Naringenin Inhibits the Aggregation of Expanded Polyglutamine Tract-Containing Protein through the Induction of Endoplasmic Reticulum Chaperone GRP78
Polyglutamine (polyQ) diseases are inherited neurodegenerative diseases characterized by the aggregation of proteins containing expanded polyQ tract. Recently, we have shown that GRP78, the endoplasmic reticulum (ER) chaperone, was significantly decreased in the cells expressing enhanced green fluor...
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| Veröffentlicht in: | Biological & pharmaceutical bulletin 2012/10/01, Vol.35(10), pp.1836-1840 |
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| creator | Yamagishi, Nobuyuki Yamamoto, Yoko Noda, Chika Hatayama, Takumi |
| description | Polyglutamine (polyQ) diseases are inherited neurodegenerative diseases characterized by the aggregation of proteins containing expanded polyQ tract. Recently, we have shown that GRP78, the endoplasmic reticulum (ER) chaperone, was significantly decreased in the cells expressing enhanced green fluorescent protein with a pathological-length polyQ tract (EGFP-polyQ97), but not with a non-pathological-length polyQ tract (EGFP-polyQ24), and the expression levels of GRP78 were inversely related to the aggregation of EGFP-polyQ97. In this study, we performed the screening for compounds that modulate the GRP78 expression in herbal medicines, and found that naringenin, one of the major constitutions of Kanzo (Glycyrrhizae Radix), induced the expression of GRP78 in several mammalian cells. Furthermore, naringenin suppressed the protein aggregation caused by EGFP-polyQ97 in mammalian cells. These findings suggested that naringenin seemed to be a new inducer of GRP78 in mammalian cells, and may be a potential therapeutic agent for diseases caused by ER stress such as polyQ diseases. |
| doi_str_mv | 10.1248/bpb.b12-00451 |
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Recently, we have shown that GRP78, the endoplasmic reticulum (ER) chaperone, was significantly decreased in the cells expressing enhanced green fluorescent protein with a pathological-length polyQ tract (EGFP-polyQ97), but not with a non-pathological-length polyQ tract (EGFP-polyQ24), and the expression levels of GRP78 were inversely related to the aggregation of EGFP-polyQ97. In this study, we performed the screening for compounds that modulate the GRP78 expression in herbal medicines, and found that naringenin, one of the major constitutions of Kanzo (Glycyrrhizae Radix), induced the expression of GRP78 in several mammalian cells. Furthermore, naringenin suppressed the protein aggregation caused by EGFP-polyQ97 in mammalian cells. These findings suggested that naringenin seemed to be a new inducer of GRP78 in mammalian cells, and may be a potential therapeutic agent for diseases caused by ER stress such as polyQ diseases.</description><identifier>ISSN: 0918-6158</identifier><identifier>EISSN: 1347-5215</identifier><identifier>DOI: 10.1248/bpb.b12-00451</identifier><identifier>PMID: 23037174</identifier><language>eng</language><publisher>Japan: The Pharmaceutical Society of Japan</publisher><subject>Animals ; Cell Line ; Cercopithecus aethiops ; COS Cells ; Endoplasmic Reticulum - drug effects ; Endoplasmic Reticulum - metabolism ; Flavanones - pharmacology ; Green Fluorescent Proteins - metabolism ; GRP78 ; Heat-Shock Proteins - metabolism ; HeLa Cells ; Humans ; Mice ; naringenin ; Peptides - metabolism ; polyglutamine disease ; protein aggregation</subject><ispartof>Biological and Pharmaceutical Bulletin, 2012/10/01, Vol.35(10), pp.1836-1840</ispartof><rights>2012 The Pharmaceutical Society of Japan</rights><rights>Copyright Japan Science and Technology Agency 