Protection Against Protein Aggregation by Alpha-Crystallin as a Mechanism of Preconditioning
Anesthetic preconditioning occurs when cells previously exposed to inhaled anesthetics are protected against subsequent injury. We hypothesize that inhaled anesthetics may cause slight protein misfolding that involves site-specific dehydration, stimulating cytoprotective mechanisms. Human neuroblast...
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| Veröffentlicht in: | Neurochemical research 2012-02, Vol.37 (2), p.244-252 |
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| creator | Ferns, Jonathan E. Theisen, Christopher S. Fibuch, Eugene E. Seidler, Norbert W. |
| description | Anesthetic preconditioning occurs when cells previously exposed to inhaled anesthetics are protected against subsequent injury. We hypothesize that inhaled anesthetics may cause slight protein misfolding that involves site-specific dehydration, stimulating cytoprotective mechanisms. Human neuroblastoma cells were exposed to ethanol (as the dehydration agent) followed by quantitative analysis of the expression of five heat shock genes: DNAJC5G, CRYAA, HSPB2, HSF4 and HSF2. There was an ethanol-induced upregulation of all genes except HSF4, similar to previous observations using isoflurane. CRYAA (the gene for alphaA-crystallin) exhibited a 23.19 and 17.15-fold increase at 24 and 48 h post ethanol exposure, respectively. Additionally, we exposed glyceraldehyde 3-phosphate dehydrogenase to ethanol, which altered oligomeric subspecies and caused protein aggregation in a concentration-dependent manner. Ethanol-mediated dehydration-induced protein aggregation was prevented by incubation with alpha-crystallin. These data indicate that ethanol mimics the effects of isoflurane presumably through a cellular preconditioning mechanism that involves dehydration-induced protein aggregation. |
| doi_str_mv | 10.1007/s11064-011-0601-4 |
| format | Article |
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We hypothesize that inhaled anesthetics may cause slight protein misfolding that involves site-specific dehydration, stimulating cytoprotective mechanisms. Human neuroblastoma cells were exposed to ethanol (as the dehydration agent) followed by quantitative analysis of the expression of five heat shock genes: DNAJC5G, CRYAA, HSPB2, HSF4 and HSF2. There was an ethanol-induced upregulation of all genes except HSF4, similar to previous observations using isoflurane. CRYAA (the gene for alphaA-crystallin) exhibited a 23.19 and 17.15-fold increase at 24 and 48 h post ethanol exposure, respectively. Additionally, we exposed glyceraldehyde 3-phosphate dehydrogenase to ethanol, which altered oligomeric subspecies and caused protein aggregation in a concentration-dependent manner. Ethanol-mediated dehydration-induced protein aggregation was prevented by incubation with alpha-crystallin. These data indicate that ethanol mimics the effects of isoflurane presumably through a cellular preconditioning mechanism that involves dehydration-induced protein aggregation.</description><identifier>ISSN: 0364-3190</identifier><identifier>EISSN: 1573-6903</identifier><identifier>DOI: 10.1007/s11064-011-0601-4</identifier><identifier>PMID: 21984199</identifier><language>eng</language><publisher>Boston: Springer US</publisher><subject>alpha-Crystallins - physiology ; Anesthetics, Inhalation - adverse effects ; Base Sequence ; Biochemistry ; Biomedical and Life Sciences ; Biomedicine ; Cell Biology ; Cell Line, Tumor ; DNA Primers ; Electrophoresis, Polyacrylamide Gel ; Heat-Shock Proteins - metabolism ; Humans ; Neurochemistry ; Neurology ; Neurosciences ; Original Paper ; Real-Time Polymerase Chain Reaction</subject><ispartof>Neurochemical research, 2012-02, Vol.37 (2), p.244-252</ispartof><rights>Springer Science+Business Media, LLC 2011</rights><rights>Springer Science+Business Media, LLC 2012</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c402t-a94488b85b6ab3bee77f5cb768679aefb6ade4cc1751381d61029c433ad8e0c43</citedby><cites>FETCH-LOGICAL-c402t-a94488b85b6ab3bee77f5cb768679aefb6ade4cc1751381d61029c433ad8e0c43</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://link.springer.com/content/pdf/10.1007/s11064-011-0601-4$$EPDF$$P50$$Gspringer$$H</linktopdf><linktohtml>$$Uhttps://link.springer.com/10.1007/s11064-011-0601-4$$EHTML$$P50$$Gspringer$$H</linktohtml><link.rule.ids>314,780,784,27923,27924,41487,42556,51318</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/21984199$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Ferns, Jonathan E.</creatorcontrib><creatorcontrib>Theisen, Christopher S.</creatorcontrib><creatorcontrib>Fibuch, Eugene E.</creatorcontrib><creatorcontrib>Seidler, Norbert W.