Retinol-induced changes in the phosphorylation levels of histones and high mobility group proteins from sertoli cells
Autor(a) principal: | |
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Data de Publicação: | 2000 |
Outros Autores: | , , , , , |
Tipo de documento: | Artigo |
Idioma: | eng |
Título da fonte: | Repositório Institucional da UFRGS |
Texto Completo: | http://hdl.handle.net/10183/21160 |
Resumo: | Chromatin proteins play a role in the organization and functions of DNA. Covalent modifications of nuclear proteins modulate their interactions with DNA sequences and are probably one of the multiple factors involved in the process of switch on/off transcriptionally active regions of DNA. Histones and high mobility group proteins (HMG) are subject to many covalent modifications that may modulate their capacity to bind to DNA. We investigated the changes induced in the phosphorylation pattern of cultured Wistar rat Sertoli cell histones and high mobility group protein subfamilies exposed to 7 µM retinol for up to 48 h. In each experiment, 6 h before the end of the retinol treatment each culture flask received 370 KBq/ml [32P]-phosphate. The histone and HMGs were isolated as previously described [Moreira et al. Medical Science Research (1994) 22: 783-784]. The total protein obtained by either method was quantified and electrophoresed as described by Spiker [Analytical Biochemistry (1980) 108: 263-265]. The gels were stained with Coomassie brilliant blue R-250 and the stained bands were cut and dissolved in 0.5 ml 30% H2O2 at 60oC for 12 h. The vials were chilled and 5.0 ml scintillation liquid was added. The radioactivity in each vial was determined with a liquid scintillation counter. Retinol treatment significantly changed the pattern of each subfamily of histone and high mobility group proteins. |
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Moreira, Jose Claudio FonsecaDal Pizzol, FelipeRocha, Adriana Brondani daKlamt, FabioRibeiro, Nede CarlosFerreira, Carlos Jose SarmentoBernard, Elena Aida2010-04-24T04:15:32Z20000100-879Xhttp://hdl.handle.net/10183/21160000297137Chromatin proteins play a role in the organization and functions of DNA. Covalent modifications of nuclear proteins modulate their interactions with DNA sequences and are probably one of the multiple factors involved in the process of switch on/off transcriptionally active regions of DNA. Histones and high mobility group proteins (HMG) are subject to many covalent modifications that may modulate their capacity to bind to DNA. We investigated the changes induced in the phosphorylation pattern of cultured Wistar rat Sertoli cell histones and high mobility group protein subfamilies exposed to 7 µM retinol for up to 48 h. In each experiment, 6 h before the end of the retinol treatment each culture flask received 370 KBq/ml [32P]-phosphate. The histone and HMGs were isolated as previously described [Moreira et al. Medical Science Research (1994) 22: 783-784]. The total protein obtained by either method was quantified and electrophoresed as described by Spiker [Analytical Biochemistry (1980) 108: 263-265]. The gels were stained with Coomassie brilliant blue R-250 and the stained bands were cut and dissolved in 0.5 ml 30% H2O2 at 60oC for 12 h. The vials were chilled and 5.0 ml scintillation liquid was added. The radioactivity in each vial was determined with a liquid scintillation counter. Retinol treatment significantly changed the pattern of each subfamily of histone and high mobility group proteins.application/pdfengBrazilian journal of medical and biological research = Revista brasileira de pesquisas médicas e biológicas. Ribeirão Preto, SP. Vol. 33, no. 3 (Mar. 2000), p. 287-293Vitamina ACélula de sertoliSertoli cellsPhosphorylationHistonesHigh mobility group proteinsRetinolRetinol-induced changes in the phosphorylation levels of histones and high mobility group proteins from sertoli cellsinfo:eu-repo/semantics/articleinfo:eu-repo/semantics/otherinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/openAccessreponame:Repositório Institucional da UFRGSinstname:Universidade Federal do Rio Grande do Sul (UFRGS)instacron:UFRGSORIGINAL000297137.pdf000297137.pdfTexto completo (inglês)application/pdf154080http://www.lume.ufrgs.br/bitstream/10183/21160/1/000297137.pdf0b949edd240b60f15e74e66c612138f1MD51TEXT000297137.pdf.txt000297137.pdf.txtExtracted Texttext/plain28760http://www.lume.ufrgs.br/bitstream/10183/21160/2/000297137.pdf.txt9d6c388a1556685e9cb12dc0c5adf29eMD52THUMBNAIL000297137.pdf.jpg000297137.pdf.jpgGenerated Thumbnailimage/jpeg1658http://www.lume.ufrgs.br/bitstream/10183/21160/3/000297137.pdf.jpg6dfe78861f33965d69bf3efb5c541fadMD5310183/211602022-10-01 05:09:29.824923oai:www.lume.ufrgs.br:10183/21160Repositório de PublicaçõesPUBhttps://lume.ufrgs.br/oai/requestopendoar:2022-10-01T08:09:29Repositório Institucional da UFRGS - Universidade Federal do Rio Grande do Sul (UFRGS)false |
