Heparin-induced tau filaments are structurally heterogeneous and differ from Alzheimer's disease filaments
Alzheimer's disease (AD) is characterized by the presence of tau filaments in the brain whose structure was recently solved. The formation of AD filaments is routinely modeled in vitro by mixing tau with heparin. This study shows that heparin-induced tau filaments are markedly different from th...
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Veröffentlicht in: | Chemical communications (Cambridge, England) England), 2018-05, Vol.54 (36), p.4573-4576 |
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creator | Fichou, Yann Vigers, Michael Goring, Andrew K Eschmann, Neil A Han, Songi |
description | Alzheimer's disease (AD) is characterized by the presence of tau filaments in the brain whose structure was recently solved. The formation of AD filaments is routinely modeled
in vitro
by mixing tau with heparin. This study shows that heparin-induced tau filaments are markedly different from the AD filaments and are highly heterogeneous.
Tau filaments formed with heparin are structurally different from Alzheimer's disease filaments extracted from human brains. Heparin creates heterogeneous filaments in which tau proteins are locally stretched and have minimal large-domain structuration. |
doi_str_mv | 10.1039/c8cc01355a |
format | Article |
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in vitro
by mixing tau with heparin. This study shows that heparin-induced tau filaments are markedly different from the AD filaments and are highly heterogeneous.
Tau filaments formed with heparin are structurally different from Alzheimer's disease filaments extracted from human brains. Heparin creates heterogeneous filaments in which tau proteins are locally stretched and have minimal large-domain structuration.</description><identifier>ISSN: 1359-7345</identifier><identifier>EISSN: 1364-548X</identifier><identifier>DOI: 10.1039/c8cc01355a</identifier><identifier>PMID: 29664486</identifier><language>eng</language><publisher>England: Royal Society of Chemistry</publisher><subject>Alzheimer Disease - pathology ; Alzheimer's disease ; Amino Acid Sequence ; Amyloid - chemistry ; Amyloid - metabolism ; Brain ; Filaments ; Heparin - chemistry ; Heparin - metabolism ; Humans ; Membrane Proteins - chemistry ; Membrane Proteins - metabolism ; Molecular Structure ; Peptide Fragments - chemistry ; Peptide Fragments - metabolism ; Protein Aggregation, Pathological - metabolism ; Protein Binding ; Protein Multimerization - drug effects ; Protein Structure, Quaternary - drug effects ; Pyrrolidines - chemistry ; Spin Labels ; Thiosulfonic Acids - chemistry</subject><ispartof>Chemical communications (Cambridge, England), 2018-05, Vol.54 (36), p.4573-4576</ispartof><rights>Copyright Royal Society of Chemistry 2018</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c378t-935020ec641273f18ae29e13b5a1d2c0331ba7c94553df41f1e2d8b5eae024833</citedby><cites>FETCH-LOGICAL-c378t-935020ec641273f18ae29e13b5a1d2c0331ba7c94553df41f1e2d8b5eae024833</cites><orcidid>0000-0001-6489-6246 ; 0000-0002-6520-0041 ; 0000-0002-5095-895X ; 0000-0003-4220-6472 ; 0000-0002-5685-6153</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780,27903,27904</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/29664486$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Fichou, Yann</creatorcontrib><creatorcontrib>Vigers, Michael</creatorcontrib><creatorcontrib>Goring, Andrew K</creatorcontrib><creatorcontrib>Eschmann, Neil A</creatorcontrib><creatorcontrib>Han, Songi</creatorcontrib><title>Heparin-induced tau filaments are structurally heterogeneous and differ from Alzheimer's disease filaments</title><title>Chemical communications (Cambridge, England)</title><addtitle>Chem Commun (Camb)</addtitle><description>Alzheimer's disease (AD) is characterized by the presence of tau filaments in the brain whose structure was recently solved. The formation of AD filaments is routinely modeled
in vitro
by mixing tau with heparin. This study shows that heparin-induced tau filaments are markedly different from the AD filaments and are highly heterogeneous.
