Epigallocatechin gallate (EGCG) reduces the intensity of pancreatic amyloid fibrils in human islet amyloid polypeptide (hIAPP) transgenic mice

The formation of amyloid fibrils by human islet amyloid polypeptide protein (hIAPP) has been implicated in pancreas dysfunction and diabetes. However, efficient treatment options to reduce amyloid fibrils in vivo are still lacking. Therefore, we tested the effect of epigallocatechin gallate (EGCG) o...

Ausführliche Beschreibung

Gespeichert in:
Bibliographische Detailangaben
Veröffentlicht in:Scientific reports 2018-01, Vol.8 (1), p.1116-12, Article 1116
Hauptverfasser: Franko, Andras, Rodriguez Camargo, Diana C., Böddrich, Annett, Garg, Divita, Rodriguez Camargo, Andres, Rathkolb, Birgit, Janik, Dirk, Aichler, Michaela, Feuchtinger, Annette, Neff, Frauke, Fuchs, Helmut, Wanker, Erich E., Reif, Bernd, Häring, Hans-Ulrich, Peter, Andreas, Hrabě de Angelis, Martin
Format: Artikel
Sprache:eng
Schlagworte:
Online-Zugang:Volltext
Tags: Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
container_end_page 12
container_issue 1
container_start_page 1116
container_title Scientific reports
container_volume 8
creator Franko, Andras
Rodriguez Camargo, Diana C.
Böddrich, Annett
Garg, Divita
Rodriguez Camargo, Andres
Rathkolb, Birgit
Janik, Dirk
Aichler, Michaela
Feuchtinger, Annette
Neff, Frauke
Fuchs, Helmut
Wanker, Erich E.
Reif, Bernd
Häring, Hans-Ulrich
Peter, Andreas
Hrabě de Angelis, Martin
description The formation of amyloid fibrils by human islet amyloid polypeptide protein (hIAPP) has been implicated in pancreas dysfunction and diabetes. However, efficient treatment options to reduce amyloid fibrils in vivo are still lacking. Therefore, we tested the effect of epigallocatechin gallate (EGCG) on fibril formation in vitro and in vivo . To determine the binding of hIAPP and EGCG, in vitro interaction studies were performed. To inhibit amyloid plaque formation in vivo , homozygous (tg/tg), hemizygous (wt/tg), and control mice (wt/wt) were treated with EGCG. EGCG bound to hIAPP in vitro and induced formation of amorphous aggregates instead of amyloid fibrils. Amyloid fibrils were detected in the pancreatic islets of tg/tg mice, which was associated with disrupted islet structure and diabetes. Although pancreatic amyloid fibrils could be detected in wt/tg mice, these animals were non-diabetic. EGCG application decreased amyloid fibril intensity in wt/tg mice, however it was ineffective in tg/tg animals. Our data indicate that EGCG inhibits amyloid fibril formation in vitro and reduces fibril intensity in non-diabetic wt/tg mice. These results demonstrate a possible in vivo effectiveness of EGCG on amyloid formation and suggest an early therapeutical application.
