Overexpression of GRP78 protects glial cells from endoplasmic reticulum stress
► GRP78 overexpression prior to injury protects C6 glioma cells from ER stress. ► GRP78 expression increases following exposure to high concentrations of glutamate. ► Transient expression of GRP78 protects against tunicamycin and glutamate injury. Endoplasmic reticulum (ER) stress induces apoptotic...
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| Veröffentlicht in: | Neuroscience letters 2011-10, Vol.504 (3), p.271-276 |
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| container_title | Neuroscience letters |
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| creator | Suyama, Kaori Watanabe, Masahiko Sakabe, Kou Okada, Yoshinori Matsuyama, Daisuke Kuroiwa, Masahiro Mochida, Joji |
| description | ► GRP78 overexpression prior to injury protects C6 glioma cells from ER stress. ► GRP78 expression increases following exposure to high concentrations of glutamate. ► Transient expression of GRP78 protects against tunicamycin and glutamate injury.
Endoplasmic reticulum (ER) stress induces apoptotic cell death by causing the accumulation of structurally abnormal proteins. The 78-kDa glucose-regulated protein (GRP78) is an ER chaperone that regulates protein folding in the ER and has been suggested to contribute to cell survival. Using the rat C6 glioma cell line and flow cytometry, we assessed GRP78 expression following tunicamycin- and glutamate-induced ER stress. The results showed that GRP78 expression is upregulated following ER stress and has protective effects on injured glial cells. Annexin V and propidium iodide labeling revealed cells transiently expressing GRP78 prior to injury were protected against high-concentrations of tunicamycin and glutamate within 72
h. Our findings support the hypothesis that GRP78 inhibits cell death associated with ER stress. |
| doi_str_mv | 10.1016/j.neulet.2011.09.045 |
| format | Article |
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Endoplasmic reticulum (ER) stress induces apoptotic cell death by causing the accumulation of structurally abnormal proteins. The 78-kDa glucose-regulated protein (GRP78) is an ER chaperone that regulates protein folding in the ER and has been suggested to contribute to cell survival. Using the rat C6 glioma cell line and flow cytometry, we assessed GRP78 expression following tunicamycin- and glutamate-induced ER stress. The results showed that GRP78 expression is upregulated following ER stress and has protective effects on injured glial cells. Annexin V and propidium iodide labeling revealed cells transiently expressing GRP78 prior to injury were protected against high-concentrations of tunicamycin and glutamate within 72
h. Our findings support the hypothesis that GRP78 inhibits cell death associated with ER stress.</description><identifier>ISSN: 0304-3940</identifier><identifier>EISSN: 1872-7972</identifier><identifier>DOI: 10.1016/j.neulet.2011.09.045</identifier><identifier>PMID: 21970967</identifier><language>eng</language><publisher>Ireland: Elsevier Ireland Ltd</publisher><subject>Animals ; Apoptosis ; Apoptosis - drug effects ; Apoptosis - physiology ; Cell Line, Tumor - drug effects ; Cell Line, Tumor - metabolism ; Endoplasmic reticulum stress ; Endoplasmic Reticulum Stress - drug effects ; Endoplasmic Reticulum Stress - genetics ; Endoplasmic Reticulum Stress - physiology ; Genes, Synthetic ; Glial cell ; Glioma - pathology ; Glutamate ; Glutamic Acid - toxicity ; GRP78 ; Heat-Shock Proteins - biosynthesis ; Heat-Shock Proteins - genetics ; Heat-Shock Proteins - physiology ; Nerve Tissue Proteins - biosynthesis ; Nerve Tissue Proteins - genetics ; Nerve Tissue Proteins - physiology ; Neurotoxins - toxicity ; Rats ; Recombinant Fusion Proteins - biosynthesis ; Recombinant Fusion Proteins - genetics ; Tunicamycin ; Tunicamycin - toxicity</subject><ispartof>Neuroscience letters, 2011-10, Vol.504 (3), p.271-276</ispartof><rights>2011 Elsevier Ireland Ltd</rights><rights>Copyright © 2011 Elsevier Ireland Ltd. All rights reserved.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c459t-99b62dfc3e94321a6674c8e9d826a1d133613abe09a50f45616b5ed7d6e816273</citedby><cites>FETCH-LOGICAL-c459t-99b62dfc3e94321a6674c8e9d826a1d133613abe09a50f45616b5ed7d6e816273</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/j.neulet.2011.09.045$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,780,784,3550,27924,27925,45995</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/21970967$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Suyama, Kaori</creatorcontrib><creatorcontrib>Watanabe, Masahiko</creatorcontrib><creatorcontrib>Sakabe, Kou</creatorcontrib><creatorcontrib>Okada, Yoshinori</creatorcontrib><creatorcontrib>Matsuyama, Daisuke</creatorcontrib><creatorcontrib>Kuroiwa, Masahiro</creatorcontrib><creatorcontrib>Mochida, Joji</creatorcontrib><title>Overexpression of GRP78 protects glial cells from endoplasmic reticulum stress</title><title>Neuroscience letters</title><addtitle>Neurosci Lett</addtitle><description>► GRP78 overexpression prior to injury protects C6 glioma cells from ER stress. ► GRP78 expression increases following exposure to high concentrations of glutamate. ► Transient expression of GRP78 protects against tunicamycin and glutamate injury.