Tau filaments formed with heparin are structurally different from Alzheimer's disease filaments extracted from human brains. Heparin creates heterogeneous filaments in which tau proteins are locally stretched and have minimal large-domain structuration.</description><subject>Alzheimer Disease - pathology</subject><subject>Alzheimer's disease</subject><subject>Amino Acid Sequence</subject><subject>Amyloid - chemistry</subject><subject>Amyloid - metabolism</subject><subject>Brain</subject><subject>Filaments</subject><subject>Heparin - chemistry</subject><subject>Heparin - metabolism</subject><subject>Humans</subject><subject>Membrane Proteins - chemistry</subject><subject>Membrane Proteins - metabolism</subject><subject>Molecular Structure</subject><subject>Peptide Fragments - chemistry</subject><subject>Peptide Fragments - metabolism</subject><subject>Protein Aggregation, Pathological - metabolism</subject><subject>Protein Binding</subject><subject>Protein Multimerization - drug effects</subject><subject>Protein Structure, Quaternary - drug effects</subject><subject>Pyrrolidines - chemistry</subject><subject>Spin Labels</subject><subject>Thiosulfonic Acids - chemistry</subject><issn>1359-7345</issn><issn>1364-548X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2018</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpdkctLw0AQxhdRbK1evCsBD4oQ3WeyOZagVih4UfAWtptZm5JH3c0e6l_v9mELzmWGmR8fH_MhdEnwA8Ese9RSa0yYEOoIDQlLeCy4_DxezyKLU8bFAJ05t8ChiJCnaECzJOFcJkO0mMBS2aqNq7b0GsqoVz4yVa0aaHsXKQuR663XvbeqrlfRHHqw3Re00PlwbsuorIwBGxnbNdG4_plD1YC9dWHvQDk4iJ2jE6NqBxe7PkIfz0_v-SSevr285uNprFkq-zhjAlMMOuGEpswQqYBmQNhMKFJSjRkjM5XqjAvBSsOJIUBLOROgAFMuGRuhu63u0nbfHlxfNJXTUNdqY7qgmAbtjPI0oDf_0EXnbRvcBYrRJEvYhrrfUtp2zlkwxdJWjbKrguBinUCRyzzfJDAO8PVO0s8aKPfo38sDcLUFrNP76yFC9gtvGIsd</recordid><startdate>20180501</startdate><enddate>20180501</enddate><creator>Fichou, Yann</creator><creator>Vigers, Michael</creator><creator>Goring, Andrew K</creator><creator>Eschmann, Neil A</creator><creator>Han, Songi</creator><general>Royal Society of Chemistry</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>7SR</scope><scope>7U5</scope><scope>8BQ</scope><scope>8FD</scope><scope>JG9</scope><scope>L7M</scope><scope>7X8</scope><orcidid>https://orcid.org/0000-0001-6489-6246</orcidid><orcidid>https://orcid.org/0000-0002-6520-0041</orcidid><orcidid>https://orcid.org/0000-0002-5095-895X</orcidid><orcidid>https://orcid.org/0000-0003-4220-6472</orcidid><orcidid>https://orcid.org/0000-0002-5685-6153</orcidid></search><sort><creationdate>20180501</creationdate><title>Heparin-induced tau filaments are structurally heterogeneous and differ from Alzheimer's disease filaments</title><author>Fichou, Yann ; 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The formation of AD filaments is routinely modeled
in vitro
by mixing tau with heparin. This study shows that heparin-induced tau filaments are markedly different from the AD filaments and are highly heterogeneous.
Tau filaments formed with heparin are structurally different from Alzheimer's disease filaments extracted from human brains. Heparin creates heterogeneous filaments in which tau proteins are locally stretched and have minimal large-domain structuration.</abstract><cop>England</cop><pub>Royal Society of Chemistry</pub><pmid>29664486</pmid><doi>10.1039/c8cc01355a</doi><tpages>4</tpages><orcidid>https://orcid.org/0000-0001-6489-6246</orcidid><orcidid>https://orcid.org/0000-0002-6520-0041</orcidid><orcidid>https://orcid.org/0000-0002-5095-895X</orcidid><orcidid>https://orcid.org/0000-0003-4220-6472</orcidid><orcidid>https://orcid.org/0000-0002-5685-6153</orcidid></addata></record> |
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source | MEDLINE; Royal Society Of Chemistry Journals 2008-; Alma/SFX Local Collection |
subjects | Alzheimer Disease - pathology Alzheimer's disease Amino Acid Sequence Amyloid - chemistry Amyloid - metabolism Brain Filaments Heparin - chemistry Heparin - metabolism Humans Membrane Proteins - chemistry Membrane Proteins - metabolism Molecular Structure Peptide Fragments - chemistry Peptide Fragments - metabolism Protein Aggregation, Pathological - metabolism Protein Binding Protein Multimerization - drug effects Protein Structure, Quaternary - drug effects Pyrrolidines - chemistry Spin Labels Thiosulfonic Acids - chemistry |
title | Heparin-induced tau filaments are structurally heterogeneous and differ from Alzheimer's disease filaments |
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