doi_str_mv 10.1038/s41598-017-18807-8
format Article
fullrecord <record><control><sourceid>proquest_pubme</sourceid><recordid>TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_5773570</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>1988938659</sourcerecordid><originalsourceid>FETCH-LOGICAL-c540t-d43e7eef32bf4947a2f368721e11005251759924a4289e7d2ca4b5f32242cd763</originalsourceid><addsrcrecordid>eNp1kc9qGzEQxpfS0oQ0L9BDEfSSHDbVv11Jl0IwrhMINIf2LGTtrK2wK20lbcAv0WeuXKfGLVQXjZjffDOjr6reE3xDMJOfEieNkjUmoiZSYlHLV9U5xbypKaP09Ul8Vl2m9ITLaajiRL2tzqhiXLZEnlc_l5PbmGEI1mSwW-fR_lVidLVcLVbXKEI3W0gobwE5n8Enl3co9Ggy3kYw2Vlkxt0QXId6t45uSIVD23k0Hrk0QD6mpzDsJpiy64r69v728fEa5Wh82oAvKqOz8K5605shweXLfVF9_7L8trirH76u7he3D7VtOM51xxkIgJ7Rdc8VF4b2rJWCEiBkv2ZDRKMU5YZTqUB01Bq-bgpOObWdaNlF9fmgO83rEToLvgwy6Cm60cSdDsbpvzPebfUmPOtGCNYIXASuXgRi-DFDynp0yUL5Og9hTpooqVosZCsK-vEf9CnM0Zf19pRUTLaNKhQ9UDaGlCL0x2EI1nvH9cFxXRzXvx3XshR9OF3jWPLH3wKwA5BKym8gnvT-v-wvJ0q35Q</addsrcrecordid><sourcetype>Open Access Repository</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>1988938659</pqid></control><display><type>article</type><title>Epigallocatechin gallate (EGCG) reduces the intensity of pancreatic amyloid fibrils in human islet amyloid polypeptide (hIAPP) transgenic mice</title><source>MEDLINE</source><source>DOAJ Directory of Open Access Journals</source><source>Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals</source><source>Nature Free</source><source>PubMed Central</source><source>Springer Nature OA/Free Journals</source><source>Free Full-Text Journals in Chemistry</source><creator>Franko, Andras ; Rodriguez Camargo, Diana C. ; Böddrich, Annett ; Garg, Divita ; Rodriguez Camargo, Andres ; Rathkolb, Birgit ; Janik, Dirk ; Aichler, Michaela ; Feuchtinger, Annette ; Neff, Frauke ; Fuchs, Helmut ; Wanker, Erich E. ; Reif, Bernd ; Häring, Hans-Ulrich ; Peter, Andreas ; Hrabě de Angelis, Martin</creator><creatorcontrib>Franko, Andras ; Rodriguez Camargo, Diana C. ; Böddrich, Annett ; Garg, Divita ; Rodriguez Camargo, Andres ; Rathkolb, Birgit ; Janik, Dirk ; Aichler, Michaela ; Feuchtinger, Annette ; Neff, Frauke ; Fuchs, Helmut ; Wanker, Erich E. ; Reif, Bernd ; Häring, Hans-Ulrich ; Peter, Andreas ; Hrabě de Angelis, Martin</creatorcontrib><description>The formation of amyloid fibrils by human islet amyloid polypeptide protein (hIAPP) has been implicated in pancreas dysfunction and diabetes. However, efficient treatment options to reduce amyloid fibrils in vivo are still lacking. Therefore, we tested the effect of epigallocatechin gallate (EGCG) on fibril formation in vitro and in vivo . To determine the binding of hIAPP and EGCG, in vitro interaction studies were performed. To inhibit amyloid plaque formation in vivo , homozygous (tg/tg), hemizygous (wt/tg), and control mice (wt/wt) were treated with EGCG. EGCG bound to hIAPP in vitro and induced formation of amorphous aggregates instead of amyloid fibrils. Amyloid fibrils were detected in the pancreatic islets of tg/tg mice, which was associated with disrupted islet structure and diabetes. Although pancreatic amyloid fibrils could be detected in wt/tg mice, these animals were non-diabetic. EGCG application decreased amyloid fibril intensity in wt/tg mice, however it was ineffective in tg/tg animals. Our data indicate that EGCG inhibits amyloid fibril formation in vitro and reduces fibril intensity in non-diabetic wt/tg mice. These results demonstrate a possible in vivo effectiveness of EGCG on amyloid formation and suggest an early therapeutical application.