Common Structure of Soluble Amyloid Oligomers Implies Common Mechanism of Pathogenesis
Soluble oligomers are common to most amyloids and may represent the primary toxic species of amyloids, like the Aβ peptide in Alzheimer's disease (AD). Here we show that all of the soluble oligomers tested display a common conformation-dependent structure that is unique to soluble oligomers reg...
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| Veröffentlicht in: | Science (American Association for the Advancement of Science) 2003-04, Vol.300 (5618), p.486-489 |
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| creator | Kayed, Rakez Head, Elizabeth Thompson, Jennifer L. McIntire, Theresa M. Milton, Saskia C. Cotman, Carl W. Glabe, Charles G. |
| description | Soluble oligomers are common to most amyloids and may represent the primary toxic species of amyloids, like the Aβ peptide in Alzheimer's disease (AD). Here we show that all of the soluble oligomers tested display a common conformation-dependent structure that is unique to soluble oligomers regardless of sequence. The in vitro toxicity of soluble oligomers is inhibited by oligomer-specific antibody. Soluble oligomers have a unique distribution in human AD brain that is distinct from fibrillar amyloid. These results indicate that different types of soluble amyloid oligomers have a common structure and suggest they share a common mechanism of toxicity. |
| doi_str_mv | 10.1126/science.1079469 |
| format | Article |
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Here we show that all of the soluble oligomers tested display a common conformation-dependent structure that is unique to soluble oligomers regardless of sequence. The in vitro toxicity of soluble oligomers is inhibited by oligomer-specific antibody. Soluble oligomers have a unique distribution in human AD brain that is distinct from fibrillar amyloid. These results indicate that different types of soluble amyloid oligomers have a common structure and suggest they share a common mechanism of toxicity.</description><identifier>ISSN: 0036-8075</identifier><identifier>EISSN: 1095-9203</identifier><identifier>DOI: 10.1126/science.1079469</identifier><identifier>PMID: 12702875</identifier><identifier>CODEN: SCIEAS</identifier><language>eng</language><publisher>Washington, DC: American Association for the Advancement of Science</publisher><subject>Aged ; Aged, 80 and over ; Alzheimer Disease - metabolism ; Alzheimer Disease - pathology ; Alzheimer's disease ; Amyloid - chemistry ; Amyloid - toxicity ; Amyloid beta-Peptides - analysis ; Amyloid beta-Peptides - chemistry ; Amyloid beta-Peptides - immunology ; Amyloid beta-Peptides - toxicity ; Amyloid beta-protein ; Amyloids ; Animals ; Antibodies ; Antibodies - immunology ; Antibody Specificity ; Biochemistry ; Biological and medical sciences ; Biopolymers - analysis ; Biopolymers - chemistry ; Biopolymers - toxicity ; Brain - pathology ; Brain Chemistry ; Cell Survival ; Degenerative and inherited degenerative diseases of the nervous system. Leukodystrophies. Prion diseases ; Humans ; Malingering ; Medical sciences ; Microscopy, Confocal ; Microscopy, Electron ; Mimicry ; Molecular Mimicry ; Neurofibrillary Tangles - chemistry ; Neurology ; Oligomers ; Origin ; Pathogenesis ; Pathogens ; Pathology ; Peptide Fragments - chemistry ; Peptide Fragments - immunology ; Peptides ; Poisons ; Protein Conformation ; Rabbits ; Reactivity ; Solar fibrils ; Solubility ; Tumor Cells, Cultured</subject><ispartof>Science (American Association for the Advancement of Science), 2003-04, Vol.300 (5618), p.486-489</ispartof><rights>Copyright 2003 American Association for the Advancement of Science</rights><rights>2003 INIST-CNRS</rights><rights>COPYRIGHT 2003 American Association for the Advancement of Science</rights><rights>COPYRIGHT 