-376 |
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| container_title | Journal of neuroscience research |
| container_volume | 34 |
| creator | Liu, W.-K. Moore, W. T. Williams, R. T. Hall, F. L. Yen, Shu-Hui |
| description | Phospho‐ and unphospho‐ peptides were used to define the essential sequence for a tau epitope, which is recognized by Tau‐1 antibody and phosphorylated in Alzheimer's disease (AD). The epitope was mapped within the amino acid residues 192–199 of tau and was phosphorylated by the p34cdc2/p58cyclin A proline directed kinase (PDPK), but not by purified mitogen activated protein kinase (p42mapk). Addition of phosphate to the last serine of the epitope was the most effective in abolishing the reactivity of the epitope to Tau‐1 antibody. Our results suggest that one and possibly more members of the PDPK family may play a role in the pathogenesis of AD. © 1993 Wiley‐Liss, Inc. |
| doi_str_mv | 10.1002/jnr.490340315 |
| format | Article |
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T. ; Williams, R. T. ; Hall, F. L. ; Yen, Shu-Hui</creator><creatorcontrib>Liu, W.-K. ; Moore, W. T. ; Williams, R. T. ; Hall, F. L. ; Yen, Shu-Hui</creatorcontrib><description>Phospho‐ and unphospho‐ peptides were used to define the essential sequence for a tau epitope, which is recognized by Tau‐1 antibody and phosphorylated in Alzheimer's disease (AD). The epitope was mapped within the amino acid residues 192–199 of tau and was phosphorylated by the p34cdc2/p58cyclin A proline directed kinase (PDPK), but not by purified mitogen activated protein kinase (p42mapk). Addition of phosphate to the last serine of the epitope was the most effective in abolishing the reactivity of the epitope to Tau‐1 antibody. Our results suggest that one and possibly more members of the PDPK family may play a role in the pathogenesis of AD. © 1993 Wiley‐Liss, Inc.</description><identifier>ISSN: 0360-4012</identifier><identifier>EISSN: 1097-4547</identifier><identifier>DOI: 10.1002/jnr.490340315</identifier><identifier>PMID: 8455212</identifier><identifier>CODEN: JNREDK</identifier><language>eng</language><publisher>Hoboken: Wiley Subscription Services, Inc., A Wiley Company</publisher><subject>Alzheimer Disease - metabolism ; Amino Acid Sequence ; Biological and medical sciences ; Degenerative and inherited degenerative diseases of the nervous system. Leukodystrophies. Prion diseases ; DNA ; Enzyme-Linked Immunosorbent Assay ; Humans ; Medical sciences ; Molecular Sequence Data ; Neurology ; Neuropeptides - metabolism ; Phosphopeptides - metabolism ; Phosphorylation ; Proline-Directed Protein Kinases ; Protein Kinases - isolation & purification ; Protein Kinases - metabolism ; tau Proteins - chemistry ; tau Proteins - immunology ; tau Proteins - metabolism</subject><ispartof>Journal of neuroscience research, 1993-02, Vol.34 (3), p.371-376</ispartof><rights>Copyright © 1993 Wiley‐Liss, Inc.</rights><rights>1993 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c3495-72cf719271260eb10e9c68f13e343c228aade665a5bffb01b14719eb6cfadb523</citedby><cites>FETCH-LOGICAL-c3495-72cf719271260eb10e9c68f13e343c228aade665a5bffb01b14719eb6cfadb523</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1002%2Fjnr.490340315$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://onlinelibrary.wiley.com/doi/full/10.1002%2Fjnr.490340315$$EHTML$$P50$$Gwiley$$H</linktohtml><link.rule.ids>314,776,780,1411,27903,27904,45553,45554</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=4582949$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/8455212$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Liu, W.-K.</creatorcontrib><creatorcontrib>Moore, W. T.</creatorcontrib><creatorcontrib>Williams, R. T.</creatorcontrib><creatorcontrib>Hall, F. L.</creatorcontrib><creatorcontrib>Yen, Shu-Hui</creatorcontrib><title>Application of synthetic phospho- and unphospho- peptides to identify phosphorylation sites in a subregion of the tau molecule, which is modified in Alzheimer's disease</title><title>Journal of neuroscience research</title><addtitle>J. Neurosci. Res</addtitle><description>Phospho‐ and unphospho‐ peptides were used to define the essential sequence for a tau epitope, which is recognized by Tau‐1 antibody and phosphorylated in Alzheimer's disease (AD). The epitope was mapped within the amino acid residues 192–199 of tau and was phosphorylated by the p34cdc2/p58cyclin A proline directed kinase (PDPK), but not by purified mitogen activated protein kinase (p42mapk). Addition of phosphate to the last serine of the epitope was the most effective in abolishing the reactivity of the epitope to Tau‐1 antibody. Our results suggest that one and possibly more members of the PDPK family may play a role in the pathogenesis of AD. © 1993 Wiley‐Liss, Inc.