2012</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c703t-ed56e5b87e22505ba84f07f3836ea10a37ae409c1b98614f07367f6adda0cc643</citedby><cites>FETCH-LOGICAL-c703t-ed56e5b87e22505ba84f07f3836ea10a37ae409c1b98614f07367f6adda0cc643</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,1883,27924,27925</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/23037174$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Yamagishi, Nobuyuki</creatorcontrib><creatorcontrib>Yamamoto, Yoko</creatorcontrib><creatorcontrib>Noda, Chika</creatorcontrib><creatorcontrib>Hatayama, Takumi</creatorcontrib><creatorcontrib>Department of Biochemistry & Molecular Biology</creatorcontrib><creatorcontrib>Kyoto Pharmaceutical University</creatorcontrib><creatorcontrib>Division of Biological Sciences</creatorcontrib><title>Naringenin Inhibits the Aggregation of Expanded Polyglutamine Tract-Containing Protein through the Induction of Endoplasmic Reticulum Chaperone GRP78</title><title>Biological & pharmaceutical bulletin</title><addtitle>Biol Pharm Bull</addtitle><description>Polyglutamine (polyQ) diseases are inherited neurodegenerative diseases characterized by the aggregation of proteins containing expanded polyQ tract. Recently, we have shown that GRP78, the endoplasmic reticulum (ER) chaperone, was significantly decreased in the cells expressing enhanced green fluorescent protein with a pathological-length polyQ tract (EGFP-polyQ97), but not with a non-pathological-length polyQ tract (EGFP-polyQ24), and the expression levels of GRP78 were inversely related to the aggregation of EGFP-polyQ97. In this study, we performed the screening for compounds that modulate the GRP78 expression in herbal medicines, and found that naringenin, one of the major constitutions of Kanzo (Glycyrrhizae Radix), induced the expression of GRP78 in several mammalian cells. Furthermore, naringenin suppressed the protein aggregation caused by EGFP-polyQ97 in mammalian cells. These findings suggested that naringenin seemed to be a new inducer of GRP78 in mammalian cells, and may be a potential therapeutic agent for diseases caused by ER stress such as polyQ diseases.</description><subject>Animals</subject><subject>Cell Line</subject><subject>Cercopithecus aethiops</subject><subject>COS Cells</subject><subject>Endoplasmic Reticulum - drug effects</subject><subject>Endoplasmic Reticulum - metabolism</subject><subject>Flavanones - pharmacology</subject><subject>Green Fluorescent Proteins - metabolism</subject><subject>GRP78</subject><subject>Heat-Shock Proteins - metabolism</subject><subject>HeLa Cells</subject><subject>Humans</subject><subject>Mice</subject><subject>naringenin</subject><subject>Peptides - metabolism</subject><subject>polyglutamine disease</subject><subject>protein aggregation</subject><issn>0918-6158</issn><issn>1347-5215</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2012</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpdkcFu1DAURSMEotPCki2KxIZNih3bibOspu0wUgWjqqwtx3lJPHLsYDsS_RD-F89MGSQ29uIdnXf1bpZ9wOgal5R_aef2usVlgRBl-FW2woTWBSsxe52tUIN5UWHGL7LLEPYIoRqV5G12URJEalzTVfb7m_TaDmC1zbd21K2OIY8j5DfD4GGQUTubuz6_-zVL20GX75x5HswS5aQt5E9eqlisnY1SJ8WQ77yLkFxx9G4ZxqNqa7tFnUW2c7ORYdIqf4So1WKWKV-PcgbvknHzuKv5u-xNL02A9y__Vfbj_u5p_bV4-L7Zrm8eClUjEgvoWAWs5TWUJUOslZz2qO4JJxVIjCSpJVDUKNw2vMKHGanqvpJdJ5FSFSVX2eeTd_bu5wIhikkHBcZIC24JAqOGUF4yjhP66T907xZvUzqBKW0IRxVvElWcKOVdCB56MXs9Sf-cVOLQl0h9idSXOPaV-I8v1qWdoDvTfwtKwOYEpKlW0jhr0t3_7VahbrUzTpToKCUsLUKECJyOkB6KMEcNq0gy3Z5M-xDlAOdV0qcSDByDEXbImd5zwvNYjdILsOQPUrjA4A</recordid><startdate>20121001</startdate><enddate>20121001</enddate><creator>Yamagishi, Nobuyuki</creator><creator>Yamamoto, Yoko</creator><creator>Noda, Chika</creator><creator>Hatayama, Takumi</creator><general>The Pharmaceutical Society of Japan</general><general>Pharmaceutical Society of Japan</general><general>Japan Science and Technology Agency</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>7QP</scope><scope>7QR</scope><scope>7TK</scope><scope>7U9</scope><scope>8FD</scope><scope>FR3</scope><scope>H94</scope><scope>P64</scope><scope>7X8</scope></search><sort><creationdate>20121001</creationdate><title>Naringenin Inhibits the Aggregation of Expanded Polyglutamine Tract-Containing Protein through the Induction of Endoplasmic