2003 American Association for the Advancement of Science</rights><rights>Copyright American Association for the Advancement of Science Apr 18, 2003</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c781t-655ed1de931c6b2036507f02fbb1d79f1a6d9732bb01647a480b47e00dfab3733</citedby><cites>FETCH-LOGICAL-c781t-655ed1de931c6b2036507f02fbb1d79f1a6d9732bb01647a480b47e00dfab3733</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.jstor.org/stable/pdf/3834203$$EPDF$$P50$$Gjstor$$H</linktopdf><linktohtml>$$Uhttps://www.jstor.org/stable/3834203$$EHTML$$P50$$Gjstor$$H</linktohtml><link.rule.ids>314,776,780,799,2871,2872,27901,27902,57992,58225</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=14747242$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/12702875$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Kayed, Rakez</creatorcontrib><creatorcontrib>Head, Elizabeth</creatorcontrib><creatorcontrib>Thompson, Jennifer L.</creatorcontrib><creatorcontrib>McIntire, Theresa M.</creatorcontrib><creatorcontrib>Milton, Saskia C.</creatorcontrib><creatorcontrib>Cotman, Carl W.</creatorcontrib><creatorcontrib>Glabe, Charles G.</creatorcontrib><title>Common Structure of Soluble Amyloid Oligomers Implies Common Mechanism of Pathogenesis</title><title>Science (American Association for the Advancement of Science)</title><addtitle>Science</addtitle><description>Soluble oligomers are common to most amyloids and may represent the primary toxic species of amyloids, like the Aβ peptide in Alzheimer's disease (AD). Here we show that all of the soluble oligomers tested display a common conformation-dependent structure that is unique to soluble oligomers regardless of sequence. The in vitro toxicity of soluble oligomers is inhibited by oligomer-specific antibody. Soluble oligomers have a unique distribution in human AD brain that is distinct from fibrillar amyloid. These results indicate that different types of soluble amyloid oligomers have a common structure and suggest they share a common mechanism of toxicity.</description><subject>Aged</subject><subject>Aged, 80 and over</subject><subject>Alzheimer Disease - metabolism</subject><subject>Alzheimer Disease - pathology</subject><subject>Alzheimer's disease</subject><subject>Amyloid - chemistry</subject><subject>Amyloid - toxicity</subject><subject>Amyloid beta-Peptides - analysis</subject><subject>Amyloid beta-Peptides - chemistry</subject><subject>Amyloid beta-Peptides - immunology</subject><subject>Amyloid beta-Peptides - toxicity</subject><subject>Amyloid beta-protein</subject><subject>Amyloids</subject><subject>Animals</subject><subject>Antibodies</subject><subject>Antibodies - immunology</subject><subject>Antibody Specificity</subject><subject>Biochemistry</subject><subject>Biological and medical sciences</subject><subject>Biopolymers - analysis</subject><subject>Biopolymers - chemistry</subject><subject>Biopolymers - toxicity</subject><subject>Brain - pathology</subject><subject>Brain Chemistry</subject><subject>Cell Survival</subject><subject>Degenerative and inherited degenerative diseases of the nervous system. 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Prion diseases</subject><subject>Humans</subject><subject>Malingering</subject><subject>Medical sciences</subject><subject>Microscopy, Confocal</subject><subject>Microscopy, Electron</subject><subject>Mimicry</subject><subject>Molecular Mimicry</subject><subject>Neurofibrillary Tangles - chemistry</subject><subject>Neurology</subject><subject>Oligomers</subject><subject>Origin</subject><subject>Pathogenesis</subject><subject>Pathogens</subject><subject>Pathology</subject><subject>Peptide Fragments - chemistry</subject><subject>Peptide Fragments - immunology</subject><subject>Peptides</subject><subject>Poisons</subject><subject>Protein