</description><identifier>ISSN: 2045-2322</identifier><identifier>EISSN: 2045-2322</identifier><identifier>DOI: 10.1038/s41598-017-18807-8</identifier><identifier>PMID: 29348618</identifier><language>eng</language><publisher>London: Nature Publishing Group UK</publisher><subject>119/118 ; 13 ; 13/1 ; 13/51 ; 14/3 ; 140/131 ; 631/45/56 ; 631/57/2269 ; 64/60 ; 692/163/2743/137/1417 ; 692/4017 ; Amylin ; Amyloid - chemistry ; Amyloid - metabolism ; Amyloidosis - metabolism ; Amyloidosis - pathology ; Animals ; Biomarkers ; Catechin - analogs &amp; derivatives ; Catechin - chemistry ; Catechin - metabolism ; Catechin - pharmacology ; Data processing ; Diabetes ; Diabetes mellitus ; Epigallocatechin gallate ; Fibrillogenesis ; Humanities and Social Sciences ; Humans ; Islet Amyloid Polypeptide - genetics ; Islet Amyloid Polypeptide - metabolism ; Mice ; Mice, Transgenic ; Models, Molecular ; Molecular Conformation ; Molecular structure ; multidisciplinary ; Neuroprotective Agents - chemistry ; Neuroprotective Agents - metabolism ; Neuroprotective Agents - pharmacology ; Pancreas ; Pancreas - metabolism ; Pancreas - pathology ; Pancreas - ultrastructure ; Polypeptides ; Protein Binding ; Rodents ; Science ; Science (multidisciplinary) ; Transgenic mice</subject><ispartof>Scientific reports, 2018-01, Vol.8 (1), p.1116-12, Article 1116</ispartof><rights>The Author(s) 2018</rights><rights>2018. This work is published under http://creativecommons.org/licenses/by/4.0/ (the “License”). Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License.</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c540t-d43e7eef32bf4947a2f368721e11005251759924a4289e7d2ca4b5f32242cd763</citedby><cites>FETCH-LOGICAL-c540t-d43e7eef32bf4947a2f368721e11005251759924a4289e7d2ca4b5f32242cd763</cites><orcidid>0000-0003-0485-5439 ; 0000-0002-5143-2677 ; 0000-0002-7898-2353</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC5773570/pdf/$$EPDF$$P50$$Gpubmedcentral$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC5773570/$$EHTML$$P50$$Gpubmedcentral$$Hfree_for_read</linktohtml><link.rule.ids>230,315,729,782,786,866,887,27931,27932,41127,42196,51583,53798,53800</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/29348618$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Franko, Andras</creatorcontrib><creatorcontrib>Rodriguez Camargo, Diana C.</creatorcontrib><creatorcontrib>Böddrich, Annett</creatorcontrib><creatorcontrib>Garg, Divita</creatorcontrib><creatorcontrib>Rodriguez Camargo, Andres</creatorcontrib><creatorcontrib>Rathkolb, Birgit</creatorcontrib><creatorcontrib>Janik, Dirk</creatorcontrib><creatorcontrib>Aichler, Michaela</creatorcontrib><creatorcontrib>Feuchtinger, Annette</creatorcontrib><creatorcontrib>Neff, Frauke</creatorcontrib><creatorcontrib>Fuchs, Helmut</creatorcontrib><creatorcontrib>Wanker, Erich E.</creatorcontrib><creatorcontrib>Reif, Bernd</creatorcontrib><creatorcontrib>Häring, Hans-Ulrich</creatorcontrib><creatorcontrib>Peter, Andreas</creatorcontrib><creatorcontrib>Hrabě de Angelis, Martin</creatorcontrib><title>Epigallocatechin gallate (EGCG) reduces the intensity of pancreatic amyloid fibrils in human islet amyloid polypeptide (hIAPP) transgenic mice</title><title>Scientific reports</title><addtitle>Sci Rep</addtitle><addtitle>Sci Rep</addtitle><description>The formation of amyloid fibrils by human islet amyloid polypeptide protein (hIAPP) has been implicated in pancreas dysfunction and diabetes. However, efficient treatment options to reduce amyloid fibrils in vivo are still lacking. Therefore, we tested the effect of epigallocatechin gallate (EGCG) on fibril formation