Proapoptotic protein glyceraldehyde-3-phosphate dehydrogenase: a possible site of action of antiapoptotic drugs
Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) has long been recognized as a classical glycolytic protein and has been used as a “housekeeping” gene in studies of genetic expression and regulation. However, recent advances reveal that GAPDH displays diverse nonglycolytic functions depending on its...
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| Veröffentlicht in: | Progress in neuro-psychopharmacology & biological psychiatry 2003-04, Vol.27 (2), p.291-301 |
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| container_title | Progress in neuro-psychopharmacology & biological psychiatry |
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| creator | Ishitani, Ryoichi Tajima, Hisao Takata, Hiroyuki Tsuchiya, Katsumi Kuwae, Toyoyasu Yamada, Mitsunori Takahashi, Hitoshi Tatton, Nadine A. Katsube, Nobuo |
| description | Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) has long been recognized as a classical glycolytic protein and has been used as a “housekeeping” gene in studies of genetic expression and regulation. However, recent advances reveal that GAPDH displays diverse nonglycolytic functions depending on its subcellular localization. Among those functions, one of the most intriguing is likely to be the induction of apoptosis. Previous works by our group and others have demonstrated that the overexpression of GAPDH and its subsequent nuclear translocation appear to be implicated in the initiation of one or more apoptotic cascades and also in the etiology of some neurological diseases. This review addresses new data demonstrating that a protein, referred to as proapoptotic protein GAPDH, with a quite mundane function in healthy cells behaves very differently during cell suicide, and summarizes emphatically the importance of this protein as a putative molecular target in developing antiapoptotic therapeutic agents for the treatment of certain neurodegenerative disorders. |
| doi_str_mv | 10.1016/S0278-5846(03)00024-1 |
| format | Article |
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However, recent advances reveal that GAPDH displays diverse nonglycolytic functions depending on its subcellular localization. Among those functions, one of the most intriguing is likely to be the induction of apoptosis. Previous works by our group and others have demonstrated that the overexpression of GAPDH and its subsequent nuclear translocation appear to be implicated in the initiation of one or more apoptotic cascades and also in the etiology of some neurological diseases. This review addresses new data demonstrating that a protein, referred to as proapoptotic protein GAPDH, with a quite mundane function in healthy cells behaves very differently during cell suicide, and summarizes emphatically the importance of this protein as a putative molecular target in developing antiapoptotic therapeutic agents for the treatment of certain neurodegenerative disorders.</description><identifier>ISSN: 0278-5846</identifier><identifier>EISSN: 1878-4216</identifier><identifier>DOI: 10.1016/S0278-5846(03)00024-1</identifier><identifier>PMID: 12657368</identifier><identifier>CODEN: PNPPD7</identifier><language>eng</language><publisher>Amsterdam: Elsevier Inc</publisher><subject>Ageing, cell death ; Aggregate formation ; Amino Acid Sequence ; Animals ; Antiapoptotic drugs ; Apoptosis ; Apoptosis - drug effects ; Apoptosis - physiology ; Biological and medical sciences ; Cell Nucleus - metabolism ; Cell physiology ; DNA, Complementary - biosynthesis ; DNA, Complementary - genetics ; Functional domains ; Fundamental and applied biological sciences. Psychology ; Gene Expression Regulation, Enzymologic - genetics ; Gene Expression Regulation, Enzymologic - physiology ; Glyceraldehyde-3-phosphate dehydrogenase ; Glyceraldehyde-3-Phosphate Dehydrogenases - drug effects ; Glyceraldehyde-3-Phosphate Dehydrogenases - genetics ; Glyceraldehyde-3-Phosphate Dehydrogenases - physiology ; Humans ; Molecular and cellular biology ; Molecular Sequence Data ; Neurodegenerative disorders ; Nuclear translocation ; Pathogenesis ; Promoter region</subject><ispartof>Progress in neuro-psychopharmacology & biological psychiatry, 2003-04, Vol.27 (2), p.291-301</ispartof><rights>2003 Elsevier Science Inc.