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Registro Completo |
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Biblioteca(s): |
Epagri-Sede. |
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Data corrente: |
20/07/2012 |
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Data da última atualização: |
20/07/2012 |
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Tipo da produção científica: |
Artigo em Periódico Indexado |
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Autoria: |
COGO, K.; ANDRADE, A.; LABATE, C. A.; BERGAMASCHI, C. C.; BERTO, L. A.; FRANCO, G. C. N.; GONÇALVES, R. B.; GROPPO, F. C. |
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Afiliação: |
Epagri |
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Título: |
Proteomic analysis of Porphyromonas gingivalis exposed to nicotine and cotinine. |
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Ano de publicação: |
2012 |
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Fonte/Imprenta: |
JOURNAL OF PERIODONTAL RESEARCH, Inglaterra, v. 1, n. 1, p. 1-10, 2012. |
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Idioma: |
Inglês |
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Conteúdo: |
Cogo K, de Andrade A, Labate CA, Bergamaschi CC, Berto LA, Franco GCN, Gonçalves RB, Groppo FC. Proteomic analysis of Porphyromonas gingivalis exposed to nicotine and cotinine. J Periodont Res 2012; doi: 10.1111/j.1600-0765.2012.01494.x.©2012 John Wiley & Sons A/S Background and Objective: Smokers are more predisposed than nonsmokers to infection with Porphyromonas gingivalis, one of the most important pathogens involved in the onset and development of periodontitis. It has also been observed that tobacco, and tobacco derivatives such as nicotine and cotinine, can induce modifications to P. gingivalis virulence. However, the effect of the major compounds derived from cigarettes on expression of protein by P. gingivalis is poorly understood. Therefore, this study aimed to evaluate and compare the effects of nicotine and cotinine on the P. gingivalis proteomic profile. Material and Methods: Total proteins of P. gingivalis exposed to nicotine and cotinine were extracted and separated by two-dimensional electrophoresis. Proteins differentially expressed were successfully identified through liquid chromatography-mass spectrometry and primary sequence databases using MASCOT search engine, and gene ontology was carried out using DAVID tools. Results: Of the approximately 410 protein spots that were reproducibly detected on each gel, 23 were differentially expressed in at least one of the treatments. A particular increase was seen in proteins involved in metabolism, virulence and acquisition of peptides, protein synthesis and folding, transcription and oxidative stress. Few proteins showed significant decreases in expression; those that did are involved in cell envelope biosynthesis and proteolysis and also in metabolism. Conclusion: Our results characterized the changes in the proteome of P. gingivalis following exposure to nicotine and cotinine, suggesting that these substances may modulate, with minor changes, protein expression. The present study is, in part, a step toward understanding the potential smoke-pathogen interaction that may occur in smokers with periodontitis. MenosCogo K, de Andrade A, Labate CA, Bergamaschi CC, Berto LA, Franco GCN, Gonçalves RB, Groppo FC. Proteomic analysis of Porphyromonas gingivalis exposed to nicotine and cotinine. J Periodont Res 2012; doi: 10.1111/j.1600-0765.2012.01494.x.©2012 John Wiley & Sons A/S Background and Objective: Smokers are more predisposed than nonsmokers to infection with Porphyromonas gingivalis, one of the most important pathogens involved in the onset and development of periodontitis. It has also been observed that tobacco, and tobacco derivatives such as nicotine and cotinine, can induce modifications to P. gingivalis virulence. However, the effect of the major compounds derived from cigarettes on expression of protein by P. gingivalis is poorly understood. Therefore, this study aimed to evaluate and compare the effects of nicotine and cotinine on the P. gingivalis proteomic profile. Material and Methods: Total proteins of P. gingivalis exposed to nicotine and cotinine were extracted and separated by two-dimensional electrophoresis. Proteins differentially expressed were successfully identified through liquid chromatography-mass spectrometry and primary sequence databases using MASCOT search engine, and gene ontology was carried out using DAVID tools. Results: Of the approximately 410 protein spots that were reproducibly detected on each gel, 23 were differentially expressed in at least one of the treatments. A particular increase was seen in proteins involved in metabol... Mostrar Tudo |
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Palavras-Chave: |
Proteina; Proteoma. |
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Categoria do assunto: |
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Marc: |
LEADER 02552naa a2200145 a 4500
001 1086117
005 2012-07-20
008 2012 bl uuuu u00u1 u #d
100 1 $aEpagri
245 $aProteomic analysis of Porphyromonas gingivalis exposed to nicotine and cotinine.