Endoplasmic reticulum (ER) stress induces apoptotic cell death by causing the accumulation of structurally abnormal proteins. The 78-kDa glucose-regulated protein (GRP78) is an ER chaperone that regulates protein folding in the ER and has been suggested to contribute to cell survival. Using the rat C6 glioma cell line and flow cytometry, we assessed GRP78 expression following tunicamycin- and glutamate-induced ER stress. The results showed that GRP78 expression is upregulated following ER stress and has protective effects on injured glial cells. Annexin V and propidium iodide labeling revealed cells transiently expressing GRP78 prior to injury were protected against high-concentrations of tunicamycin and glutamate within 72
h. Our findings support the hypothesis that GRP78 inhibits cell death associated with ER stress.</description><subject>Animals</subject><subject>Apoptosis</subject><subject>Apoptosis - drug effects</subject><subject>Apoptosis - physiology</subject><subject>Cell Line, Tumor - drug effects</subject><subject>Cell Line, Tumor - metabolism</subject><subject>Endoplasmic reticulum stress</subject><subject>Endoplasmic Reticulum Stress - drug effects</subject><subject>Endoplasmic Reticulum Stress - genetics</subject><subject>Endoplasmic Reticulum Stress - physiology</subject><subject>Genes, Synthetic</subject><subject>Glial cell</subject><subject>Glioma - pathology</subject><subject>Glutamate</subject><subject>Glutamic Acid - toxicity</subject><subject>GRP78</subject><subject>Heat-Shock Proteins - biosynthesis</subject><subject>Heat-Shock Proteins - genetics</subject><subject>Heat-Shock Proteins - physiology</subject><subject>Nerve Tissue Proteins - biosynthesis</subject><subject>Nerve Tissue Proteins - genetics</subject><subject>Nerve Tissue Proteins - physiology</subject><subject>Neurotoxins - toxicity</subject><subject>Rats</subject><subject>Recombinant Fusion Proteins - biosynthesis</subject><subject>Recombinant Fusion Proteins - genetics</subject><subject>Tunicamycin</subject><subject>Tunicamycin - toxicity</subject><issn>0304-3940</issn><issn>1872-7972</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2011</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kE1LwzAYx4Mobk6_gUhunlqftGnSXAQRnYI4ET2HLHkqGX2ZSTv029ux6dHTc_m_PT9CzhmkDJi4WqUtDjX2aQaMpaBS4MUBmbJSZolUMjskU8iBJ7niMCEnMa4AoGAFPyaTjCkJSsgpeV5sMODXOmCMvmtpV9H564ss6Tp0Pdo-0o_am5parOtIq9A1FFvXrWsTG29pwN7boR4aGvttxCk5qkwd8Wx_Z-T9_u7t9iF5Wswfb2-eEssL1SdKLUXmKpuj4nnGjBCS2xKVKzNhmGN5LlhulgjKFFDxQjCxLNBJJ7BkIpP5jFzucseZnwPGXjc-bjeaFrshagWcK8UFjEq-U9rQxRiw0uvgGxO-NQO9BalXegdSb0FqUHoEOdou9gXDskH3Z_olNwqudwIc39x4DDpaj61F58PITbvO_9_wA6fmhlM</recordid><startdate>20111031</startdate><enddate>20111031</enddate><creator>Suyama, Kaori</creator><creator>Watanabe, Masahiko</creator><creator>Sakabe, Kou</creator><creator>Okada, Yoshinori</creator><creator>Matsuyama, Daisuke</creator><creator>Kuroiwa, Masahiro</creator><creator>Mochida, Joji</creator><general>Elsevier Ireland Ltd</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>7TK</scope></search><sort><creationdate>20111031</creationdate><title>Overexpression of GRP78 protects glial cells from endoplasmic reticulum stress</title><author>Suyama, Kaori ; Watanabe, Masahiko ; Sakabe, Kou ; Okada, Yoshinori ; Matsuyama, Daisuke ; Kuroiwa, Masahiro ; Mochida, Joji</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c459t-99b62dfc3e94321a6674c8e9d826a1d133613abe09a50f45616b5ed7d6e816273</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2011</creationdate><topic>Animals</topic><topic>Apoptosis</topic><topic>Apoptosis - drug effects</topic><topic>Apoptosis - physiology</topic><topic>Cell Line, Tumor - drug effects</topic><topic>Cell Line, Tumor - metabolism</topic><topic>Endoplasmic reticulum stress</topic><topic>Endoplasmic Reticulum Stress - drug effects</topic><topic>Endoplasmic Reticulum Stress - genetics</topic><topic>Endoplasmic Reticulum Stress - physiology</topic><topic>Genes, Synthetic</topic><topic>Glial cell</topic><topic>Glioma - pathology</topic><topic>Glutamate</topic><topic>Glutamic Acid - toxicity</topic><topic>GRP78</topic><topic>Heat-Shock Proteins - biosynthesis</topic><topic>Heat-Shock Proteins - genetics</topic><topic>Heat-Shock Proteins - physiology</topic><topic>Nerve Tissue Proteins - biosynthesis</topic><topic>Nerve Tissue Proteins - genetics</topic><topic>Nerve Tissue Proteins - physiology</topic><topic>Neurotoxins - toxicity</topic><topic>Rats</topic><topic>Recombinant Fusion Proteins - biosynthesis</topic><topic>Recombinant Fusion Proteins - genetics</topic><topic>Tunicamycin</topic><topic>Tunicamycin - toxicity</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Suyama, Kaori</creatorcontrib><creatorcontrib>Watanabe, Masahiko</creatorcontrib><creatorcontrib>Sakabe, Kou</creatorcontrib><creatorcontrib>Okada, Yoshinori</creatorcontrib><creatorcontrib>Matsuyama, Daisuke</creatorcontrib><creatorcontrib>Kuroiwa, Masahiro</creatorcontrib><creatorcontrib>Mochida, Joji</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Neurosciences Abstracts</collection><jtitle>Neuroscience letters</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Suyama, Kaori</au><au>Watanabe, Masahiko</au><au>Sakabe, Kou</au><au>Okada, Yoshinori</au><au>Matsuyama, Daisuke</au><au>Kuroiwa, Masahiro</au><au>Mochida, Joji</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Overexpression of GRP78 protects glial cells from endoplasmic reticulum stress</atitle><jtitle>Neuroscience letters</jtitle><addtitle>Neurosci Lett</addtitle><date>2011-10-31</date><risdate>2011</risdate><volume>504</volume><issue>3</issue><spage>271</spage><epage>276</epage><pages>271-276</pages><issn>0304-3940</issn><eissn>1872-7972</eissn><abstract>► GRP78 overexpression prior to injury protects C6 glioma cells from ER stress. ► GRP78 expression increases following exposure to high concentrations of glutamate. ► Transient expression of GRP78 protects against tunicamycin and glutamate injury.
Endoplasmic reticulum (ER) stress induces apoptotic cell death by causing the accumulation of structurally abnormal proteins. The 78-kDa glucose-regulated protein (GRP78) is an ER chaperone that regulates protein folding in the ER and has been suggested to contribute to cell survival. Using the rat C6 glioma cell line and flow cytometry, we assessed GRP78 expression following tunicamycin- and glutamate-induced ER stress. The results showed that GRP78 expression is upregulated following ER stress and has protective effects on injured glial cells. Annexin V and propidium iodide labeling revealed cells transiently expressing GRP78 prior to injury were protected against high-concentrations of tunicamycin and glutamate within 72
h. Our findings support the hypothesis that GRP78 inhibits cell death associated with ER stress.</abstract><cop>Ireland</cop><pub>Elsevier Ireland Ltd</pub><pmid>21970967</pmid><doi>10.1016/j.neulet.2011.09.045</doi><tpages>6</tpages></addata></record> |
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| subjects | Animals Apoptosis Apoptosis - drug effects Apoptosis - physiology Cell Line, Tumor - drug effects Cell Line, Tumor - metabolism Endoplasmic reticulum stress Endoplasmic Reticulum Stress - drug effects Endoplasmic Reticulum Stress - genetics Endoplasmic Reticulum Stress - physiology Genes, Synthetic Glial cell Glioma - pathology Glutamate Glutamic Acid - toxicity GRP78 Heat-Shock Proteins - biosynthesis Heat-Shock Proteins - genetics Heat-Shock Proteins - physiology Nerve Tissue Proteins - biosynthesis Nerve Tissue Proteins - genetics Nerve Tissue Proteins - physiology Neurotoxins - toxicity Rats Recombinant Fusion Proteins - biosynthesis Recombinant Fusion Proteins - genetics Tunicamycin Tunicamycin - toxicity |
| title | Overexpression of GRP78 protects glial cells from endoplasmic reticulum stress |
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