Transthyretin forms amyloid fibrils at physiological pH with ultrasonication
In transthyretin (TTR)-related amyloidosis, wild-type TTR (WT-TTR), as well as mutated TTRs play important roles in the pathogenesis of senile systemic amyloidosis and familial amyloidotic polyneuropathy. However, WT-TTR usually forms stable tetramers at physiological pH, and the mechanism of such f...
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| Veröffentlicht in: | Amyloid 2008, Vol.15 (4), p.234-239 |
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| creator | Misumi, Yohei Ueda, Mitsuharu Fujimori, Hiromi Shinriki, Satoru Meng, Wei Kim, Jaemi Saito, Shiori Obayashi, Konen Uchino, Makoto Ando, Yukio |
| description | In transthyretin (TTR)-related amyloidosis, wild-type TTR (WT-TTR), as well as mutated TTRs play important roles in the pathogenesis of senile systemic amyloidosis and familial amyloidotic polyneuropathy. However, WT-TTR usually forms stable tetramers at physiological pH, and the mechanism of such fibril formation under physiological conditions remains to be elucidated. In this study, we demonstrated WT-TTR amyloid fibril formation at physiological pH with ultrasonication. Cross-linked SDS-PAGE and circular dichroism revealed that ultrasonication induced both tetrameric TTR dissociation and monomeric TTR denaturation. These results indicate that extremely low pH is not an essential condition for TTR amyloid fibril formation if TTR is degenerated in such conditions. In addition, this method allows analysis of accelerator factors or inhibitory agents in TTR amyloid fibril formation at neutral pH. |
| doi_str_mv | 10.1080/13506120802524684 |
| format | Article |
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However, WT-TTR usually forms stable tetramers at physiological pH, and the mechanism of such fibril formation under physiological conditions remains to be elucidated. In this study, we demonstrated WT-TTR amyloid fibril formation at physiological pH with ultrasonication. Cross-linked SDS-PAGE and circular dichroism revealed that ultrasonication induced both tetrameric TTR dissociation and monomeric TTR denaturation. These results indicate that extremely low pH is not an essential condition for TTR amyloid fibril formation if TTR is degenerated in such conditions. In addition, this method allows analysis of accelerator factors or inhibitory agents in TTR amyloid fibril formation at neutral pH.</description><identifier>ISSN: 1350-6129</identifier><identifier>EISSN: 1744-2818</identifier><identifier>DOI: 10.1080/13506120802524684</identifier><identifier>PMID: 19065294</identifier><language>eng</language><publisher>England: Informa UK Ltd</publisher><subject>Amyloid - chemistry ; Amyloid - metabolism ; Amyloid - ultrastructure ; Amyloid fibrils ; amyloidosis ; Humans ; Hydrogen-Ion Concentration ; In Vitro Techniques ; Microscopy, Electron, Transmission ; Multiprotein Complexes - chemistry ; Multiprotein Complexes - metabolism ; physiological pH ; Prealbumin - chemistry ; Prealbumin - metabolism ; Prealbumin - ultrastructure ; Protein Structure, Quaternary ; Sonication ; transthyretin ; ultrasonication</subject><ispartof>Amyloid, 2008, Vol.15 (4), p.234-239</ispartof><rights>2008 Informa UK Ltd All rights reserved: reproduction in whole or part not permitted 