</rights><rights>2003 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c457t-1890eb6a370e1bf730c2ec224a1d6fc16c8c9fa2747b1e2c53163aca0a9cdc2d3</citedby><cites>FETCH-LOGICAL-c457t-1890eb6a370e1bf730c2ec224a1d6fc16c8c9fa2747b1e2c53163aca0a9cdc2d3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/S0278584603000241$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,776,780,3537,27901,27902,65534</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=14617167$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/12657368$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Ishitani, Ryoichi</creatorcontrib><creatorcontrib>Tajima, Hisao</creatorcontrib><creatorcontrib>Takata, Hiroyuki</creatorcontrib><creatorcontrib>Tsuchiya, Katsumi</creatorcontrib><creatorcontrib>Kuwae, Toyoyasu</creatorcontrib><creatorcontrib>Yamada, Mitsunori</creatorcontrib><creatorcontrib>Takahashi, Hitoshi</creatorcontrib><creatorcontrib>Tatton, Nadine A.</creatorcontrib><creatorcontrib>Katsube, Nobuo</creatorcontrib><title>Proapoptotic protein glyceraldehyde-3-phosphate dehydrogenase: a possible site of action of antiapoptotic drugs</title><title>Progress in neuro-psychopharmacology & biological psychiatry</title><addtitle>Prog Neuropsychopharmacol Biol Psychiatry</addtitle><description>Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) has long been recognized as a classical glycolytic protein and has been used as a “housekeeping” gene in studies of genetic expression and regulation. However, recent advances reveal that GAPDH displays diverse nonglycolytic functions depending on its subcellular localization. Among those functions, one of the most intriguing is likely to be the induction of apoptosis. Previous works by our group and others have demonstrated that the overexpression of GAPDH and its subsequent nuclear translocation appear to be implicated in the initiation of one or more apoptotic cascades and also in the etiology of some neurological diseases. This review addresses new data demonstrating that a protein, referred to as proapoptotic protein GAPDH, with a quite mundane function in healthy cells behaves very differently during cell suicide, and summarizes emphatically the importance of this protein as a putative molecular target in developing antiapoptotic therapeutic agents for the treatment of certain neurodegenerative disorders.</description><subject>Ageing, cell death</subject><subject>Aggregate formation</subject><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>Antiapoptotic drugs</subject><subject>Apoptosis</subject><subject>Apoptosis - drug effects</subject><subject>Apoptosis - physiology</subject><subject>Biological and medical sciences</subject><subject>Cell Nucleus - metabolism</subject><subject>Cell physiology</subject><subject>DNA, Complementary - biosynthesis</subject><subject>DNA, Complementary - genetics</subject><subject>Functional domains</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Gene Expression Regulation, Enzymologic - genetics</subject><subject>Gene Expression Regulation, Enzymologic - physiology</subject><subject>Glyceraldehyde-3-phosphate dehydrogenase</subject><subject>Glyceraldehyde-3-Phosphate Dehydrogenases - drug effects</subject><subject>Glyceraldehyde-3-Phosphate Dehydrogenases - genetics</subject><subject>Glyceraldehyde-3-Phosphate Dehydrogenases - physiology</subject><subject>Humans</subject><subject>Molecular and cellular biology</subject><subject>Molecular Sequence Data</subject><subject>Neurodegenerative disorders</subject><subject>Nuclear translocation</subject><subject>Pathogenesis</subject><subject>Promoter region</subject><issn>0278-5846</issn><issn>1878-4216</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2003</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkM-v0zAMgCME4o0HfwKoFxAcCnHSJh0XhJ74JT0JJOAcua67BXVNSTKk_ffkbRM7crLlfLbjT4inIF-DBPPmu1S2q9uuMS-lfiWlVE0N98QKulJuFJj7YvUPuRKPUvpVINBSPxRXoExrtelWInyLAZew5JA9VUsMmf1cbaYDccRp4O1h4FrXyzakZYuZq2Mphg3PmPhthdUSUvL9xFXy5TmMFVL2YT5mc_aX4UPcb9Jj8WDEKfGTc7wWPz9--HHzub79-unLzfvbmprW5hq6teTeoLaSoR-tlqSYlGoQBjMSGOpoPaKyje2BFbUajEZCiWsaSA36Wrw4zS0n_d5zym7nE_E04cxhn5zVoK1u2wK2J5BiOSTy6JbodxgPDqS7M-2Opt2dRie1O5p2UPqenRfs-x0Pl66z2gI8PwOYCKcx4kw-XbjGgAVjC_fuxHHR8cdzdIk8z8SDj0zZDcH_5yt_AeGYnTM</recordid><startdate>20030401</startdate><enddate>20030401</enddate><creator>Ishitani, Ryoichi</creator><creator>Tajima, Hisao</creator><creator>Takata, Hiroyuki</creator><creator>Tsuchiya, Katsumi</creator><creator>Kuwae, Toyoyasu</creator><creator>Yamada, Mitsunori</creator><creator>Takahashi, Hitoshi</creator><creator>Tatton, Nadine A.