260 $c2012
520 $aCogo K, de Andrade A, Labate CA, Bergamaschi CC, Berto LA, Franco GCN, Gonçalves RB, Groppo FC. Proteomic analysis of Porphyromonas gingivalis exposed to nicotine and cotinine. J Periodont Res 2012; doi: 10.1111/j.1600-0765.2012.01494.x.©2012 John Wiley & Sons A/S Background and Objective: Smokers are more predisposed than nonsmokers to infection with Porphyromonas gingivalis, one of the most important pathogens involved in the onset and development of periodontitis. It has also been observed that tobacco, and tobacco derivatives such as nicotine and cotinine, can induce modifications to P. gingivalis virulence. However, the effect of the major compounds derived from cigarettes on expression of protein by P. gingivalis is poorly understood. Therefore, this study aimed to evaluate and compare the effects of nicotine and cotinine on the P. gingivalis proteomic profile. Material and Methods: Total proteins of P. gingivalis exposed to nicotine and cotinine were extracted and separated by two-dimensional electrophoresis. Proteins differentially expressed were successfully identified through liquid chromatography-mass spectrometry and primary sequence databases using MASCOT search engine, and gene ontology was carried out using DAVID tools. Results: Of the approximately 410 protein spots that were reproducibly detected on each gel, 23 were differentially expressed in at least one of the treatments. A particular increase was seen in proteins involved in metabolism, virulence and acquisition of peptides, protein synthesis and folding, transcription and oxidative stress. Few proteins showed significant decreases in expression; those that did are involved in cell envelope biosynthesis and proteolysis and also in metabolism. Conclusion: Our results characterized the changes in the proteome of P. gingivalis following exposure to nicotine and cotinine, suggesting that these substances may modulate, with minor changes, protein expression. The present study is, in part, a step toward understanding the potential smoke-pathogen interaction that may occur in smokers with periodontitis.
653 $aProteina
653 $aProteoma
773 $tJOURNAL OF PERIODONTAL RESEARCH, Inglaterra$gv. 1, n. 1, p. 1-10, 2012.
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Epagri-Sede (Epagri-Sede) |
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Biblioteca(s): |
Epagri-Sede. |
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Data corrente: |
07/06/2011 |
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Data da última atualização: |
07/06/2011 |
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Tipo da produção científica: |
Artigo em Periódico Indexado |
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Circulação/Nível: |
-- - -- |
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Autoria: |
COSTA-JUNIOR, H. M.; GARAVELLO, N. M.; DUARTE, M. L.; BERTI, D. A.; GLASER, T.; ANDRADE, A.; LABATE, C. A.; FERREIRA, A. T. S.; JE, P.; J, X.; JE, K.; D., S.; PERALES, J. E. A.; XAVIER-NETO, J.; KRIEGER, J. E.; SCHECHTMAN, D. |
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Afiliação: |
Epagri |
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Título: |
Phosphoproteomics profiling suggests a role for nuclear ?IPKC in transcription processes of undifferentiated murine embryonic stem cells. |
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Ano de publicação: |
2010 |
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Fonte/Imprenta: |
Journal of Proteome Research, EEU, v. 9, n. 12, p. 6191-6206, 2010. |
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Idioma: |
Inglês |
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Conteúdo: |
Protein kinase C (PKC) plays a key role in embryonic stem cell (ESC) proliferation, self-renewal, and differentiation. However, the function of specific PKC isoenzymes have yet to be determined. Of the PKCs expressed in undifferentiated ESCs, âIPKC was the only isoenzyme abundantly expressed in the nuclei. To investigate the role of âÉPKC in these cells, we employed a phosphoproteomics strategy and used two classical (cPKC) peptide modulators and one âIPKC-specific inhibitor peptide. We identified 13 nuclear proteins that are direct or indirect âÉPKC substrates in undifferentiated ESCs. These proteins are known to be involved in regulating transcription, splicing, and chromatin remodeling during proliferation and differentiation. Inhibiting âÉPKC had no effect on DNA synthesis in undifferentiated ESCs. However, upon differentiation, many cells seized to express âÉPKC and âÉPKC was frequently found in the cytoplasm. Taken together, our results suggest that âIPKC takes part in the processes that maintain ESCs in their undifferentiated state. |
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Palavras-Chave: |
Proteoma. |
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Categoria do assunto: |
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Marc: |
LEADER 01514naa a2200133 a 4500
001 1077294
005 2011-06-07
008 2010 bl uuuu u00u1 u #d
100 1 $aEpagri
245 $aPhosphoproteomics profiling suggests a role for nuclear ?IPKC in transcription processes of undifferentiated murine embryonic stem cells.
260 $c2010
520 $aProtein kinase C (PKC) plays a key role in embryonic stem cell (ESC) proliferation, self-renewal, and differentiation. However, the function of specific PKC isoenzymes have yet to be determined. Of the PKCs expressed in undifferentiated ESCs, âIPKC was the only isoenzyme abundantly expressed in the nuclei. To investigate the role of âÉPKC in these cells, we employed a phosphoproteomics strategy and used two classical (cPKC) peptide modulators and one âIPKC-specific inhibitor peptide. We identified 13 nuclear proteins that are direct or indirect âÉPKC substrates in undifferentiated ESCs. These proteins are known to be involved in regulating transcription, splicing, and chromatin remodeling during proliferation and differentiation. Inhibiting âÉPKC had no effect on DNA synthesis in undifferentiated ESCs. However, upon differentiation, many cells seized to express âÉPKC and âÉPKC was frequently found in the cytoplasm. Taken together, our results suggest that âIPKC takes part in the processes that maintain ESCs in their undifferentiated state.
653 $aProteoma
773 $tJournal of Proteome Research, EEU$gv. 9, n. 12, p. 6191-6206, 2010.
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