in vitro and in vivo . To determine the binding of hIAPP and EGCG, in vitro interaction studies were performed. To inhibit amyloid plaque formation in vivo , homozygous (tg/tg), hemizygous (wt/tg), and control mice (wt/wt) were treated with EGCG. EGCG bound to hIAPP in vitro and induced formation of amorphous aggregates instead of amyloid fibrils. Amyloid fibrils were detected in the pancreatic islets of tg/tg mice, which was associated with disrupted islet structure and diabetes. Although pancreatic amyloid fibrils could be detected in wt/tg mice, these animals were non-diabetic. EGCG application decreased amyloid fibril intensity in wt/tg mice, however it was ineffective in tg/tg animals. Our data indicate that EGCG inhibits amyloid fibril formation in vitro and reduces fibril intensity in non-diabetic wt/tg mice. These results demonstrate a possible in vivo effectiveness of EGCG on amyloid formation and suggest an early therapeutical application.</description><subject>119/118</subject><subject>13</subject><subject>13/1</subject><subject>13/51</subject><subject>14/3</subject><subject>140/131</subject><subject>631/45/56</subject><subject>631/57/2269</subject><subject>64/60</subject><subject>692/163/2743/137/1417</subject><subject>692/4017</subject><subject>Amylin</subject><subject>Amyloid - chemistry</subject><subject>Amyloid - metabolism</subject><subject>Amyloidosis - metabolism</subject><subject>Amyloidosis - pathology</subject><subject>Animals</subject><subject>Biomarkers</subject><subject>Catechin - analogs &amp; derivatives</subject><subject>Catechin - chemistry</subject><subject>Catechin - metabolism</subject><subject>Catechin - pharmacology</subject><subject>Data processing</subject><subject>Diabetes</subject><subject>Diabetes mellitus</subject><subject>Epigallocatechin gallate</subject><subject>Fibrillogenesis</subject><subject>Humanities and Social Sciences</subject><subject>Humans</subject><subject>Islet Amyloid Polypeptide - genetics</subject><subject>Islet Amyloid Polypeptide - metabolism</subject><subject>Mice</subject><subject>Mice, Transgenic</subject><subject>Models, Molecular</subject><subject>Molecular Conformation</subject><subject>Molecular structure</subject><subject>multidisciplinary</subject><subject>Neuroprotective Agents - chemistry</subject><subject>Neuroprotective Agents - metabolism</subject><subject>Neuroprotective Agents - pharmacology</subject><subject>Pancreas</subject><subject>Pancreas - metabolism</subject><subject>Pancreas - pathology</subject><subject>Pancreas - ultrastructure</subject><subject>Polypeptides</subject><subject>Protein Binding</subject><subject>Rodents</subject><subject>Science</subject><subject>Science (multidisciplinary)</subject><subject>Transgenic mice</subject><issn>2045-2322</issn><issn>2045-2322</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2018</creationdate><recordtype>article</recordtype><sourceid>C6C</sourceid><sourceid>EIF</sourceid><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>AZQEC</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><sourceid>GNUQQ</sourceid><recordid>eNp1kc9qGzEQxpfS0oQ0L9BDEfSSHDbVv11Jl0IwrhMINIf2LGTtrK2wK20lbcAv0WeuXKfGLVQXjZjffDOjr6reE3xDMJOfEieNkjUmoiZSYlHLV9U5xbypKaP09Ul8Vl2m9ITLaajiRL2tzqhiXLZEnlc_l5PbmGEI1mSwW-fR_lVidLVcLVbXKEI3W0gobwE5n8Enl3co9Ggy3kYw2Vlkxt0QXId6t45uSIVD23k0Hrk0QD6mpzDsJpiy64r69v728fEa5Wh82oAvKqOz8K5605shweXLfVF9_7L8trirH76u7he3D7VtOM51xxkIgJ7Rdc8VF4b2rJWCEiBkv2ZDRKMU5YZTqUB01Bq-bgpOObWdaNlF9fmgO83rEToLvgwy6Cm60cSdDsbpvzPebfUmPOtGCNYIXASuXgRi-DFDynp0yUL5Og9hTpooqVosZCsK-vEf9CnM0Zf19pRUTLaNKhQ9UDaGlCL0x2EI1nvH9cFxXRzXvx3XshR9OF3jWPLH3wKwA5BKym8gnvT-v-wvJ0q35Q</recordid><startdate>20180118</startdate><enddate>20180118</enddate><creator>Franko, Andras</creator><creator>Rodriguez Camargo, Diana C.