p47phox-Dependent Reactive Oxygen Species Stimulate Nuclear Translocation of the FoxO1 Transcription Factor During Metabolic Inhibition in Cardiomyoblasts
Reactive oxygen species (ROS) control forkhead box O (FOXO) transcription factor activity by influencing their nuclear translocation. However, knowledge of the ROS cellular source(s) involved herein remains scarce. Recently, we have shown p47 phox -dependent activation of ROS-producing NADPH oxidase...
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| Veröffentlicht in: | Cell biochemistry and biophysics 2018-09, Vol.76 (3), p.401-410 |
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| creator | ter Horst, Ellis N. Hahn, Nynke E. Geerts, Dirk Musters, René J. P. Paulus, Walter J. van Rossum, Albert C. Meischl, Christof Piek, Jan J. Niessen, Hans W. M. Krijnen, Paul A. J. |
| description | Reactive oxygen species (ROS) control forkhead box O (FOXO) transcription factor activity by influencing their nuclear translocation. However, knowledge of the ROS cellular source(s) involved herein remains scarce. Recently, we have shown p47
phox
-dependent activation of ROS-producing NADPH oxidase (NOX) at the nuclear pore in H9c2 rat cardiomyoblasts in response to ischemia. This localizes NOX perfectly to affect protein nuclear translocation, including that of transcription factors. In the current study, involvement of p47
phox
-dependent production of ROS in the nuclear translocation of FOXO1 was analyzed in H9c2 cells following 4 h of metabolic inhibition (MI), which mimics the effects of ischemia. Nuclear translocation of FOXO1 was determined by quantitative digital-imaging fluorescence and western blot analysis. Subsequently, the effect of inhibiting p47
phox
-dependent ROS production by short hairpin RNA (shRNA) transfection on FOXO1 translocation was analyzed by digital-imaging microscopy. MI induced a significant translocation of FOXO1 into the nucleus. Transfection with p47
phox
-shRNA successfully knocked-down p47
phox
expression, reduced nuclear nitrotyrosine production, an indirect marker for ROS production, and inhibited the nuclear translocation of FOXO1 following MI. With these results, we show for the first time that nuclear import of FOXO1 induced by MI in H9c2 depends critically on p47
phox
-mediated ROS production. |
| doi_str_mv | 10.1007/s12013-018-0847-4 |
| format | Article |
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phox
-dependent activation of ROS-producing NADPH oxidase (NOX) at the nuclear pore in H9c2 rat cardiomyoblasts in response to ischemia. This localizes NOX perfectly to affect protein nuclear translocation, including that of transcription factors. In the current study, involvement of p47
phox
-dependent production of ROS in the nuclear translocation of FOXO1 was analyzed in H9c2 cells following 4 h of metabolic inhibition (MI), which mimics the effects of ischemia. Nuclear translocation of FOXO1 was determined by quantitative digital-imaging fluorescence and western blot analysis. Subsequently, the effect of inhibiting p47
phox
-dependent ROS production by short hairpin RNA (shRNA) transfection on FOXO1 translocation was analyzed by digital-imaging microscopy. MI induced a significant translocation of FOXO1 into the nucleus. Transfection with p47
phox
-shRNA successfully knocked-down p47
phox
expression, reduced nuclear nitrotyrosine production, an indirect marker for ROS production, and inhibited the nuclear translocation of FOXO1 following MI. With these results, we show for the first time that nuclear import of FOXO1 induced by MI in H9c2 depends critically on p47
phox
-mediated ROS production.</description><identifier>ISSN: 1085-9195</identifier><identifier>EISSN: 1559-0283</identifier><identifier>DOI: 10.1007/s12013-018-0847-4</identifier><identifier>PMID: 29956081</identifier><language>eng</language><publisher>New York: Springer US</publisher><subject>Biochemistry ; Biological and Medical Physics ; Biomedical and Life Sciences ; Biophysics ; Biotechnology ; Cell Biology ; Digital imaging ; Fluorescence ; Forkhead protein ; FOXO1 protein ; Ischemia ; Life Sciences ; Metabolism ; NAD(P)H oxidase ; Nitrotyrosine ; Nuclear transport ; Original Paper ; Pharmacology/Toxicology ; Protein transport ; Proteins ; Reactive oxygen species ; Ribonucleic acid ; RNA ; Small intestine ; Transcription factors ; Transfection ; Translocation</subject><ispartof>Cell biochemistry and biophysics, 2018-09, Vol.76 (3), p.401-410</ispartof><rights>The Author(s) 2018</rights><rights>Cell Biochemistry and Biophysics is a copyright of Springer, (2018). All Rights Reserved. © 2018. This work is published under http://creativecommons.org/licenses/by/4.0/ (the “License”). Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License.</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c470t-7639bd6f72a30696e3b80b5346034331a54d448214f04e28c62cf60fa3a2cb6b3</citedby><cites>FETCH-LOGICAL-c470t-7639bd6f72a30696e3b80b5346034331a54d448214f04e28c62cf60fa3a2cb6b3</cites><orcidid>0000-0002-3721-565X</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://link.springer.com/content/pdf/10.1007/s12013-018-0847-4$$EPDF$$P50$$Gspringer$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://link.springer.com/10.1007/s12013-018-0847-4$$EHTML$$P50$$Gspringer$$Hfree_for_read</linktohtml><link.rule.ids>230,314,776,780,881,27903,27904,41467,42536,51298</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/29956081$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>ter Horst, Ellis N.</creatorcontrib><creatorcontrib>Hahn, Nynke E.</creatorcontrib><creatorcontrib>Geerts, Dirk</creatorcontrib><creatorcontrib>Musters, René J. P.</creatorcontrib><creatorcontrib>Paulus, Walter J.</creatorcontrib><creatorcontrib>van Rossum, Albert C.</creatorcontrib><creatorcontrib>Meischl, Christof</creatorcontrib><creatorcontrib>Piek, Jan J.</creatorcontrib><creatorcontrib>Niessen, Hans W. M.</creatorcontrib><creatorcontrib>Krijnen, Paul A. J.</creatorcontrib><title>p47phox-Dependent Reactive Oxygen Species Stimulate Nuclear Translocation of the FoxO1 Transcription Factor During Metabolic Inhibition in Cardiomyoblasts</title><title>Cell biochemistry and biophysics</title><addtitle>Cell Biochem Biophys</addtitle><addtitle>Cell Biochem Biophys</addtitle><description>Reactive oxygen species (ROS) control forkhead box O (FOXO) transcription factor activity by influencing their nuclear translocation. However, knowledge of the ROS cellular source(s) involved herein remains scarce. Recently, we have shown p47
phox
-dependent activation of ROS-producing NADPH oxidase (NOX) at the nuclear pore in H9c2 rat cardiomyoblasts in response to ischemia. This localizes NOX perfectly to affect protein nuclear translocation, including that of transcription factors. In the current study, involvement of p47
phox
-dependent production of ROS in the nuclear translocation of FOXO1 was analyzed in H9c2 cells following 4 h of metabolic inhibition (MI), which mimics the effects of ischemia. Nuclear translocation of FOXO1 was determined by quantitative digital-imaging fluorescence and western blot analysis. Subsequently, the effect of inhibiting p47
phox
-dependent ROS production by short hairpin RNA (shRNA) transfection on FOXO1 translocation was analyzed by digital-imaging microscopy. MI induced a significant translocation of FOXO1 into the nucleus. Transfection with p47
phox
-shRNA successfully knocked-down p47
phox
expression, reduced nuclear nitrotyrosine production, an indirect marker for ROS production, and inhibited the nuclear translocation of FOXO1 following MI. With these results, we show for the first time that nuclear import of FOXO1 induced by MI in H9c2 depends critically on p47
phox
-mediated ROS production.</description><subject>Biochemistry</subject><subject>Biological and Medical Physics</subject><subject>Biomedical and Life Sciences</subject><subject>Biophysics</subject><subject>Biotechnology</subject><subject>Cell Biology</subject><subject>Digital imaging</subject><subject>Fluorescence</subject><subject>Forkhead protein</subject><subject>FOXO1 protein</subject><subject>Ischemia</subject><subject>Life Sciences</subject><subject>Metabolism</subject><subject>NAD(P)H oxidase</subject><subject>Nitrotyrosine</subject><subject>Nuclear transport</subject><subject>Original Paper</subject><subject>Pharmacology/Toxicology</subject><subject>Protein transport</subject><subject>Proteins</subject><subject>Reactive oxygen species</subject><subject>Ribonucleic acid</subject><subject>RNA</subject><subject>Small intestine</subject><subject>Transcription