Reticulum Chaperone GRP78</title><author>Yamagishi, Nobuyuki ; Yamamoto, Yoko ; Noda, Chika ; Hatayama, Takumi</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c703t-ed56e5b87e22505ba84f07f3836ea10a37ae409c1b98614f07367f6adda0cc643</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2012</creationdate><topic>Animals</topic><topic>Cell Line</topic><topic>Cercopithecus aethiops</topic><topic>COS Cells</topic><topic>Endoplasmic Reticulum - drug effects</topic><topic>Endoplasmic Reticulum - metabolism</topic><topic>Flavanones - pharmacology</topic><topic>Green Fluorescent Proteins - metabolism</topic><topic>GRP78</topic><topic>Heat-Shock Proteins - metabolism</topic><topic>HeLa Cells</topic><topic>Humans</topic><topic>Mice</topic><topic>naringenin</topic><topic>Peptides - metabolism</topic><topic>polyglutamine disease</topic><topic>protein aggregation</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Yamagishi, Nobuyuki</creatorcontrib><creatorcontrib>Yamamoto, Yoko</creatorcontrib><creatorcontrib>Noda, Chika</creatorcontrib><creatorcontrib>Hatayama, Takumi</creatorcontrib><creatorcontrib>Department of Biochemistry & Molecular Biology</creatorcontrib><creatorcontrib>Kyoto Pharmaceutical University</creatorcontrib><creatorcontrib>Division of Biological Sciences</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Calcium & Calcified Tissue Abstracts</collection><collection>Chemoreception Abstracts</collection><collection>Neurosciences Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>Technology Research Database</collection><collection>Engineering Research Database</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Biological & pharmaceutical bulletin</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Yamagishi, Nobuyuki</au><au>Yamamoto, Yoko</au><au>Noda, Chika</au><au>Hatayama, Takumi</au><aucorp>Department of Biochemistry & Molecular Biology</aucorp><aucorp>Kyoto Pharmaceutical University</aucorp><aucorp>Division of Biological Sciences</aucorp><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Naringenin Inhibits the Aggregation of Expanded Polyglutamine Tract-Containing Protein through the Induction of Endoplasmic Reticulum Chaperone GRP78</atitle><jtitle>Biological & pharmaceutical bulletin</jtitle><addtitle>Biol Pharm Bull</addtitle><date>2012-10-01</date><risdate>2012</risdate><volume>35</volume><issue>10</issue><spage>1836</spage><epage>1840</epage><pages>1836-1840</pages><issn>0918-6158</issn><eissn>1347-5215</eissn><abstract>Polyglutamine (polyQ) diseases are inherited neurodegenerative diseases characterized by the aggregation of proteins containing expanded polyQ tract. Recently, we have shown that GRP78, the endoplasmic reticulum (ER) chaperone, was significantly decreased in the cells expressing enhanced green fluorescent protein with a pathological-length polyQ tract (EGFP-polyQ97), but not with a non-pathological-length polyQ tract (EGFP-polyQ24), and the expression levels of GRP78 were inversely related to the aggregation of EGFP-polyQ97. In this study, we performed the screening for compounds that modulate the GRP78 expression in herbal medicines, and found that naringenin, one of the major constitutions of Kanzo (Glycyrrhizae Radix), induced the expression of GRP78 in several mammalian cells. Furthermore, naringenin suppressed the protein aggregation caused by EGFP-polyQ97 in mammalian cells. 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| subjects | Animals Cell Line Cercopithecus aethiops COS Cells Endoplasmic Reticulum - drug effects Endoplasmic Reticulum - metabolism Flavanones - pharmacology Green Fluorescent Proteins - metabolism GRP78 Heat-Shock Proteins - metabolism HeLa Cells Humans Mice naringenin Peptides - metabolism polyglutamine disease protein aggregation |
| title | Naringenin Inhibits the Aggregation of Expanded Polyglutamine Tract-Containing Protein through the Induction of Endoplasmic Reticulum Chaperone GRP78 |
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