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Registro Completo |
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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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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
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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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