factors</subject><subject>Transfection</subject><subject>Translocation</subject><issn>1085-9195</issn><issn>1559-0283</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2018</creationdate><recordtype>article</recordtype><sourceid>C6C</sourceid><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>AZQEC</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><sourceid>GNUQQ</sourceid><recordid>eNp1kU1v1DAQhiMEoqXwA7ggS1x6CYw_4iQXJLRl20qFlWg5W44z2XWV2MFOqt2_wq8laUr5kDjZ0jzzesZPkrym8I4C5O8jZUB5CrRIoRB5Kp4kxzTLyhRYwZ9OdyiytKRldpS8iPEWgDEQ4nlyxMoyk1DQ4-RHL_J-5_fpGfboanQD-YraDPYOyWZ_2KIj1z0ai5FcD7YbWz0g-TKaFnUgN0G72HqjB-sd8Q0ZdkjWfr-hS8kE29-X1lOiD-RsDNZtyWccdOVba8il29nK3iPWkZUOtfXdwVetjkN8mTxrdBvx1cN5knxbf7pZXaRXm_PL1cer1IgchjSXvKxq2eRMc5ClRF4VUGVcSOCCc6ozUQtRMCoaEMgKI5lpJDSaa2YqWfGT5MOS249Vh7WZ_iDoVvXBdjoclNdW_V1xdqe2_k5JKHPIYAo4fQgI_vuIcVCdjQbbVjv0Y1QMJCtYPomZ0Lf_oLd-DG5ab6YoY5mQYqLoQpngYwzYPA5DQc3m1WJeTebVbF7NPW_-3OKx45fqCWALEPvZAobfT_8_9ScYL7ut</recordid><startdate>20180901</startdate><enddate>20180901</enddate><creator>ter Horst, Ellis N.</creator><creator>Hahn, Nynke E.</creator><creator>Geerts, Dirk</creator><creator>Musters, René J. 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P.</au><au>Paulus, Walter J.</au><au>van Rossum, Albert C.</au><au>Meischl, Christof</au><au>Piek, Jan J.</au><au>Niessen, Hans W. M.</au><au>Krijnen, Paul A. J.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>p47phox-Dependent Reactive Oxygen Species Stimulate Nuclear Translocation of the FoxO1 Transcription Factor During Metabolic Inhibition in Cardiomyoblasts</atitle><jtitle>Cell biochemistry and biophysics</jtitle><stitle>Cell Biochem Biophys</stitle><addtitle>Cell Biochem Biophys</addtitle><date>2018-09-01</date><risdate>2018</risdate><volume>76</volume><issue>3</issue><spage>401</spage><epage>410</epage><pages>401-410</pages><issn>1085-9195</issn><eissn>1559-0283</eissn><abstract>Reactive oxygen species (ROS) control forkhead box O (FOXO) transcription factor activity by influencing their nuclear translocation. However, knowledge of the ROS cellular source(s) involved herein remains scarce. Recently, we have shown p47
phox
-dependent activation of ROS-producing NADPH oxidase (NOX) at the nuclear pore in H9c2 rat cardiomyoblasts in response to ischemia. This localizes NOX perfectly to affect protein nuclear translocation, including that of transcription factors. In the current study, involvement of p47
phox
-dependent production of ROS in the nuclear translocation of FOXO1 was analyzed in H9c2 cells following 4 h of metabolic inhibition (MI), which mimics the effects of ischemia. Nuclear translocation of FOXO1 was determined by quantitative digital-imaging fluorescence and western blot analysis. Subsequently, the effect of inhibiting p47
phox
-dependent ROS production by short hairpin RNA (shRNA) transfection on FOXO1 translocation was analyzed by digital-imaging microscopy. MI induced a significant translocation of FOXO1 into the nucleus. Transfection with p47
phox
-shRNA successfully knocked-down p47
phox
expression, reduced nuclear nitrotyrosine production, an indirect marker for ROS production, and inhibited the nuclear translocation of FOXO1 following MI. With these results, we show for the first time that nuclear import of FOXO1 induced by MI in H9c2 depends critically on p47
phox
-mediated ROS production.</abstract><cop>New York</cop><pub>Springer US</pub><pmid>29956081</pmid><doi>10.1007/s12013-018-0847-4</doi><tpages>10</tpages><orcidid>https://orcid.org/0000-0002-3721-565X</orcidid><oa>free_for_read</oa></addata></record> |
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| ispartof | Cell biochemistry and biophysics, 2018-09, Vol.76 (3), p.401-410 |
| issn | 1085-9195 1559-0283 |
| language | eng |
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| source | SpringerLink Journals (MCLS) |
| subjects | Biochemistry Biological and Medical Physics Biomedical and Life Sciences Biophysics Biotechnology Cell Biology Digital imaging Fluorescence Forkhead protein FOXO1 protein Ischemia Life Sciences Metabolism NAD(P)H oxidase Nitrotyrosine Nuclear transport Original Paper Pharmacology/Toxicology Protein transport Proteins Reactive oxygen species Ribonucleic acid RNA Small intestine Transcription factors Transfection Translocation |
| title | p47phox-Dependent Reactive Oxygen Species Stimulate Nuclear Translocation of the FoxO1 Transcription Factor During Metabolic Inhibition in Cardiomyoblasts |
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