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...
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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 |
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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 & 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 & 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 & 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 & 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 & Medical Complete (Alumni)</collection><collection>ProQuest Biological Science Collection</collection><collection>Health & 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> |
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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 |