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Submitted on October 16, 2006
Revised on January 2, 2007
Accepted on January 8, 2007

Quantitative proteomic analysis of human endothelial cell membrane rafts: Evidence of MARCKS and MRP regulation in the sphingosine 1-phosphate-induced barrier enhancement

Yurong Guo, Patrick A Singleton, Austin Rowshan, Marjan Gucek, Robert N Cole, David R. M. Graham, Jennifer E Van Eyk, and Joe G. N. Garcia

Department of Medicine, Johns Hopkins University, Baltimore, MD 21224

Corresponding Author: yguo7{at}jhmi.edu

Endothelial cell barrier dysfunction results in the increased vascular permeability observed in inflammation, tumor metastasis, angiogenesis, and atherosclerosis. Sphingosine 1-phosphate (S1P), a biologically-active phosphorylated lipid growth factor released from activated platelets, enhances the endothelial cell barrier integrity in vitro and in vivo. To begin to identify the molecular mechanisms mediating S1P induced endothelial barrier enhancement, quantitative proteomic analysis (iTRAQTM) was performed on membrane rafts isolated from human pulmonary artery endothelial cells in the absence or presence of S1P stimulation. Our results demonstrated that S1P mediates rapid and specific recruitment (1 µM, 5min) of myristoylated alanine-rich C-kinase substrate (MARCKS) and MARCKS-related protein (MRP) to membrane rafts. Western blot experiments confirmed these findings with both MARCKS and MRP. Finally, siRNA-mediated silencing of MARCKS or MRP or both attenuates S1P -mediated endothelial cell barrier enhancement. These data suggest the regulation of S1P-mediated endothelial cell barrier enhancement via the cell specific localization of MARCKS and MRP and validate the utility of proteomic approaches in the identification of novel molecular targets.


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