Heat shock protein 70 inhibits hydrogen peroxide-induced nucleolar fragmentation via suppressing cleavage and down-regulation of nucleolin
It has been reported that nucleolar fragmentation is a part of the overall apoptotic morphology, however, it is currently obscure whether and how nucleolar fragmentation can be induced by hydrogen peroxide (H₂O₂) and heat shock protein 70 (Hsp70) can prevent nucleolar fragmentation. To dissect these...
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| Veröffentlicht in: | Cell stress & chaperones 2012-01, Vol.17 (1), p.121-130 |
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| creator | Wang, Kangkai Deng, Gonghua Chen, Guangwen Liu, Meidong Yi, Yuxin Yang, Tubao McMillan, Daniel R. Xiao, Xiangzhong |
| description | It has been reported that nucleolar fragmentation is a part of the overall apoptotic morphology, however, it is currently obscure whether and how nucleolar fragmentation can be induced by hydrogen peroxide (H₂O₂) and heat shock protein 70 (Hsp70) can prevent nucleolar fragmentation. To dissect these two questions, C₂C₁₂ myogenic cells and immortalized mouse embryonic fibroblasts (MEFs) with heat shock transcriptional factor 1 (HSF1) null mutation were treated with heat shock response (HS) (42.5 ± 0.5°C for 1 h and recovery at 37°C for 24 h) and then were insulted with 0.5 mmol/L H₂O₂. Morphological changes of nucleoli were observed under contrast microscope or electronic microscope. It was found that (1) stimulation with H₂O₂-induced nucleolar fragmentation by mediating cleavage and down-regulation of nucleolar protein, nucleolin in C₂C₁₂ myocytes and MEFs; (2) HS suppressed nucleolar fragmentation by inducing the expression of Hsp70 in an HSF1-dependent manner as indicated by assays of transfection with Hsp70 antisense oligonucleotides (AS-ONs) or recombinant plasmids of full-length Hsp70 cDNA; (3) protection of Hsp70 against nucleolar fragmentation was related to its accumulation in nucleolus mediated by nuclear localization sequence and its inhibition against cleavage and down-regulation of nucleolin. These results suggested that H₂O₂-induced nucleolar fragmentation and HS or Hsp70 inhibit H₂O₂-induced nucleolar fragmentation through the translocation of Hsp70 into nucleolar and its protection against impairment of nucleolin. |
| doi_str_mv | 10.1007/s12192-011-0292-4 |
| format | Article |
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To dissect these two questions, C₂C₁₂ myogenic cells and immortalized mouse embryonic fibroblasts (MEFs) with heat shock transcriptional factor 1 (HSF1) null mutation were treated with heat shock response (HS) (42.5 ± 0.5°C for 1 h and recovery at 37°C for 24 h) and then were insulted with 0.5 mmol/L H₂O₂. Morphological changes of nucleoli were observed under contrast microscope or electronic microscope. It was found that (1) stimulation with H₂O₂-induced nucleolar fragmentation by mediating cleavage and down-regulation of nucleolar protein, nucleolin in C₂C₁₂ myocytes and MEFs; (2) HS suppressed nucleolar fragmentation by inducing the expression of Hsp70 in an HSF1-dependent manner as indicated by assays of transfection with Hsp70 antisense oligonucleotides (AS-ONs) or recombinant plasmids of full-length Hsp70 cDNA; (3) protection of Hsp70 against nucleolar fragmentation was related to its accumulation in nucleolus mediated by nuclear localization sequence and its inhibition against cleavage and down-regulation of nucleolin. These results suggested that H₂O₂-induced nucleolar fragmentation and HS or Hsp70 inhibit H₂O₂-induced nucleolar fragmentation through the translocation of Hsp70 into nucleolar and its protection against impairment of nucleolin.</description><identifier>ISSN: 1355-8145</identifier><identifier>EISSN: 1466-1268</identifier><identifier>DOI: 10.1007/s12192-011-0292-4</identifier><identifier>PMID: 21960124</identifier><language>eng</language><publisher>Dordrecht: Springer</publisher><subject>Animals ; Apoptosis ; Biochemistry ; Biomedical and Life Sciences ; Biomedicine ; Cancer Research ; Cell Biology ; Cell Line ; Cell nucleolus ; Cell Nucleolus - drug effects ; Cell Nucleolus - metabolism ; Cellular immunity ; COS cells ; DNA-Binding Proteins - genetics ; DNA-Binding Proteins - metabolism ; Down regulation ; Heat shock proteins ; Heat Shock Transcription Factors ; HeLa cells ; HSP70 Heat-Shock Proteins - genetics ; HSP70 Heat-Shock Proteins - metabolism ; Hydrogen Peroxide - pharmacology ; Immunology ; Mice ; Neurosciences ; Nucleolin ; Oligonucleotides, Antisense - pharmacology ; Original Paper ; Oxidative stress ; Phosphoproteins - metabolism ; Plasmids ; RNA-Binding Proteins - metabolism ; Shock heating ; Temperature ; Transcription Factors - genetics ; Transcription Factors - metabolism ; Transfection</subject><ispartof>Cell stress & chaperones, 2012-01, Vol.17 (1), p.121-130</ispartof><rights>2012 Cell Stress Society International</rights><rights>Cell Stress Society International 2011</rights><rights>Cell Stress Society International 2012</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c490t-e7fad0b9f438e3c44a22dab6228428ffe7a97494754c8b47caf69aa95d05a2f83</citedby><cites>FETCH-LOGICAL-c490t-e7fad0b9f438e3c44a22dab6228428ffe7a97494754c8b47caf69aa95d05a2f83</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.jstor.org/stable/pdf/41412292$$EPDF$$P50$$Gjstor$$H</linktopdf><linktohtml>$$Uhttps://www.jstor.org/stable/41412292$$EHTML$$P50$$Gjstor$$H</linktohtml><link.rule.ids>230,314,725,778,782,801,883,27911,27912,41475,42544,51306,53778,53780,58004,58237</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/21960124$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Wang, Kangkai</creatorcontrib><creatorcontrib>Deng, Gonghua</creatorcontrib><creatorcontrib>Chen, Guangwen</creatorcontrib><creatorcontrib>Liu, Meidong</creatorcontrib><creatorcontrib>Yi, Yuxin</creatorcontrib><creatorcontrib>Yang, Tubao</creatorcontrib><creatorcontrib>McMillan, Daniel R.</creatorcontrib><creatorcontrib>Xiao, Xiangzhong</creatorcontrib><title>Heat shock protein 70 inhibits hydrogen peroxide-induced nucleolar fragmentation via suppressing cleavage and down-regulation of nucleolin</title><title>Cell stress & chaperones</title><addtitle>Cell Stress and Chaperones</addtitle><addtitle>Cell Stress Chaperones</addtitle><description>It has been reported that nucleolar fragmentation is a part of the overall apoptotic morphology, however, it is currently obscure whether and how nucleolar fragmentation can be induced by hydrogen peroxide (H₂O₂) and heat shock protein 70 (Hsp70) can prevent nucleolar fragmentation. To dissect these two questions, C₂C₁₂ myogenic cells and immortalized mouse embryonic fibroblasts (MEFs) with heat shock transcriptional factor 1 (HSF1) null mutation were treated with heat shock response (HS) (42.5 ± 0.5°C for 1 h and recovery at 37°C for 24 h) and then were insulted with 0.5 mmol/L H₂O₂. Morphological changes of nucleoli were observed under contrast microscope or electronic microscope. It was found that (1) stimulation with H₂O₂-induced nucleolar fragmentation by mediating cleavage and down-regulation of nucleolar protein, nucleolin in C₂C₁₂ myocytes and MEFs; (2) HS suppressed nucleolar fragmentation by inducing the expression of Hsp70 in an HSF1-dependent manner as indicated by assays of transfection with Hsp70 antisense oligonucleotides (AS-ONs) or recombinant plasmids of full-length Hsp70 cDNA; (3) protection of Hsp70 against nucleolar fragmentation was related to its accumulation in nucleolus mediated by nuclear localization sequence and its inhibition against cleavage and down-regulation of nucleolin. These results suggested that H₂O₂-induced nucleolar fragmentation and HS or Hsp70 inhibit H₂O₂-induced nucleolar fragmentation through the translocation of Hsp70 into nucleolar and its protection against impairment of nucleolin.</description><subject>Animals</subject><subject>Apoptosis</subject><subject>Biochemistry</subject><subject>Biomedical and Life Sciences</subject><subject>Biomedicine</subject><subject>Cancer Research</subject><subject>Cell Biology</subject><subject>Cell Line</subject><subject>Cell nucleolus</subject><subject>Cell Nucleolus - drug effects</subject><subject>Cell Nucleolus - metabolism</subject><subject>Cellular immunity</subject><subject>COS cells</subject><subject>DNA-Binding Proteins - genetics</subject><subject>DNA-Binding Proteins - metabolism</subject><subject>Down regulation</subject><subject>Heat shock proteins</subject><subject>Heat Shock Transcription Factors</subject><subject>HeLa cells</subject><subject>HSP70 Heat-Shock Proteins - genetics</subject><subject>HSP70 Heat-Shock Proteins - metabolism</subject><subject>Hydrogen Peroxide - pharmacology</subject><subject>Immunology</subject><subject>Mice</subject><subject>Neurosciences</subject><subject>Nucleolin</subject><subject>Oligonucleotides, Antisense - pharmacology</subject><subject>Original Paper</subject><subject>Oxidative stress</subject><subject>Phosphoproteins - metabolism</subject><subject>Plasmids</subject><subject>RNA-Binding Proteins - metabolism</subject><subject>Shock heating</subject><subject>Temperature</subject><subject>Transcription Factors - genetics</subject><subject>Transcription Factors - 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shock protein 70 inhibits hydrogen peroxide-induced nucleolar fragmentation via suppressing cleavage and down-regulation of nucleolin</title><author>Wang, Kangkai ; Deng, Gonghua ; Chen, Guangwen ; Liu, Meidong ; Yi, Yuxin ; Yang, Tubao ; McMillan, Daniel