Caspase 3 Activation Is Essential for Neuroprotection in Preconditioning
Sublethal insults can induce tolerance to subsequent stressors in neurons. As cell death activators such as ROS generation and decreased ATP can initiate tolerance, we tested whether other cellular elements normally associated with neuronal injury could add to this process. In an in vivo model of is...
Gespeichert in:
| Veröffentlicht in: | Proceedings of the National Academy of Sciences - PNAS 2003-01, Vol.100 (2), p.715-720 |
|---|---|
| Hauptverfasser: | , , , , , , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 720 |
|---|---|
| container_issue | 2 |
| container_start_page | 715 |
| container_title | Proceedings of the National Academy of Sciences - PNAS |
| container_volume | 100 |
| creator | McLaughlin, BethAnn Hartnett, Karen A. Erhardt, Joseph A. Legos, Jeffrey J. White, Ray F. Barone, Frank C. Aizenman, Elias |
| description | Sublethal insults can induce tolerance to subsequent stressors in neurons. As cell death activators such as ROS generation and decreased ATP can initiate tolerance, we tested whether other cellular elements normally associated with neuronal injury could add to this process. In an in vivo model of ischemic tolerance, we were surprised to observe widespread caspase 3 cleavage, without cell death, in preconditioned tissue. To dissect the preconditioning pathways activating caspases, and the mechanisms by which these proteases are held in check, we developed an in vitro model of excitotoxic tolerance. In this model, antioxidants and caspase inhibitors blocked ischemia-induced protection against N-methyl-D-aspartate toxicity. Moreover, agents that blocked preconditioning also attenuated induction of HSP 70; transient overexpression of a constitutive form of this protein prevented HSP 70 up-regulation and blocked tolerance. We outline a neuroprotective pathway where events normally associated with apoptotic cell death are critical for cell survival. |
| doi_str_mv | 10.1073/pnas.0232966100 |
| format | Article |
| fullrecord | <record><control><sourceid>jstor_proqu</sourceid><recordid>TN_cdi_proquest_journals_201340912</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><jstor_id>3138209</jstor_id><sourcerecordid>3138209</sourcerecordid><originalsourceid>FETCH-LOGICAL-c586t-174d4df2e96a214210fbce19de7b3dfa83bfca360db727f9ab12b574044ef4ba3</originalsourceid><addsrcrecordid>eNptkUFv1DAQhS0EokvLmQugiAO3tDO2YycHDtWq0EoVcChny0ns4lXWDrZT0X_fhF11C-JkWfO9pzfzCHmDcIog2dnodToFymgjBAI8IyuEBkvBG3hOVgBUljWn_Ii8SmkDAE1Vw0tyhLSilApYkcu1TqNOpmDFeZfdnc4u-OIqFRcpGZ-dHgobYvHVTDGMMWTT_QGcL75H0wXfu-Xv_O0JeWH1kMzr_XtMfny-uFlfltffvlytz6_LrqpFLlHynveWmkZoipwi2LYz2PRGtqy3umat7TQT0LeSStvoFmlbSQ6cG8tbzY7Jp53vOLVb03dzyKgHNUa31fFeBe3U3xPvfqrbcKeQIwg66z_u9TH8mkzKautSZ4ZBexOmpLAWHCQXM_jhH3ATpujn3RQFZHy-8-J2toO6GFKKxj4GQVBLQ2ppSB0amhXvn-Y_8PtKZuDdHliUBztQVEmsnizw37my0zBk8zvP4NsduEk5xEeSIaspNOwB6Iuuag</addsrcrecordid><sourcetype>Open Access Repository</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>201340912</pqid></control><display><type>article</type><title>Caspase 3 Activation Is Essential for Neuroprotection in Preconditioning</title><source>Jstor Complete Legacy</source><source>MEDLINE</source><source>PubMed Central</source><source>Alma/SFX Local Collection</source><source>Free Full-Text Journals in Chemistry</source><creator>McLaughlin, BethAnn ; Hartnett, Karen A. ; Erhardt, Joseph A. ; Legos, Jeffrey J. ; White, Ray F. ; Barone, Frank C. ; Aizenman, Elias</creator><creatorcontrib>McLaughlin, BethAnn ; Hartnett, Karen A. ; Erhardt, Joseph A. ; Legos, Jeffrey J. ; White, Ray F. ; Barone, Frank C. ; Aizenman, Elias</creatorcontrib><description>Sublethal insults can induce tolerance to subsequent stressors in neurons. As cell death activators such as ROS generation and decreased ATP can initiate tolerance, we tested whether other cellular elements normally associated with neuronal injury could add to this process. In an in vivo model of ischemic tolerance, we were surprised to observe widespread caspase 3 cleavage, without cell death, in preconditioned tissue. To dissect the preconditioning pathways activating caspases, and the mechanisms by which these proteases are held in check, we developed an in vitro model of excitotoxic tolerance. In this model, antioxidants and caspase inhibitors blocked ischemia-induced protection against N-methyl-D-aspartate toxicity. Moreover, agents that blocked preconditioning also attenuated induction of HSP 70; transient overexpression of a constitutive form of this protein prevented HSP 70 up-regulation and blocked tolerance. We outline a neuroprotective pathway where events normally associated with apoptotic cell death are critical for cell survival.