Journal
JOURNAL OF PROTEOME RESEARCH
Volume 9, Issue 6, Pages 2812-2824Publisher
AMER CHEMICAL SOC
DOI: 10.1021/pr901194x
Keywords
Oxidized phospholipid; Ox-PAPC; endothelial cell; atherosclerosis; phosphoproteomics; signal transduction; phosphatase inhibitor
Categories
Funding
- American Heart Association (Western States)
- German Academic Exchange Service
- NIH [HL030568, HG002807]
- UCLA [T32 CA009056]
- NATIONAL CANCER INSTITUTE [T32CA009056] Funding Source: NIH RePORTER
- NATIONAL HEART, LUNG, AND BLOOD INSTITUTE [P01HL030568] Funding Source: NIH RePORTER
- NATIONAL HUMAN GENOME RESEARCH INSTITUTE [K22HG002807] Funding Source: NIH RePORTER
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Previous studies have shown that oxidized products of the phospholipid PAPC (Ox-PAPC) are strong activators of aortic endothelial cells and play an important role in atherosclerosis and other inflammatory diseases. We and others have demonstrated that Ox-PAPC activates specific signaling pathways and regulates a large number of genes. Using a phosphoproteomic approach based on phosphopeptide enrichment and mass spectrometry analysis, we identified candidate changes in Ox-PAPC-induced protein phosphorylation of 228 proteins. Functional annotation of these proteins showed an enrichment of the regulation of cytoskeleton, junctional components, and tyrosine kinases, all of which may contribute to the phenotypic and molecular changes observed in endothelial cells treated with Ox-PAPC. Many changes in protein phosphorylation induced by Ox-PAPC are reported here for the first time and provide new insights into the mechanism of activation by oxidized lipids, including phosphorylation-based signal transduction.
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