</creator><creator>Katsube, Nobuo</creator><general>Elsevier Inc</general><general>Elsevier</general><scope>IQODW</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>7X8</scope></search><sort><creationdate>20030401</creationdate><title>Proapoptotic protein glyceraldehyde-3-phosphate dehydrogenase: a possible site of action of antiapoptotic drugs</title><author>Ishitani, Ryoichi ; Tajima, Hisao ; Takata, Hiroyuki ; Tsuchiya, Katsumi ; Kuwae, Toyoyasu ; Yamada, Mitsunori ; Takahashi, Hitoshi ; Tatton, Nadine A. ; Katsube, Nobuo</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c457t-1890eb6a370e1bf730c2ec224a1d6fc16c8c9fa2747b1e2c53163aca0a9cdc2d3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2003</creationdate><topic>Ageing, cell death</topic><topic>Aggregate formation</topic><topic>Amino Acid Sequence</topic><topic>Animals</topic><topic>Antiapoptotic drugs</topic><topic>Apoptosis</topic><topic>Apoptosis - drug effects</topic><topic>Apoptosis - physiology</topic><topic>Biological and medical sciences</topic><topic>Cell Nucleus - metabolism</topic><topic>Cell physiology</topic><topic>DNA, Complementary - biosynthesis</topic><topic>DNA, Complementary - genetics</topic><topic>Functional domains</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Gene Expression Regulation, Enzymologic - genetics</topic><topic>Gene Expression Regulation, Enzymologic - physiology</topic><topic>Glyceraldehyde-3-phosphate dehydrogenase</topic><topic>Glyceraldehyde-3-Phosphate Dehydrogenases - drug effects</topic><topic>Glyceraldehyde-3-Phosphate Dehydrogenases - genetics</topic><topic>Glyceraldehyde-3-Phosphate Dehydrogenases - physiology</topic><topic>Humans</topic><topic>Molecular and cellular biology</topic><topic>Molecular Sequence Data</topic><topic>Neurodegenerative disorders</topic><topic>Nuclear translocation</topic><topic>Pathogenesis</topic><topic>Promoter region</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Ishitani, Ryoichi</creatorcontrib><creatorcontrib>Tajima, Hisao</creatorcontrib><creatorcontrib>Takata, Hiroyuki</creatorcontrib><creatorcontrib>Tsuchiya, Katsumi</creatorcontrib><creatorcontrib>Kuwae, Toyoyasu</creatorcontrib><creatorcontrib>Yamada, Mitsunori</creatorcontrib><creatorcontrib>Takahashi, Hitoshi</creatorcontrib><creatorcontrib>Tatton, Nadine A.</creatorcontrib><creatorcontrib>Katsube, Nobuo</creatorcontrib><collection>Pascal-Francis</collection><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>Progress in neuro-psychopharmacology & biological psychiatry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Ishitani, Ryoichi</au><au>Tajima, Hisao</au><au>Takata, Hiroyuki</au><au>Tsuchiya, Katsumi</au><au>Kuwae, Toyoyasu</au><au>Yamada, Mitsunori</au><au>Takahashi, Hitoshi</au><au>Tatton, Nadine A.</au><au>Katsube, Nobuo</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Proapoptotic protein glyceraldehyde-3-phosphate dehydrogenase: a possible site of action of antiapoptotic drugs</atitle><jtitle>Progress in neuro-psychopharmacology & biological psychiatry</jtitle><addtitle>Prog Neuropsychopharmacol Biol Psychiatry</addtitle><date>2003-04-01</date><risdate>2003</risdate><volume>27</volume><issue>2</issue><spage>291</spage><epage>301</epage><pages>291-301</pages><issn>0278-5846</issn><eissn>1878-4216</eissn><coden>PNPPD7</coden><abstract>Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) has long been recognized as a classical glycolytic protein and has been used as a “housekeeping” gene in studies of genetic expression and regulation. However, recent advances reveal that GAPDH displays diverse nonglycolytic functions depending on its subcellular localization. Among those functions, one of the most intriguing is likely to be the induction of apoptosis. Previous works by our group and others have demonstrated that the overexpression of GAPDH and its subsequent nuclear translocation appear to be implicated in the initiation of one or more apoptotic cascades and also in the etiology of some neurological diseases. 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| subjects | Ageing, cell death Aggregate formation Amino Acid Sequence Animals Antiapoptotic drugs Apoptosis Apoptosis - drug effects Apoptosis - physiology Biological and medical sciences Cell Nucleus - metabolism Cell physiology DNA, Complementary - biosynthesis DNA, Complementary - genetics Functional domains Fundamental and applied biological sciences. Psychology Gene Expression Regulation, Enzymologic - genetics Gene Expression Regulation, Enzymologic - physiology Glyceraldehyde-3-phosphate dehydrogenase Glyceraldehyde-3-Phosphate Dehydrogenases - drug effects Glyceraldehyde-3-Phosphate Dehydrogenases - genetics Glyceraldehyde-3-Phosphate Dehydrogenases - physiology Humans Molecular and cellular biology Molecular Sequence Data Neurodegenerative disorders Nuclear translocation Pathogenesis Promoter region |
| title | Proapoptotic protein glyceraldehyde-3-phosphate dehydrogenase: a possible site of action of antiapoptotic drugs |
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