dc.title.pt_BR.fl_str_mv |
Retinol-induced changes in the phosphorylation levels of histones and high mobility group proteins from sertoli cells |
title |
Retinol-induced changes in the phosphorylation levels of histones and high mobility group proteins from sertoli cells |
spellingShingle |
Retinol-induced changes in the phosphorylation levels of histones and high mobility group proteins from sertoli cells Moreira, Jose Claudio Fonseca Vitamina A Célula de sertoli Sertoli cells Phosphorylation Histones High mobility group proteins Retinol |
title_short |
Retinol-induced changes in the phosphorylation levels of histones and high mobility group proteins from sertoli cells |
title_full |
Retinol-induced changes in the phosphorylation levels of histones and high mobility group proteins from sertoli cells |
title_fullStr |
Retinol-induced changes in the phosphorylation levels of histones and high mobility group proteins from sertoli cells |
title_full_unstemmed |
Retinol-induced changes in the phosphorylation levels of histones and high mobility group proteins from sertoli cells |
title_sort |
Retinol-induced changes in the phosphorylation levels of histones and high mobility group proteins from sertoli cells |
author |
Moreira, Jose Claudio Fonseca |
author_facet |
Moreira, Jose Claudio Fonseca Dal Pizzol, Felipe Rocha, Adriana Brondani da Klamt, Fabio Ribeiro, Nede Carlos Ferreira, Carlos Jose Sarmento Bernard, Elena Aida |
author_role |
author |
author2 |
Dal Pizzol, Felipe Rocha, Adriana Brondani da Klamt, Fabio Ribeiro, Nede Carlos Ferreira, Carlos Jose Sarmento Bernard, Elena Aida |
author2_role |
author author author author author author |
dc.contributor.author.fl_str_mv |
Moreira, Jose Claudio Fonseca Dal Pizzol, Felipe Rocha, Adriana Brondani da Klamt, Fabio Ribeiro, Nede Carlos Ferreira, Carlos Jose Sarmento Bernard, Elena Aida |
dc.subject.por.fl_str_mv |
Vitamina A Célula de sertoli |
topic |
Vitamina A Célula de sertoli Sertoli cells Phosphorylation Histones High mobility group proteins Retinol |
dc.subject.eng.fl_str_mv |
Sertoli cells Phosphorylation Histones High mobility group proteins Retinol |
description |
Chromatin proteins play a role in the organization and functions of DNA. Covalent modifications of nuclear proteins modulate their interactions with DNA sequences and are probably one of the multiple factors involved in the process of switch on/off transcriptionally active regions of DNA. Histones and high mobility group proteins (HMG) are subject to many covalent modifications that may modulate their capacity to bind to DNA. We investigated the changes induced in the phosphorylation pattern of cultured Wistar rat Sertoli cell histones and high mobility group protein subfamilies exposed to 7 µM retinol for up to 48 h. In each experiment, 6 h before the end of the retinol treatment each culture flask received 370 KBq/ml [32P]-phosphate. The histone and HMGs were isolated as previously described [Moreira et al. Medical Science Research (1994) 22: 783-784]. The total protein obtained by either method was quantified and electrophoresed as described by Spiker [Analytical Biochemistry (1980) 108: 263-265]. The gels were stained with Coomassie brilliant blue R-250 and the stained bands were cut and dissolved in 0.5 ml 30% H2O2 at 60oC for 12 h. The vials were chilled and 5.0 ml scintillation liquid was added. The radioactivity in each vial was determined with a liquid scintillation counter. Retinol treatment significantly changed the pattern of each subfamily of histone and high mobility group proteins. |
publishDate |
2000 |
dc.date.issued.fl_str_mv |
2000 |
dc.date.accessioned.fl_str_mv |
2010-04-24T04:15:32Z |
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info:eu-repo/semantics/article info:eu-repo/semantics/other |
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article |
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publishedVersion |
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http://hdl.handle.net/10183/21160 |
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0100-879X |
dc.identifier.nrb.pt_BR.fl_str_mv |
000297137 |
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http://hdl.handle.net/10183/21160 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.ispartof.pt_BR.fl_str_mv |
Brazilian journal of medical and biological research = Revista brasileira de pesquisas médicas e biológicas. Ribeirão Preto, SP. Vol. 33, no. 3 (Mar. 2000), p. 287-293 |
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openAccess |
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