Conformation</subject><subject>Rabbits</subject><subject>Reactivity</subject><subject>Solar fibrils</subject><subject>Solubility</subject><subject>Tumor Cells, Cultured</subject><issn>0036-8075</issn><issn>1095-9203</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2003</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>8G5</sourceid><sourceid>BEC</sourceid><sourceid>BENPR</sourceid><sourceid>GUQSH</sourceid><sourceid>M2O</sourceid><recordid>eNqN0t-r0zAUB_Agind3-uyLSBFUfOhufrRN-ziHzsF0wvS-hjQ97c1Im5m0cO9_b8aKl8mQ0YdA8_mmOT0HoVcEzwih2Y1XGjoFM4J5kWTFEzQhuEjjgmL2FE0wZlmcY55eoWvvdxiHvYI9R1eEckxznk7Q7cK2re2ibe8G1Q8OIltHW2uG0kA0bx-M1VW0MbqxLTgfrdq90eCjMfUN1J3stG8PqR-yv7MNdOC1f4Ge1dJ4eDmuU_Try-efi6_xerNcLebrWPGc9HGWplCRCgpGVFaGS2cp5jWmdVmSihc1kVlVcEbLEpMs4TLJcZlwwLiqZck4Y1P04Xju3tnfA_hetNorMEZ2YAcveMIILVKcBfn-v5Lk4TvBBfj2H7izg-tCFYISlhacJjSg-IgaaUDorra9k-pQvJPGdlDr8HpOwg_PKA91TdHsjA9PBa1WZwMfTwLB9HDfN3LwXqy23y-3m9vL7aflxTZfrk9tfM4qaww0IELTF5tTf3P0ylnvHdRi73Qr3YMgWBxGW4yjLcbRDok3Y1-GsoXq0Y-zHMC7EUivpKmd7JT2jy7hydi710e38711f_dZzpJwMfYHG7UEyA</recordid><startdate>20030418</startdate><enddate>20030418</enddate><creator>Kayed, Rakez</creator><creator>Head, Elizabeth</creator><creator>Thompson, Jennifer L.</creator><creator>McIntire, Theresa M.</creator><creator>Milton, Saskia C.</creator><creator>Cotman, Carl W.</creator><creator>Glabe, Charles G.</creator><general>American Association for the Advancement of Science</general><general>The American Association for the Advancement of Science</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>8GL</scope><scope>IBG</scope><scope>IOV</scope><scope>ISN</scope><scope>0-V</scope><scope>3V.</scope><scope>7QF</scope><scope>7QG</scope><scope>7QL</scope><scope>7QP</scope><scope>7QQ</scope><scope>7QR</scope><scope>7SC</scope><scope>7SE</scope><scope>7SN</scope><scope>7SP</scope><scope>7SR</scope><scope>7SS</scope><scope>7T7</scope><scope>7TA</scope><scope>7TB</scope><scope>7TK</scope><scope>7TM</scope><scope>7U5</scope><scope>7U9</scope><scope>7X2</scope><scope>7X7</scope><scope>7XB</scope><scope>88A</scope><scope>88B</scope><scope>88E</scope><scope>88I</scope><scope>8AF</scope><scope>8BQ</scope><scope>8FD</scope><scope>8FE</scope><scope>8FG</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>8G5</scope><scope>ABJCF</scope><scope>ABUWG</scope><scope>AEUYN</scope><scope>AFKRA</scope><scope>ALSLI</scope><scope>ARAPS</scope><scope>ATCPS</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BEC</scope><scope>BENPR</scope><scope>BGLVJ</scope><scope>BHPHI</scope><scope>BKSAR</scope><scope>C1K</scope><scope>CCPQU</scope><scope>CJNVE</scope><scope>D1I</scope><scope>DWQXO</scope><scope>F28</scope><scope>FR3</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>GUQSH</scope><scope>H8D</scope><scope>H8G</scope><scope>H94</scope><scope>HCIFZ</scope><scope>JG9</scope><scope>JQ2</scope><scope>K9-</scope><scope>K9.</scope><scope>KB.</scope><scope>KR7</scope><scope>L6V</scope><scope>L7M</scope><scope>LK8</scope><scope>L~C</scope><scope>L~D</scope><scope>M0K</scope><scope>M0P</scope><scope>M0R</scope><scope>M0S</scope><scope>M1P</scope><scope>M2O</scope><scope>M2P</scope><scope>M7N</scope><scope>M7P</scope><scope>M7S</scope><scope>MBDVC</scope><scope>P5Z</scope><scope>P62</scope><scope>P64</scope><scope>PATMY</scope><scope>PCBAR</scope><scope>PDBOC</scope><scope>PQEDU</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PRINS</scope><scope>PTHSS</scope><scope>PYCSY</scope><scope>Q9U</scope><scope>R05</scope><scope>RC3</scope></search><sort><creationdate>20030418</creationdate><title>Common Structure of Soluble Amyloid Oligomers Implies Common Mechanism of Pathogenesis</title><author>Kayed, Rakez ; 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Prion diseases</topic><topic>Humans</topic><topic>Malingering</topic><topic>Medical