</description><identifier>ISSN: 0027-8424</identifier><identifier>EISSN: 1091-6490</identifier><identifier>DOI: 10.1073/pnas.0232966100</identifier><identifier>PMID: 12522260</identifier><language>eng</language><publisher>United States: National Academy of Sciences</publisher><subject>Animals ; bcl-X Protein ; Biological Sciences ; Caspase 3 ; Caspases - physiology ; Cell death ; Cells, Cultured ; Enzyme Activation ; HSP70 Heat-Shock Proteins - biosynthesis ; Inductive reasoning ; Insults ; Ischemic Preconditioning ; Medical research ; N-Methylaspartate - pharmacology ; Neurology ; Neurons ; Neurons - pathology ; Neuroscience ; Potassium Channels - physiology ; Preconditioning ; Protein synthesis ; Proto-Oncogene Proteins c-bcl-2 - biosynthesis ; Rats ; Reactive Oxygen Species ; Time Factors ; Up regulation</subject><ispartof>Proceedings of the National Academy of Sciences - PNAS, 2003-01, Vol.100 (2), p.715-720</ispartof><rights>Copyright 1993-2003 National Academy of Sciences of the United States of America</rights><rights>Copyright National Academy of Sciences Jan 21, 2003</rights><rights>Copyright © 2003, The National Academy of Sciences 2003</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c586t-174d4df2e96a214210fbce19de7b3dfa83bfca360db727f9ab12b574044ef4ba3</citedby><cites>FETCH-LOGICAL-c586t-174d4df2e96a214210fbce19de7b3dfa83bfca360db727f9ab12b574044ef4ba3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Uhttp://www.pnas.org/content/100/2.cover.gif</thumbnail><linktopdf>$$Uhttps://www.jstor.org/stable/pdf/3138209$$EPDF$$P50$$Gjstor$$H</linktopdf><linktohtml>$$Uhttps://www.jstor.org/stable/3138209$$EHTML$$P50$$Gjstor$$H</linktohtml><link.rule.ids>230,314,723,776,780,799,881,27901,27902,53766,53768,57992,58225</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/12522260$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>McLaughlin, BethAnn</creatorcontrib><creatorcontrib>Hartnett, Karen A.</creatorcontrib><creatorcontrib>Erhardt, Joseph A.</creatorcontrib><creatorcontrib>Legos, Jeffrey J.</creatorcontrib><creatorcontrib>White, Ray F.</creatorcontrib><creatorcontrib>Barone, Frank C.</creatorcontrib><creatorcontrib>Aizenman, Elias</creatorcontrib><title>Caspase 3 Activation Is Essential for Neuroprotection in Preconditioning</title><title>Proceedings of the National Academy of Sciences - PNAS</title><addtitle>Proc Natl Acad Sci U S A</addtitle><description>Sublethal insults can induce tolerance to subsequent stressors in neurons. As cell death activators such as ROS generation and decreased ATP can initiate tolerance, we tested whether other cellular elements normally associated with neuronal injury could add to this process. In an in vivo model of ischemic tolerance, we were surprised to observe widespread caspase 3 cleavage, without cell death, in preconditioned tissue. To dissect the preconditioning pathways activating caspases, and the mechanisms by which these proteases are held in check, we developed an in vitro model of excitotoxic tolerance. In this model, antioxidants and caspase inhibitors blocked ischemia-induced protection against N-methyl-D-aspartate toxicity. Moreover, agents that blocked preconditioning also attenuated induction of HSP 70; transient overexpression of a constitutive form of this protein prevented HSP 70 up-regulation and blocked tolerance. We outline a neuroprotective pathway where events normally associated with apoptotic cell death are critical for cell survival.