R. ; Xiao, Xiangzhong</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c490t-e7fad0b9f438e3c44a22dab6228428ffe7a97494754c8b47caf69aa95d05a2f83</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2012</creationdate><topic>Animals</topic><topic>Apoptosis</topic><topic>Biochemistry</topic><topic>Biomedical and Life Sciences</topic><topic>Biomedicine</topic><topic>Cancer Research</topic><topic>Cell Biology</topic><topic>Cell Line</topic><topic>Cell nucleolus</topic><topic>Cell Nucleolus - drug effects</topic><topic>Cell Nucleolus - metabolism</topic><topic>Cellular immunity</topic><topic>COS cells</topic><topic>DNA-Binding Proteins - genetics</topic><topic>DNA-Binding Proteins - metabolism</topic><topic>Down regulation</topic><topic>Heat shock proteins</topic><topic>Heat Shock Transcription Factors</topic><topic>HeLa cells</topic><topic>HSP70 Heat-Shock Proteins - genetics</topic><topic>HSP70 Heat-Shock Proteins - metabolism</topic><topic>Hydrogen Peroxide - pharmacology</topic><topic>Immunology</topic><topic>Mice</topic><topic>Neurosciences</topic><topic>Nucleolin</topic><topic>Oligonucleotides, Antisense - pharmacology</topic><topic>Original Paper</topic><topic>Oxidative stress</topic><topic>Phosphoproteins - metabolism</topic><topic>Plasmids</topic><topic>RNA-Binding Proteins - metabolism</topic><topic>Shock heating</topic><topic>Temperature</topic><topic>Transcription Factors - genetics</topic><topic>Transcription Factors - metabolism</topic><topic>Transfection</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Wang, Kangkai</creatorcontrib><creatorcontrib>Deng, 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Chaperones</addtitle><date>2012-01-01</date><risdate>2012</risdate><volume>17</volume><issue>1</issue><spage>121</spage><epage>130</epage><pages>121-130</pages><issn>1355-8145</issn><eissn>1466-1268</eissn><abstract>It has been reported that nucleolar fragmentation is a part of the overall apoptotic morphology, however, it is currently obscure whether and how nucleolar fragmentation can be induced by hydrogen peroxide (H₂O₂) and heat shock protein 70 (Hsp70) can prevent nucleolar fragmentation. To dissect these two questions, C₂C₁₂ myogenic cells and immortalized mouse embryonic fibroblasts (MEFs) with heat shock transcriptional factor 1 (HSF1) null mutation were treated with heat shock response (HS) (42.5 ± 0.5°C for 1 h and recovery at 37°C for 24 h) and then were insulted with 0.5 mmol/L H₂O₂. Morphological changes of nucleoli were observed under contrast microscope or electronic microscope. It was found that (1) stimulation with H₂O₂-induced nucleolar fragmentation by mediating cleavage and down-regulation of nucleolar protein, nucleolin in C₂C₁₂ myocytes and MEFs; (2) HS suppressed nucleolar fragmentation by inducing the expression of Hsp70 in an HSF1-dependent manner as indicated by assays of transfection with Hsp70 antisense oligonucleotides (AS-ONs) or recombinant plasmids of full-length Hsp70 cDNA; (3) protection of Hsp70 against nucleolar fragmentation was related to its accumulation in nucleolus mediated by nuclear localization sequence and its inhibition against cleavage and down-regulation of nucleolin. These results suggested that H₂O₂-induced nucleolar fragmentation and HS or Hsp70 inhibit H₂O₂-induced nucleolar fragmentation through the translocation of Hsp70 into nucleolar and its protection against impairment of nucleolin.</abstract><cop>Dordrecht</cop><pub>Springer</pub><pmid>21960124</pmid><doi>10.1007/s12192-011-0292-4</doi><tpages>10</tpages><oa>free_for_read</oa></addata></record> |
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| source | MEDLINE; Jstor Complete Legacy; Springer Nature - Complete Springer Journals; EZB-FREE-00999 freely available EZB journals; PubMed Central; Alma/SFX Local Collection |
| subjects | Animals Apoptosis Biochemistry Biomedical and Life Sciences Biomedicine Cancer Research Cell Biology Cell Line Cell nucleolus Cell Nucleolus - drug effects Cell Nucleolus - metabolism Cellular immunity COS cells DNA-Binding Proteins - genetics DNA-Binding Proteins - metabolism Down regulation Heat shock proteins Heat Shock Transcription Factors HeLa cells HSP70 Heat-Shock Proteins - genetics HSP70 Heat-Shock Proteins - metabolism Hydrogen Peroxide - pharmacology Immunology Mice Neurosciences Nucleolin Oligonucleotides, Antisense - pharmacology Original Paper Oxidative stress Phosphoproteins - metabolism Plasmids RNA-Binding Proteins - metabolism Shock heating Temperature Transcription Factors - genetics Transcription Factors - metabolism Transfection |
| title | Heat shock protein 70 inhibits hydrogen peroxide-induced nucleolar fragmentation via suppressing cleavage and down-regulation of nucleolin |
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