sciences</topic><topic>Microscopy, Confocal</topic><topic>Microscopy, Electron</topic><topic>Mimicry</topic><topic>Molecular Mimicry</topic><topic>Neurofibrillary Tangles - chemistry</topic><topic>Neurology</topic><topic>Oligomers</topic><topic>Origin</topic><topic>Pathogenesis</topic><topic>Pathogens</topic><topic>Pathology</topic><topic>Peptide Fragments - chemistry</topic><topic>Peptide Fragments - immunology</topic><topic>Peptides</topic><topic>Poisons</topic><topic>Protein Conformation</topic><topic>Rabbits</topic><topic>Reactivity</topic><topic>Solar fibrils</topic><topic>Solubility</topic><topic>Tumor Cells, Cultured</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Kayed, Rakez</creatorcontrib><creatorcontrib>Head, Elizabeth</creatorcontrib><creatorcontrib>Thompson, Jennifer L.</creatorcontrib><creatorcontrib>McIntire, Theresa 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Here we show that all of the soluble oligomers tested display a common conformation-dependent structure that is unique to soluble oligomers regardless of sequence. The in vitro toxicity of soluble oligomers is inhibited by oligomer-specific antibody. Soluble oligomers have a unique distribution in human AD brain that is distinct from fibrillar amyloid. These results indicate that different types of soluble amyloid oligomers have a common structure and suggest they share a common mechanism of toxicity.</abstract><cop>Washington, DC</cop><pub>American Association for the Advancement of Science</pub><pmid>12702875</pmid><doi>10.1126/science.1079469</doi><tpages>4</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0036-8075 |
| ispartof | Science (American Association for the Advancement of Science), 2003-04, Vol.300 (5618), p.486-489 |
| issn | 0036-8075 1095-9203 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_743129506 |
| source | MEDLINE; Science Online_科学在线; JSTOR Complete Journals |
| subjects | Aged Aged, 80 and over Alzheimer Disease - metabolism Alzheimer Disease - pathology Alzheimer's disease Amyloid - chemistry Amyloid - toxicity Amyloid beta-Peptides - analysis Amyloid beta-Peptides - chemistry Amyloid beta-Peptides - immunology Amyloid beta-Peptides - toxicity Amyloid beta-protein Amyloids Animals Antibodies Antibodies - immunology Antibody Specificity Biochemistry Biological and medical sciences Biopolymers - analysis Biopolymers - chemistry Biopolymers - toxicity Brain - pathology Brain Chemistry Cell Survival Degenerative and inherited degenerative diseases of the nervous system. Leukodystrophies. Prion diseases Humans Malingering Medical sciences Microscopy, Confocal Microscopy, Electron Mimicry Molecular Mimicry Neurofibrillary Tangles - chemistry Neurology Oligomers Origin Pathogenesis Pathogens Pathology Peptide Fragments - chemistry Peptide Fragments - immunology Peptides Poisons Protein Conformation Rabbits Reactivity Solar fibrils Solubility Tumor Cells, Cultured |
| title | Common Structure of Soluble Amyloid Oligomers Implies Common Mechanism of Pathogenesis |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-02-04T15%3A47%3A46IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-gale_proqu&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Common%20Structure%20of%20Soluble%20Amyloid%20Oligomers%20Implies%20Common%20Mechanism%20of%20Pathogenesis&rft.jtitle=Science%20(American%20Association%20for%20the%20Advancement%20of%20Science)&rft.au=Kayed,%20Rakez&rft.date=2003-04-18&rft.volume=300&rft.issue=5618&rft.spage=486&rft.epage=489&rft.pages=486-489&rft.issn=0036-8075&rft.eissn=1095-9203&rft.coden=SCIEAS&rft_id=info:doi/10.1126/science.1079469&rft_dat=%3Cgale_proqu%3EA100962720%3C/gale_proqu%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=213597242&rft_id=info:pmid/12702875&rft_galeid=A100962720&rft_jstor_id=3834203&rfr_iscdi=true |