</description><subject>Alzheimer Disease - metabolism</subject><subject>Amino Acid Sequence</subject><subject>Biological and medical sciences</subject><subject>Degenerative and inherited degenerative diseases of the nervous system. Leukodystrophies. Prion diseases</subject><subject>DNA</subject><subject>Enzyme-Linked Immunosorbent Assay</subject><subject>Humans</subject><subject>Medical sciences</subject><subject>Molecular Sequence Data</subject><subject>Neurology</subject><subject>Neuropeptides - metabolism</subject><subject>Phosphopeptides - metabolism</subject><subject>Phosphorylation</subject><subject>Proline-Directed Protein Kinases</subject><subject>Protein Kinases - isolation & purification</subject><subject>Protein Kinases - metabolism</subject><subject>tau Proteins - chemistry</subject><subject>tau Proteins - immunology</subject><subject>tau Proteins - metabolism</subject><issn>0360-4012</issn><issn>1097-4547</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1993</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkU1v1DAQhiNEVZbCkSOSDwgupPgzXh9XFbttVYrEh5C4WI4zJi7ZJNiJSvhF_ExcNkSc4GCN7Hnm8Uhvlj0h-JRgTF_dtOGUK8w4ZkTcy1YEK5lzweX9bIVZgXOOCX2QPYzxBmOslGDH2fGaC0EJXWU_N33feGsG37WocyhO7VDD4C3q6y6mkyPTVmhsl2sP_eAriGjoUKrt4N30Bw5TczBFPyTCt8igOJYBvsz65EaDGdG-a8CODbxEt7W3NfIxPVXeeajupjbNjxr8HsKLiCofwUR4lB0500R4PNeT7OP29Yez8_zq7e7ibHOVW8aVyCW1ThJFJaEFhpJgULZYO8KAcWYpXRtTQVEII0rnSkxKwhMOZWGdqUpB2Un2_ODtQ_dthDjovY8Wmsa00I1RS1EwSZj8L0gKrqT6DeYH0IYuxgBO98HvTZg0wfouQp0i1EuEiX86i8dyD9VCz5ml_rO5b6I1jQumtT4uGBdrqrhKmDxgt76B6d9_6svrd38vMC_s4wDfl0kTvupCMin0p-udfv95u31zuTvXlP0C0UvG7g</recordid><startdate>19930215</startdate><enddate>19930215</enddate><creator>Liu, W.-K.</creator><creator>Moore, W. T.</creator><creator>Williams, R. T.</creator><creator>Hall, F. L.</creator><creator>Yen, Shu-Hui</creator><general>Wiley Subscription Services, Inc., A Wiley Company</general><general>Wiley-Liss</general><scope>BSCLL</scope><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>19930215</creationdate><title>Application of synthetic phospho- and unphospho- peptides to identify phosphorylation sites in a subregion of the tau molecule, which is modified in Alzheimer's disease</title><author>Liu, W.-K. ; Moore, W. T. ; Williams, R. T. ; Hall, F. L. ; Yen, Shu-Hui</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c3495-72cf719271260eb10e9c68f13e343c228aade665a5bffb01b14719eb6cfadb523</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1993</creationdate><topic>Alzheimer Disease - metabolism</topic><topic>Amino Acid Sequence</topic><topic>Biological and medical sciences</topic><topic>Degenerative and inherited degenerative diseases of the nervous system. Leukodystrophies. Prion diseases</topic><topic>DNA</topic><topic>Enzyme-Linked Immunosorbent Assay</topic><topic>Humans</topic><topic>Medical sciences</topic><topic>Molecular Sequence Data</topic><topic>Neurology</topic><topic>Neuropeptides - metabolism</topic><topic>Phosphopeptides - metabolism</topic><topic>Phosphorylation</topic><topic>Proline-Directed Protein Kinases</topic><topic>Protein Kinases - isolation & purification</topic><topic>Protein Kinases - metabolism</topic><topic>tau Proteins - chemistry</topic><topic>tau Proteins - immunology</topic><topic>tau Proteins - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Liu, W.-K.</creatorcontrib><creatorcontrib>Moore, W. T.</creatorcontrib><creatorcontrib>Williams, R. T.</creatorcontrib><creatorcontrib>Hall, F. 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L.</au><au>Yen, Shu-Hui</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Application of synthetic phospho- and unphospho- peptides to identify phosphorylation sites in a subregion of the tau molecule, which is modified in Alzheimer's disease</atitle><jtitle>Journal of neuroscience research</jtitle><addtitle>J. Neurosci. Res</addtitle><date>1993-02-15</date><risdate>1993</risdate><volume>34</volume><issue>3</issue><spage>371</spage><epage>376</epage><pages>371-376</pages><issn>0360-4012</issn><eissn>1097-4547</eissn><coden>JNREDK</coden><abstract>Phospho‐ and unphospho‐ peptides were used to define the essential sequence for a tau epitope, which is recognized by Tau‐1 antibody and phosphorylated in Alzheimer's disease (AD). The epitope was mapped within the amino acid residues 192–199 of tau and was phosphorylated by the p34cdc2/p58cyclin A proline directed kinase (PDPK), but not by purified mitogen activated protein kinase (p42mapk). Addition of phosphate to the last serine of the epitope was the most effective in abolishing the reactivity of the epitope to Tau‐1 antibody. Our results suggest that one and possibly more members of the PDPK family may play a role in the pathogenesis of AD. © 1993 Wiley‐Liss, Inc.</abstract><cop>Hoboken</cop><pub>Wiley Subscription Services, Inc., A Wiley Company</pub><pmid>8455212</pmid><doi>10.1002/jnr.490340315</doi><tpages>6</tpages></addata></record> |
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| source | MEDLINE; Wiley Online Library Journals Frontfile Complete |
| subjects | Alzheimer Disease - metabolism Amino Acid Sequence Biological and medical sciences Degenerative and inherited degenerative diseases of the nervous system. Leukodystrophies. Prion diseases DNA Enzyme-Linked Immunosorbent Assay Humans Medical sciences Molecular Sequence Data Neurology Neuropeptides - metabolism Phosphopeptides - metabolism Phosphorylation Proline-Directed Protein Kinases Protein Kinases - isolation & purification Protein Kinases - metabolism tau Proteins - chemistry tau Proteins - immunology tau Proteins - metabolism |
| title | Application of synthetic phospho- and unphospho- peptides to identify phosphorylation sites in a subregion of the tau molecule, which is modified in Alzheimer's disease |
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