A proteomic analysis of C-reactive protein stimulated THP-1 monocytes
<p>Abstract</p> <p>Background</p> <p>C-reactive protein (CRP) is a predictor of cardiovascular risk. It circulates as a pentameric protein in plasma. Recently, a potential dissociation mechanism from the disc-shaped pentameric CRP (pCRP) into single monomers (monomeric...
| Main Authors: | , , , , , , , , |
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| Format: | Article |
| Language: | English |
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BMC
2011-01-01
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| Series: | Proteome Science |
| Online Access: | http://www.proteomesci.com/content/9/1/1 |
| _version_ | 1831538600203780096 |
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| author | Ayhan Mustafa Lancaster Graeme I Oliva Karen Habersberger Jonathon Eisenhardt Steffen U Woollard Kevin J Bannasch Holger Rice Greg E Peter Karlheinz |
| author_facet | Ayhan Mustafa Lancaster Graeme I Oliva Karen Habersberger Jonathon Eisenhardt Steffen U Woollard Kevin J Bannasch Holger Rice Greg E Peter Karlheinz |
| author_sort | Ayhan Mustafa |
| collection | DOAJ |
| description | <p>Abstract</p> <p>Background</p> <p>C-reactive protein (CRP) is a predictor of cardiovascular risk. It circulates as a pentameric protein in plasma. Recently, a potential dissociation mechanism from the disc-shaped pentameric CRP (pCRP) into single monomers (monomeric or mCRP) has been described. It has been shown that mCRP has strong pro-inflammatory effects on monocytes. To further define the role of mCRP in determining monocyte phenotype, the effects of CRP isoforms on THP-1 protein expression profiles were determined. The hypothesis to be tested was that mCRP induces specific changes in the protein expression profile of THP-1 cells that differ from that of pCRP.</p> <p>Methods</p> <p>Protein cell lysates from control and mCRP, pCRP or LPS-treated THP-1 cells were displayed using 2-dimensional SDS PAGE and compared. Differentially expressed proteins were identified by MALDI-TOF MS and confirmed by Western blotting.</p> <p>Results</p> <p>mCRP significantly up-regulates ubiquitin-activating enzyme E1, a member of the ubiquitin-proteasome system in THP-1 monocytes. Furthermore, HSP 70, alpha-actinin-4 (ACTN4) and alpha-enolase/enolase 1 were upregulated. The proteomic profile of LPS and pCRP treated monocytes differ significantly from that of mCRP.</p> <p>Conclusion</p> <p>The data obtained in this study support the hypothesis that isoform-specific effects of CRP may differentially regulate the phenotype of monocytes.</p> |
| first_indexed | 2024-12-16T23:26:56Z |
| format | Article |
| id | doaj.art-4fdd65a4746448eaab3c9201611c22d1 |
| institution | Directory Open Access Journal |
| issn | 1477-5956 |
| language | English |
| last_indexed | 2024-12-16T23:26:56Z |
| publishDate | 2011-01-01 |
| publisher | BMC |
| record_format | Article |
| series | Proteome Science |
| spelling | doaj.art-4fdd65a4746448eaab3c9201611c22d12022-12-21T22:11:59ZengBMCProteome Science1477-59562011-01-0191110.1186/1477-5956-9-1A proteomic analysis of C-reactive protein stimulated THP-1 monocytesAyhan MustafaLancaster Graeme IOliva KarenHabersberger JonathonEisenhardt Steffen UWoollard Kevin JBannasch HolgerRice Greg EPeter Karlheinz<p>Abstract</p> <p>Background</p> <p>C-reactive protein (CRP) is a predictor of cardiovascular risk. It circulates as a pentameric protein in plasma. Recently, a potential dissociation mechanism from the disc-shaped pentameric CRP (pCRP) into single monomers (monomeric or mCRP) has been described. It has been shown that mCRP has strong pro-inflammatory effects on monocytes. To further define the role of mCRP in determining monocyte phenotype, the effects of CRP isoforms on THP-1 protein expression profiles were determined. The hypothesis to be tested was that mCRP induces specific changes in the protein expression profile of THP-1 cells that differ from that of pCRP.</p> <p>Methods</p> <p>Protein cell lysates from control and mCRP, pCRP or LPS-treated THP-1 cells were displayed using 2-dimensional SDS PAGE and compared. Differentially expressed proteins were identified by MALDI-TOF MS and confirmed by Western blotting.</p> <p>Results</p> <p>mCRP significantly up-regulates ubiquitin-activating enzyme E1, a member of the ubiquitin-proteasome system in THP-1 monocytes. Furthermore, HSP 70, alpha-actinin-4 (ACTN4) and alpha-enolase/enolase 1 were upregulated. The proteomic profile of LPS and pCRP treated monocytes differ significantly from that of mCRP.</p> <p>Conclusion</p> <p>The data obtained in this study support the hypothesis that isoform-specific effects of CRP may differentially regulate the phenotype of monocytes.</p>http://www.proteomesci.com/content/9/1/1 |
| spellingShingle | Ayhan Mustafa Lancaster Graeme I Oliva Karen Habersberger Jonathon Eisenhardt Steffen U Woollard Kevin J Bannasch Holger Rice Greg E Peter Karlheinz A proteomic analysis of C-reactive protein stimulated THP-1 monocytes Proteome Science |
| title | A proteomic analysis of C-reactive protein stimulated THP-1 monocytes |
| title_full | A proteomic analysis of C-reactive protein stimulated THP-1 monocytes |
| title_fullStr | A proteomic analysis of C-reactive protein stimulated THP-1 monocytes |
| title_full_unstemmed | A proteomic analysis of C-reactive protein stimulated THP-1 monocytes |
| title_short | A proteomic analysis of C-reactive protein stimulated THP-1 monocytes |
| title_sort | proteomic analysis of c reactive protein stimulated thp 1 monocytes |
| url | http://www.proteomesci.com/content/9/1/1 |
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