</creator><creator>Böddrich, Annett</creator><creator>Garg, Divita</creator><creator>Rodriguez Camargo, Andres</creator><creator>Rathkolb, Birgit</creator><creator>Janik, Dirk</creator><creator>Aichler, Michaela</creator><creator>Feuchtinger, Annette</creator><creator>Neff, Frauke</creator><creator>Fuchs, Helmut</creator><creator>Wanker, Erich E.</creator><creator>Reif, Bernd</creator><creator>Häring, Hans-Ulrich</creator><creator>Peter, Andreas</creator><creator>Hrabě de Angelis, Martin</creator><general>Nature Publishing Group UK</general><general>Nature Publishing Group</general><scope>C6C</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>3V.</scope><scope>7X7</scope><scope>7XB</scope><scope>88A</scope><scope>88E</scope><scope>88I</scope><scope>8FE</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BHPHI</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>LK8</scope><scope>M0S</scope><scope>M1P</scope><scope>M2P</scope><scope>M7P</scope><scope>PIMPY</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>Q9U</scope><scope>7X8</scope><scope>5PM</scope><orcidid>https://orcid.org/0000-0003-0485-5439</orcidid><orcidid>https://orcid.org/0000-0002-5143-2677</orcidid><orcidid>https://orcid.org/0000-0002-7898-2353</orcidid></search><sort><creationdate>20180118</creationdate><title>Epigallocatechin gallate (EGCG) reduces the intensity of pancreatic amyloid fibrils in human islet amyloid polypeptide (hIAPP) transgenic mice</title><author>Franko, Andras ; Rodriguez Camargo, Diana C. ; Böddrich, Annett ; Garg, Divita ; Rodriguez Camargo, Andres ; Rathkolb, Birgit ; Janik, Dirk ; Aichler, Michaela ; Feuchtinger, Annette ; Neff, Frauke ; Fuchs, Helmut ; Wanker, Erich E. ; Reif, Bernd ; Häring, Hans-Ulrich ; Peter, Andreas ; Hrabě de Angelis, Martin</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c540t-d43e7eef32bf4947a2f368721e11005251759924a4289e7d2ca4b5f32242cd763</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2018</creationdate><topic>119/118</topic><topic>13</topic><topic>13/1</topic><topic>13/51</topic><topic>14/3</topic><topic>140/131</topic><topic>631/45/56</topic><topic>631/57/2269</topic><topic>64/60</topic><topic>692/163/2743/137/1417</topic><topic>692/4017</topic><topic>Amylin</topic><topic>Amyloid - chemistry</topic><topic>Amyloid - metabolism</topic><topic>Amyloidosis - metabolism</topic><topic>Amyloidosis - pathology</topic><topic>Animals</topic><topic>Biomarkers</topic><topic>Catechin - analogs &amp; derivatives</topic><topic>Catechin - chemistry</topic><topic>Catechin - metabolism</topic><topic>Catechin - pharmacology</topic><topic>Data processing</topic><topic>Diabetes</topic><topic>Diabetes mellitus</topic><topic>Epigallocatechin gallate</topic><topic>Fibrillogenesis</topic><topic>Humanities and Social Sciences</topic><topic>Humans</topic><topic>Islet Amyloid Polypeptide - genetics</topic><topic>Islet Amyloid Polypeptide - metabolism</topic><topic>Mice</topic><topic>Mice, Transgenic</topic><topic>Models, Molecular</topic><topic>Molecular Conformation</topic><topic>Molecular structure</topic><topic>multidisciplinary</topic><topic>Neuroprotective Agents - chemistry</topic><topic>Neuroprotective Agents - metabolism</topic><topic>Neuroprotective Agents - pharmacology</topic><topic>Pancreas</topic><topic>Pancreas - metabolism</topic><topic>Pancreas - pathology</topic><topic>Pancreas - ultrastructure</topic><topic>Polypeptides</topic><topic>Protein Binding</topic><topic>Rodents</topic><topic>Science</topic><topic>Science (multidisciplinary)</topic><topic>Transgenic mice</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Franko, Andras</creatorcontrib><creatorcontrib>Rodriguez Camargo, Diana C.