</creatorcontrib><title>Protection Against Protein Aggregation by Alpha-Crystallin as a Mechanism of Preconditioning</title><title>Neurochemical research</title><addtitle>Neurochem Res</addtitle><addtitle>Neurochem Res</addtitle><description>Anesthetic preconditioning occurs when cells previously exposed to inhaled anesthetics are protected against subsequent injury. We hypothesize that inhaled anesthetics may cause slight protein misfolding that involves site-specific dehydration, stimulating cytoprotective mechanisms. Human neuroblastoma cells were exposed to ethanol (as the dehydration agent) followed by quantitative analysis of the expression of five heat shock genes: DNAJC5G, CRYAA, HSPB2, HSF4 and HSF2. There was an ethanol-induced upregulation of all genes except HSF4, similar to previous observations using isoflurane. CRYAA (the gene for alphaA-crystallin) exhibited a 23.19 and 17.15-fold increase at 24 and 48 h post ethanol exposure, respectively. Additionally, we exposed glyceraldehyde 3-phosphate dehydrogenase to ethanol, which altered oligomeric subspecies and caused protein aggregation in a concentration-dependent manner. Ethanol-mediated dehydration-induced protein aggregation was prevented by incubation with alpha-crystallin. These data indicate that ethanol mimics the effects of isoflurane presumably through a cellular preconditioning mechanism that involves dehydration-induced protein aggregation.</description><subject>alpha-Crystallins - physiology</subject><subject>Anesthetics, Inhalation - adverse effects</subject><subject>Base Sequence</subject><subject>Biochemistry</subject><subject>Biomedical and Life Sciences</subject><subject>Biomedicine</subject><subject>Cell Biology</subject><subject>Cell Line, Tumor</subject><subject>DNA Primers</subject><subject>Electrophoresis, Polyacrylamide Gel</subject><subject>Heat-Shock Proteins - metabolism</subject><subject>Humans</subject><subject>Neurochemistry</subject><subject>Neurology</subject><subject>Neurosciences</subject><subject>Original Paper</subject><subject>Real-Time Polymerase Chain Reaction</subject><issn>0364-3190</issn><issn>1573-6903</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2012</creationdate><recordtype>article</recordtype><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>eNp1kEtLxDAUhYMoOj5-gBspblxV723SPJbD4AtGdKE7IaRpWiuddkw6i_n3pjM-QHCV5J7vnBsOIacIlwggrgIicJYCYgocMGU7ZIK5oClXQHfJBGhUKSo4IIchvANEV4b75CBDJRkqNSGvT74fnB2avkumtWm6MCSbUTO-a-9qs9GKdTJtl28mnfl1GEzbRt2ExCQPzr6ZrgmLpK-i09m-K5vR0nT1MdmrTBvcydd5RF5urp9nd-n88fZ-Np2nlkE2pEYxJmUh84KbghbOCVHlthBccqGMq-K4dMxaFDlSiSVHyJRllJpSOoiXI3KxzV36_mPlwqAXTbCubU3n-lXQKuNS5gxG8vwP-d6vfBc_pxUKyqTgECHcQtb3IXhX6aVvFsavNYIei9fb4nUsXo_F6zH47Ct4VSxc-eP4bjoC2RYIUepq5383_5_6CYkzjc0</recordid><startdate>20120201</startdate><enddate>20120201</enddate><creator>Ferns, Jonathan E.</creator><creator>Theisen, Christopher S.</creator><creator>Fibuch, Eugene E.</creator><creator>Seidler, Norbert W.</creator><general>Springer US</general><general>Springer Nature B.V</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>3V.</scope><scope>7QR</scope><scope>7TK</scope><scope>7U7</scope><scope>7X7</scope><scope>7XB</scope><scope>88A</scope><scope>88E</scope><scope>8AO</scope><scope>8FD</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>C1K</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FR3</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>M7P</scope><scope>P64</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PRINS</scope></search><sort><creationdate>20120201</creationdate><title>Protection Against Protein Aggregation by Alpha-Crystallin as a Mechanism of Preconditioning</title><author>Ferns, Jonathan E. ; 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We hypothesize that inhaled anesthetics may cause slight protein misfolding that involves site-specific dehydration, stimulating cytoprotective mechanisms. Human neuroblastoma cells were exposed to ethanol (as the dehydration agent) followed by quantitative analysis of the expression of five heat shock genes: DNAJC5G, CRYAA, HSPB2, HSF4 and HSF2. There was an ethanol-induced upregulation of all genes except HSF4, similar to previous observations using isoflurane. CRYAA (the gene for alphaA-crystallin) exhibited a 23.19 and 17.15-fold increase at 24 and 48 h post ethanol exposure, respectively. Additionally, we exposed glyceraldehyde 3-phosphate dehydrogenase to ethanol, which altered oligomeric subspecies and caused protein aggregation in a concentration-dependent manner. Ethanol-mediated dehydration-induced protein aggregation was prevented by incubation with alpha-crystallin. These data indicate that ethanol mimics the effects of isoflurane presumably through a cellular preconditioning mechanism that involves dehydration-induced protein aggregation.</abstract><cop>Boston</cop><pub>Springer US</pub><pmid>21984199</pmid><doi>10.1007/s11064-011-0601-4</doi><tpages>9</tpages></addata></record> |
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| subjects | alpha-Crystallins - physiology Anesthetics, Inhalation - adverse effects Base Sequence Biochemistry Biomedical and Life Sciences Biomedicine Cell Biology Cell Line, Tumor DNA Primers Electrophoresis, Polyacrylamide Gel Heat-Shock Proteins - metabolism Humans Neurochemistry Neurology Neurosciences Original Paper Real-Time Polymerase Chain Reaction |
| title | Protection Against Protein Aggregation by Alpha-Crystallin as a Mechanism of Preconditioning |
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