2008</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c404t-903b42507caaf952043369d64e47988b42346f2fe611dc5f0be60ec4d82be7a33</citedby><cites>FETCH-LOGICAL-c404t-903b42507caaf952043369d64e47988b42346f2fe611dc5f0be60ec4d82be7a33</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.tandfonline.com/doi/pdf/10.1080/13506120802524684$$EPDF$$P50$$Ginformahealthcare$$H</linktopdf><linktohtml>$$Uhttps://www.tandfonline.com/doi/full/10.1080/13506120802524684$$EHTML$$P50$$Ginformahealthcare$$H</linktohtml><link.rule.ids>314,776,780,4010,27900,27901,27902,59620,59726,60409,60515,61194,61229,61375,61410</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/19065294$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Misumi, Yohei</creatorcontrib><creatorcontrib>Ueda, Mitsuharu</creatorcontrib><creatorcontrib>Fujimori, Hiromi</creatorcontrib><creatorcontrib>Shinriki, Satoru</creatorcontrib><creatorcontrib>Meng, Wei</creatorcontrib><creatorcontrib>Kim, Jaemi</creatorcontrib><creatorcontrib>Saito, Shiori</creatorcontrib><creatorcontrib>Obayashi, Konen</creatorcontrib><creatorcontrib>Uchino, Makoto</creatorcontrib><creatorcontrib>Ando, Yukio</creatorcontrib><title>Transthyretin forms amyloid fibrils at physiological pH with ultrasonication</title><title>Amyloid</title><addtitle>Amyloid</addtitle><description>In transthyretin (TTR)-related amyloidosis, wild-type TTR (WT-TTR), as well as mutated TTRs play important roles in the pathogenesis of senile systemic amyloidosis and familial amyloidotic polyneuropathy. However, WT-TTR usually forms stable tetramers at physiological pH, and the mechanism of such fibril formation under physiological conditions remains to be elucidated. In this study, we demonstrated WT-TTR amyloid fibril formation at physiological pH with ultrasonication. Cross-linked SDS-PAGE and circular dichroism revealed that ultrasonication induced both tetrameric TTR dissociation and monomeric TTR denaturation. These results indicate that extremely low pH is not an essential condition for TTR amyloid fibril formation if TTR is degenerated in such conditions. In addition, this method allows analysis of accelerator factors or inhibitory agents in TTR amyloid fibril formation at neutral pH.</description><subject>Amyloid - chemistry</subject><subject>Amyloid - metabolism</subject><subject>Amyloid - ultrastructure</subject><subject>Amyloid fibrils</subject><subject>amyloidosis</subject><subject>Humans</subject><subject>Hydrogen-Ion Concentration</subject><subject>In Vitro Techniques</subject><subject>Microscopy, Electron, Transmission</subject><subject>Multiprotein Complexes - chemistry</subject><subject>Multiprotein Complexes - metabolism</subject><subject>physiological pH</subject><subject>Prealbumin - chemistry</subject><subject>Prealbumin - metabolism</subject><subject>Prealbumin - ultrastructure</subject><subject>Protein Structure, Quaternary</subject><subject>Sonication</subject><subject>transthyretin</subject><subject>ultrasonication</subject><issn>1350-6129</issn><issn>1744-2818</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2008</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kEtLBSEYhiWK7j-gTcyq3ZS3cZTaRHSDA21qLY6jjeGMJ3WI8-_zcA5EBK389HveF3kAOEPwEkEOrxBpIEO4jLjBlHG6Aw5RS2mNOeK7ZS77ugDiAByl9AEhJlDwfXCABGQNFvQQLF6jmlIeVtFkN1U2xDFValz54PrKui46X-65Wg6r5IIP704rXy2fqi-Xh2r2OaoUpvKYXZhOwJ5VPpnT7XkM3h7uX--e6sXL4_Pd7aLWFNJcC0g6ihvYaqWsaDCkhDDRM2poKzgvO0KZxdYwhHrdWNgZBo2mPcedaRUhx-Bi07uM4XM2KcvRJW28V5MJc5JM8BYj2hYQbUAdQ0rRWLmMblRxJRGUa4Xyj8KSOd-Wz91o-p_E1lkBbjaAm9a61FeIvpdZFWfRFpvaJUn-67_-FR-M8nnQKhr5EeY4FXH__O4bTM6Rmg</recordid><startdate>2008</startdate><enddate>2008</enddate><creator>Misumi, Yohei</creator><creator>Ueda, Mitsuharu</creator><creator>Fujimori, Hiromi</creator><creator>Shinriki, Satoru</creator><creator>Meng, Wei</creator><creator>Kim, Jaemi</creator><creator>Saito, Shiori</creator><creator>Obayashi, Konen</creator><creator>Uchino, Makoto</creator><creator>Ando, Yukio</creator><general>Informa UK Ltd</general><general>Taylor & Francis</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></search><sort><creationdate>2008</creationdate><title>Transthyretin forms amyloid fibrils at physiological pH with ultrasonication</title><author>Misumi, Yohei ; Ueda, Mitsuharu ; Fujimori, Hiromi ; Shinriki, Satoru ; Meng, Wei ; Kim, Jaemi ; Saito, Shiori ; Obayashi, Konen ; Uchino, Makoto ; Ando, Yukio</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c404t-903b42507caaf952043369d64e47988b42346f2fe611dc5f0be60ec4d82be7a33</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2008</creationdate><topic>Amyloid - chemistry</topic><topic>Amyloid - metabolism</topic><topic>Amyloid - ultrastructure</topic><topic>Amyloid fibrils</topic><topic>amyloidosis</topic><topic>Humans</topic><topic>Hydrogen-Ion Concentration</topic><topic>In Vitro Techniques</topic><topic>Microscopy, Electron, Transmission</topic><topic>Multiprotein Complexes - chemistry</topic><topic>Multiprotein Complexes - metabolism</topic><topic>physiological pH</topic><topic>Prealbumin - chemistry</topic><topic>Prealbumin - metabolism</topic><topic>Prealbumin - ultrastructure</topic><topic>Protein Structure, Quaternary</topic><topic>Sonication</topic><topic>transthyretin</topic><topic>ultrasonication</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Misumi, Yohei</creatorcontrib><creatorcontrib>Ueda, Mitsuharu</creatorcontrib><creatorcontrib>Fujimori, Hiromi</creatorcontrib><creatorcontrib>Shinriki, Satoru</creatorcontrib><creatorcontrib>Meng, Wei</creatorcontrib><creatorcontrib>Kim, Jaemi</creatorcontrib><creatorcontrib>Saito, Shiori</creatorcontrib><creatorcontrib>Obayashi, Konen</creatorcontrib><creatorcontrib>Uchino, Makoto</creatorcontrib><creatorcontrib>Ando, Yukio</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><jtitle>Amyloid</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Misumi, Yohei</au><au>Ueda, Mitsuharu</au><au>Fujimori, Hiromi</au><au>Shinriki, Satoru</au><au>Meng, Wei</au><au>Kim, Jaemi</au><au>Saito, Shiori</au><au>Obayashi, Konen</au><au>Uchino, Makoto</au><au>Ando, Yukio</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Transthyretin forms amyloid fibrils at physiological pH with ultrasonication</atitle><jtitle>Amyloid</jtitle><addtitle>Amyloid</addtitle><date>2008</date><risdate>2008</risdate><volume>15</volume><issue>4</issue><spage>234</spage><epage>239</epage><pages>234-239</pages><issn>1350-6129</issn><eissn>1744-2818</eissn><abstract>In transthyretin (TTR)-related amyloidosis, wild-type TTR (WT-TTR), as well as mutated TTRs play important roles in the pathogenesis of senile systemic amyloidosis and familial amyloidotic polyneuropathy. However, WT-TTR usually forms stable tetramers at physiological pH, and the mechanism of such fibril formation under physiological conditions remains to be elucidated. In this study, we demonstrated WT-TTR amyloid fibril formation at physiological pH with ultrasonication. Cross-linked SDS-PAGE and circular dichroism revealed that ultrasonication induced both tetrameric TTR dissociation and monomeric TTR denaturation. These results indicate that extremely low pH is not an essential condition for TTR amyloid fibril formation if TTR is degenerated in such conditions. In addition, this method allows analysis of accelerator factors or inhibitory agents in TTR amyloid fibril formation at neutral pH.</abstract><cop>England</cop><pub>Informa UK Ltd</pub><pmid>19065294</pmid><doi>10.1080/13506120802524684</doi><tpages>6</tpages></addata></record> |
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| subjects | Amyloid - chemistry Amyloid - metabolism Amyloid - ultrastructure Amyloid fibrils amyloidosis Humans Hydrogen-Ion Concentration In Vitro Techniques Microscopy, Electron, Transmission Multiprotein Complexes - chemistry Multiprotein Complexes - metabolism physiological pH Prealbumin - chemistry Prealbumin - metabolism Prealbumin - ultrastructure Protein Structure, Quaternary Sonication transthyretin ultrasonication |
| title | Transthyretin forms amyloid fibrils at physiological pH with ultrasonication |
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