</description><subject>Animals</subject><subject>bcl-X Protein</subject><subject>Biological Sciences</subject><subject>Caspase 3</subject><subject>Caspases - physiology</subject><subject>Cell death</subject><subject>Cells, Cultured</subject><subject>Enzyme Activation</subject><subject>HSP70 Heat-Shock Proteins - biosynthesis</subject><subject>Inductive reasoning</subject><subject>Insults</subject><subject>Ischemic Preconditioning</subject><subject>Medical research</subject><subject>N-Methylaspartate - pharmacology</subject><subject>Neurology</subject><subject>Neurons</subject><subject>Neurons - pathology</subject><subject>Neuroscience</subject><subject>Potassium Channels - physiology</subject><subject>Preconditioning</subject><subject>Protein synthesis</subject><subject>Proto-Oncogene Proteins c-bcl-2 - biosynthesis</subject><subject>Rats</subject><subject>Reactive Oxygen Species</subject><subject>Time Factors</subject><subject>Up regulation</subject><issn>0027-8424</issn><issn>1091-6490</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2003</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNptkUFv1DAQhS0EokvLmQugiAO3tDO2YycHDtWq0EoVcChny0ns4lXWDrZT0X_fhF11C-JkWfO9pzfzCHmDcIog2dnodToFymgjBAI8IyuEBkvBG3hOVgBUljWn_Ii8SmkDAE1Vw0tyhLSilApYkcu1TqNOpmDFeZfdnc4u-OIqFRcpGZ-dHgobYvHVTDGMMWTT_QGcL75H0wXfu-Xv_O0JeWH1kMzr_XtMfny-uFlfltffvlytz6_LrqpFLlHynveWmkZoipwi2LYz2PRGtqy3umat7TQT0LeSStvoFmlbSQ6cG8tbzY7Jp53vOLVb03dzyKgHNUa31fFeBe3U3xPvfqrbcKeQIwg66z_u9TH8mkzKautSZ4ZBexOmpLAWHCQXM_jhH3ATpujn3RQFZHy-8-J2toO6GFKKxj4GQVBLQ2ppSB0amhXvn-Y_8PtKZuDdHliUBztQVEmsnizw37my0zBk8zvP4NsduEk5xEeSIaspNOwB6Iuuag</recordid><startdate>20030121</startdate><enddate>20030121</enddate><creator>McLaughlin, BethAnn</creator><creator>Hartnett, Karen A.</creator><creator>Erhardt, Joseph A.</creator><creator>Legos, Jeffrey J.</creator><creator>White, Ray F.</creator><creator>Barone, Frank C.</creator><creator>Aizenman, Elias</creator><general>National Academy of Sciences</general><general>National Acad Sciences</general><general>The National Academy of Sciences</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>7QG</scope><scope>7QL</scope><scope>7QP</scope><scope>7QR</scope><scope>7SN</scope><scope>7SS</scope><scope>7T5</scope><scope>7TK</scope><scope>7TM</scope><scope>7TO</scope><scope>7U9</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>H94</scope><scope>M7N</scope><scope>P64</scope><scope>RC3</scope><scope>5PM</scope></search><sort><creationdate>20030121</creationdate><title>Caspase 3 Activation Is Essential for Neuroprotection in Preconditioning</title><author>McLaughlin, BethAnn ; Hartnett, Karen A. ; Erhardt, Joseph A. ; Legos, Jeffrey J. ; White, Ray F. ; Barone, Frank C. ; Aizenman, Elias</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c586t-174d4df2e96a214210fbce19de7b3dfa83bfca360db727f9ab12b574044ef4ba3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2003</creationdate><topic>Animals</topic><topic>bcl-X Protein</topic><topic>Biological Sciences</topic><topic>Caspase 3</topic><topic>Caspases - physiology</topic><topic>Cell death</topic><topic>Cells, Cultured</topic><topic>Enzyme Activation</topic><topic>HSP70 Heat-Shock Proteins - biosynthesis</topic><topic>Inductive reasoning</topic><topic>Insults</topic><topic>Ischemic Preconditioning</topic><topic>Medical research</topic><topic>N-Methylaspartate - pharmacology</topic><topic>Neurology</topic><topic>Neurons</topic><topic>Neurons - pathology</topic><topic>Neuroscience</topic><topic>Potassium Channels - physiology</topic><topic>Preconditioning</topic><topic>Protein synthesis</topic><topic>Proto-Oncogene Proteins c-bcl-2 - biosynthesis</topic><topic>Rats</topic><topic>Reactive Oxygen Species</topic><topic>Time Factors</topic><topic>Up regulation</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>McLaughlin, BethAnn</creatorcontrib><creatorcontrib>Hartnett, Karen A.</creatorcontrib><creatorcontrib>Erhardt, Joseph A.</creatorcontrib><creatorcontrib>Legos, Jeffrey J.</creatorcontrib><creatorcontrib>White, Ray F.</creatorcontrib><creatorcontrib>Barone, Frank C.