Quantitative phosphoproteomic analysis of prion-infected neuronal cells
<p>Abstract</p> <p>Prion diseases or transmissible spongiform encephalopathies (TSEs) are fatal diseases associated with the conversion of the cellular prion protein (PrP<sup>C</sup>) to the abnormal prion protein (PrP<sup>Sc</sup>). Since the molecular mech...
| Main Authors: | , , , |
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| Format: | Article |
| Language: | English |
| Published: |
BMC
2010-09-01
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| Series: | Cell Communication and Signaling |
| Online Access: | http://www.biosignaling.com/content/8/1/28 |
| _version_ | 1817994225985257472 |
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| author | Löwer Johannes Ajuh Paul Wagner Wibke Wessler Silja |
| author_facet | Löwer Johannes Ajuh Paul Wagner Wibke Wessler Silja |
| author_sort | Löwer Johannes |
| collection | DOAJ |
| description | <p>Abstract</p> <p>Prion diseases or transmissible spongiform encephalopathies (TSEs) are fatal diseases associated with the conversion of the cellular prion protein (PrP<sup>C</sup>) to the abnormal prion protein (PrP<sup>Sc</sup>). Since the molecular mechanisms in pathogenesis are widely unclear, we analyzed the global phospho-proteome and detected a differential pattern of tyrosine- and threonine phosphorylated proteins in PrP<sup>Sc</sup>-replicating and pentosan polysulfate (PPS)-rescued N2a cells in two-dimensional gel electrophoresis. To quantify phosphorylated proteins, we performed a SILAC (stable isotope labeling by amino acids in cell culture) analysis and identified 105 proteins, which showed a regulated phosphorylation upon PrP<sup>Sc </sup>infection. Among those proteins, we validated the dephosphorylation of stathmin and Cdc2 and the induced phosphorylation of cofilin in PrP<sup>Sc</sup>-infected N2a cells in Western blot analyses. Our analysis showed for the first time a differentially regulated phospho-proteome in PrP<sup>Sc </sup>infection, which could contribute to the establishment of novel protein markers and to the development of novel therapeutic intervention strategies in targeting prion-associated disease.</p> |
| first_indexed | 2024-04-14T01:49:12Z |
| format | Article |
| id | doaj.art-ee5218bf498a433c83f23f13a583adff |
| institution | Directory Open Access Journal |
| issn | 1478-811X |
| language | English |
| last_indexed | 2024-04-14T01:49:12Z |
| publishDate | 2010-09-01 |
| publisher | BMC |
| record_format | Article |
| series | Cell Communication and Signaling |
| spelling | doaj.art-ee5218bf498a433c83f23f13a583adff2022-12-22T02:19:24ZengBMCCell Communication and Signaling1478-811X2010-09-01812810.1186/1478-811X-8-28Quantitative phosphoproteomic analysis of prion-infected neuronal cellsLöwer JohannesAjuh PaulWagner WibkeWessler Silja<p>Abstract</p> <p>Prion diseases or transmissible spongiform encephalopathies (TSEs) are fatal diseases associated with the conversion of the cellular prion protein (PrP<sup>C</sup>) to the abnormal prion protein (PrP<sup>Sc</sup>). Since the molecular mechanisms in pathogenesis are widely unclear, we analyzed the global phospho-proteome and detected a differential pattern of tyrosine- and threonine phosphorylated proteins in PrP<sup>Sc</sup>-replicating and pentosan polysulfate (PPS)-rescued N2a cells in two-dimensional gel electrophoresis. To quantify phosphorylated proteins, we performed a SILAC (stable isotope labeling by amino acids in cell culture) analysis and identified 105 proteins, which showed a regulated phosphorylation upon PrP<sup>Sc </sup>infection. Among those proteins, we validated the dephosphorylation of stathmin and Cdc2 and the induced phosphorylation of cofilin in PrP<sup>Sc</sup>-infected N2a cells in Western blot analyses. Our analysis showed for the first time a differentially regulated phospho-proteome in PrP<sup>Sc </sup>infection, which could contribute to the establishment of novel protein markers and to the development of novel therapeutic intervention strategies in targeting prion-associated disease.</p>http://www.biosignaling.com/content/8/1/28 |
| spellingShingle | Löwer Johannes Ajuh Paul Wagner Wibke Wessler Silja Quantitative phosphoproteomic analysis of prion-infected neuronal cells Cell Communication and Signaling |
| title | Quantitative phosphoproteomic analysis of prion-infected neuronal cells |
| title_full | Quantitative phosphoproteomic analysis of prion-infected neuronal cells |
| title_fullStr | Quantitative phosphoproteomic analysis of prion-infected neuronal cells |
| title_full_unstemmed | Quantitative phosphoproteomic analysis of prion-infected neuronal cells |
| title_short | Quantitative phosphoproteomic analysis of prion-infected neuronal cells |
| title_sort | quantitative phosphoproteomic analysis of prion infected neuronal cells |
| url | http://www.biosignaling.com/content/8/1/28 |
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