</creatorcontrib><creatorcontrib>Böddrich, Annett</creatorcontrib><creatorcontrib>Garg, Divita</creatorcontrib><creatorcontrib>Rodriguez Camargo, Andres</creatorcontrib><creatorcontrib>Rathkolb, Birgit</creatorcontrib><creatorcontrib>Janik, Dirk</creatorcontrib><creatorcontrib>Aichler, Michaela</creatorcontrib><creatorcontrib>Feuchtinger, Annette</creatorcontrib><creatorcontrib>Neff, Frauke</creatorcontrib><creatorcontrib>Fuchs, Helmut</creatorcontrib><creatorcontrib>Wanker, Erich E.</creatorcontrib><creatorcontrib>Reif, Bernd</creatorcontrib><creatorcontrib>Häring, Hans-Ulrich</creatorcontrib><creatorcontrib>Peter, Andreas</creatorcontrib><creatorcontrib>Hrabě de Angelis, Martin</creatorcontrib><collection>Springer Nature OA/Free Journals</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>ProQuest Central (Corporate)</collection><collection>Health &amp; Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Biology Database (Alumni Edition)</collection><collection>Medical Database (Alumni Edition)</collection><collection>Science Database (Alumni Edition)</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Natural Science Collection</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>ProQuest Central (Alumni Edition)</collection><collection>ProQuest Central UK/Ireland</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>ProQuest Central</collection><collection>Natural Science Collection</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central Korea</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Health &amp; Medical Complete (Alumni)</collection><collection>ProQuest Biological Science Collection</collection><collection>Health &amp; Medical Collection (Alumni Edition)</collection><collection>Medical Database</collection><collection>Science Database</collection><collection>Biological Science Database</collection><collection>Access via ProQuest (Open Access)</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>ProQuest Central Basic</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Scientific reports</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Franko, Andras</au><au>Rodriguez Camargo, Diana C.</au><au>Böddrich, Annett</au><au>Garg, Divita</au><au>Rodriguez Camargo, Andres</au><au>Rathkolb, Birgit</au><au>Janik, Dirk</au><au>Aichler, Michaela</au><au>Feuchtinger, Annette</au><au>Neff, Frauke</au><au>Fuchs, Helmut</au><au>Wanker, Erich E.</au><au>Reif, Bernd</au><au>Häring, Hans-Ulrich</au><au>Peter, Andreas</au><au>Hrabě de Angelis, Martin</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Epigallocatechin gallate (EGCG) reduces the intensity of pancreatic amyloid fibrils in human islet amyloid polypeptide (hIAPP) transgenic mice</atitle><jtitle>Scientific reports</jtitle><stitle>Sci Rep</stitle><addtitle>Sci Rep</addtitle><date>2018-01-18</date><risdate>2018</risdate><volume>8</volume><issue>1</issue><spage>1116</spage><epage>12</epage><pages>1116-12</pages><artnum>1116</artnum><issn>2045-2322</issn><eissn>2045-2322</eissn><abstract>The formation of amyloid fibrils by human islet amyloid polypeptide protein (hIAPP) has been implicated in pancreas dysfunction and diabetes. However, efficient treatment options to reduce amyloid fibrils in vivo are still lacking. Therefore, we tested the effect of epigallocatechin gallate (EGCG) on