</creatorcontrib><creatorcontrib>Aizenman, Elias</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Animal Behavior Abstracts</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Calcium & Calcified Tissue Abstracts</collection><collection>Chemoreception Abstracts</collection><collection>Ecology Abstracts</collection><collection>Entomology Abstracts (Full archive)</collection><collection>Immunology Abstracts</collection><collection>Neurosciences Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Oncogenes and Growth Factors Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Proceedings of the National Academy of Sciences - PNAS</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>McLaughlin, BethAnn</au><au>Hartnett, Karen A.</au><au>Erhardt, Joseph A.</au><au>Legos, Jeffrey J.</au><au>White, Ray F.</au><au>Barone, Frank C.</au><au>Aizenman, Elias</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Caspase 3 Activation Is Essential for Neuroprotection in Preconditioning</atitle><jtitle>Proceedings of the National Academy of Sciences - PNAS</jtitle><addtitle>Proc Natl Acad Sci U S A</addtitle><date>2003-01-21</date><risdate>2003</risdate><volume>100</volume><issue>2</issue><spage>715</spage><epage>720</epage><pages>715-720</pages><issn>0027-8424</issn><eissn>1091-6490</eissn><abstract>Sublethal insults can induce tolerance to subsequent stressors in neurons. As cell death activators such as ROS generation and decreased ATP can initiate tolerance, we tested whether other cellular elements normally associated with neuronal injury could add to this process. In an in vivo model of ischemic tolerance, we were surprised to observe widespread caspase 3 cleavage, without cell death, in preconditioned tissue. To dissect the preconditioning pathways activating caspases, and the mechanisms by which these proteases are held in check, we developed an in vitro model of excitotoxic tolerance. In this model, antioxidants and caspase inhibitors blocked ischemia-induced protection against N-methyl-D-aspartate toxicity. Moreover, agents that blocked preconditioning also attenuated induction of HSP 70; transient overexpression of a constitutive form of this protein prevented HSP 70 up-regulation and blocked tolerance. We outline a neuroprotective pathway where events normally associated with apoptotic cell death are critical for cell survival.</abstract><cop>United States</cop><pub>National Academy of Sciences</pub><pmid>12522260</pmid><doi>10.1073/pnas.0232966100</doi><tpages>6</tpages><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0027-8424 |
| ispartof | Proceedings of the National Academy of Sciences - PNAS, 2003-01, Vol.100 (2), p.715-720 |
| issn | 0027-8424 1091-6490 |
| language | eng |
| recordid | cdi_proquest_journals_201340912 |
| source | Jstor Complete Legacy; MEDLINE; PubMed Central; Alma/SFX Local Collection; Free Full-Text Journals in Chemistry |
| subjects | Animals bcl-X Protein Biological Sciences Caspase 3 Caspases - physiology Cell death Cells, Cultured Enzyme Activation HSP70 Heat-Shock Proteins - biosynthesis Inductive reasoning Insults Ischemic Preconditioning Medical research N-Methylaspartate - pharmacology Neurology Neurons Neurons - pathology Neuroscience Potassium Channels - physiology Preconditioning Protein synthesis Proto-Oncogene Proteins c-bcl-2 - biosynthesis Rats Reactive Oxygen Species Time Factors Up regulation |
| title | Caspase 3 Activation Is Essential for Neuroprotection in Preconditioning |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-02-15T02%3A43%3A22IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-jstor_proqu&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Caspase%203%20Activation%20Is%20Essential%20for%20Neuroprotection%20in%20Preconditioning&rft.jtitle=Proceedings%20of%20the%20National%20Academy%20of%20Sciences%20-%20PNAS&rft.au=McLaughlin,%20BethAnn&rft.date=2003-01-21&rft.volume=100&rft.issue=2&rft.spage=715&rft.epage=720&rft.pages=715-720&rft.issn=0027-8424&rft.eissn=1091-6490&rft_id=info:doi/10.1073/pnas.0232966100&rft_dat=%3Cjstor_proqu%3E3138209%3C/jstor_proqu%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=201340912&rft_id=info:pmid/12522260&rft_jstor_id=3138209&rfr_iscdi=true |