Characterization of Inflammatory and Immune Processes

Proteomic analysis of the inflammatory response of endothelial cells

 

In collaboration with the team of J-P Girard at IPBS, we use large-scale proteomic analysis associated with label-free quantification to study the pathways and processes activated in endothelial cells (ECs) under inflammatory conditions. Using such methods, we could extensively map the ECs proteome, and provided the most complete proteomic characterization to date of the human EC response to several inflammatory cytokines, such as TNFα, IFNg and IL1β.

Recently we used such a global proteomic approach to analyze IL-33 function in endothelial cells. IL-33 is a nuclear cytokine from the IL-1 family that plays important roles in health and disease. We compared the extracellular and intracellular roles of IL-33 in primary human endothelial cells, and found that exogenous extracellular IL-33 acts as a cytokine inducing expression of a distinct set of proteins associated with inflammatory responses in endothelial cells, but not as a nuclear factor.

 

References

Bouyssié, Gonzalez de Peredo et al (2007) Mascot file parsing and quantification (MFPaQ), a new software to parse, validate, and quantify proteomics data generated by ICAT and SILAC mass spectrometric analyses: application to the proteomics study of membrane proteins from primary human endothelial cells. Molecular & cellular proteomics : MCP 6, 1621-1637.

Gautier et al (2012). Label-free quantification and shotgun analysis of complex proteomes by one-dimensional SDS-PAGE/NanoLC-MS: evaluation for the large scale analysis of inflammatory human endothelial cells. Molecular & cellular proteomics : MCP 11, 527-539.

Gautier et al (2016) Extracellular IL-33 cytokine, but not endogenous nuclear IL-33, regulates protein expression in endothelial cells. Sci Rep 6, 34255.

Proteomic analysis of the inflammatory response of
endothelial cells upon TNFa/IFNg stimulation