fibril formation in vitro and in vivo . To determine the binding of hIAPP and EGCG, in vitro interaction studies were performed. To inhibit amyloid plaque formation in vivo , homozygous (tg/tg), hemizygous (wt/tg), and control mice (wt/wt) were treated with EGCG. EGCG bound to hIAPP in vitro and induced formation of amorphous aggregates instead of amyloid fibrils. Amyloid fibrils were detected in the pancreatic islets of tg/tg mice, which was associated with disrupted islet structure and diabetes. Although pancreatic amyloid fibrils could be detected in wt/tg mice, these animals were non-diabetic. EGCG application decreased amyloid fibril intensity in wt/tg mice, however it was ineffective in tg/tg animals. Our data indicate that EGCG inhibits amyloid fibril formation in vitro and reduces fibril intensity in non-diabetic wt/tg mice. These results demonstrate a possible in vivo effectiveness of EGCG on amyloid formation and suggest an early therapeutical application.</abstract><cop>London</cop><pub>Nature Publishing Group UK</pub><pmid>29348618</pmid><doi>10.1038/s41598-017-18807-8</doi><tpages>12</tpages><orcidid>https://orcid.org/0000-0003-0485-5439</orcidid><orcidid>https://orcid.org/0000-0002-5143-2677</orcidid><orcidid>https://orcid.org/0000-0002-7898-2353</orcidid><oa>free_for_read</oa></addata></record>
fulltext fulltext
identifier ISSN: 2045-2322
ispartof Scientific reports, 2018-01, Vol.8 (1), p.1116-12, Article 1116
issn 2045-2322
2045-2322
language eng
recordid cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_5773570
source MEDLINE; DOAJ Directory of Open Access Journals; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; Nature Free; PubMed Central; Springer Nature OA/Free Journals; Free Full-Text Journals in Chemistry
subjects 119/118
13
13/1
13/51
14/3
140/131
631/45/56
631/57/2269
64/60
692/163/2743/137/1417
692/4017
Amylin
Amyloid - chemistry
Amyloid - metabolism
Amyloidosis - metabolism
Amyloidosis - pathology
Animals
Biomarkers
Catechin - analogs & derivatives
Catechin - chemistry
Catechin - metabolism
Catechin - pharmacology
Data processing
Diabetes
Diabetes mellitus
Epigallocatechin gallate
Fibrillogenesis
Humanities and Social Sciences
Humans
Islet Amyloid Polypeptide - genetics
Islet Amyloid Polypeptide - metabolism
Mice
Mice, Transgenic
Models, Molecular
Molecular Conformation
Molecular structure
multidisciplinary
Neuroprotective Agents - chemistry
Neuroprotective Agents - metabolism
Neuroprotective Agents - pharmacology
Pancreas
Pancreas - metabolism
Pancreas - pathology
Pancreas - ultrastructure
Polypeptides
Protein Binding
Rodents
Science
Science (multidisciplinary)
Transgenic mice
title Epigallocatechin gallate (EGCG) reduces the intensity of pancreatic amyloid fibrils in human islet amyloid polypeptide (hIAPP) transgenic mice
url https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2024-12-05T21%3A12%3A35IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_pubme&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Epigallocatechin%20gallate%20(EGCG)%20reduces%20the%20intensity%20of%20pancreatic%20amyloid%20fibrils%20in%20human%20islet%20amyloid%20polypeptide%20(hIAPP)%20transgenic%20mice&rft.jtitle=Scientific%20reports&rft.au=Franko,%20Andras&rft.date=2018-01-18&rft.volume=8&rft.issue=1&rft.spage=1116&rft.epage=12&rft.pages=1116-12&rft.artnum=1116&rft.issn=2045-2322&rft.eissn=2045-2322&rft_id=info:doi/10.1038/s41598-017-18807-8&rft_dat=%3Cproquest_pubme%3E1988938659%3C/proquest_pubme%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=1988938659&rft_id=info:pmid/29348618&rfr_iscdi=true