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Quantitative S-nitrosylation proteome reveals the susceptibility of translational machinery to oxidized low-density lipoprotein in vascular endothelial cells

ABSTRACT: Oxidized low-density lipoprotein (ox-LDL) can impair endothelial function and lead to the development of atherosclerosis. Protein S-nitrosylation is sensitive to the cellular redox state and acts as a crucial regulator and executor of NO signaling pathways. Aberrant S-nitrosylation contributes to the pathogenesis of cardiovascular and cerebrovascular diseases. However, the effect of ox-LDL on S-nitrosylation and its significance for endothelial dysfunction have not been studied at the S-nitrosylation proteome level. In our study, many key proteins belonged to ribosomal structure and translational regulatory proteins, covering the entire translation process. These results indicated that S-nitrosylation of the translational machinery in vascular endothelial cells was susceptible to ox-LDL.

ORGANISM(S): Homo Sapiens

SUBMITTER: Lianli Chi

PROVIDER: PXD009386 | iProX | Wed Apr 04 00:00:00 BST 2018

REPOSITORIES: iProX

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			Action	DRS
	S-nitrosylation_1.raw	Raw
	S-nitrosylation_2.raw	Raw
	S-nitrosylation_3.raw	Raw

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Project description:High-density lipoprotein (HDL) is a mixture of complex particles mediating reverse cholesterol transport (RCT) and several cytoprotective activities. Despite its relevance for human health, many aspects of HDL-mediated lipid trafficking and cellular signaling remain elusive at the mo-lecular level. During HDL’s journey throughout the body, its functions are mediated through in-teractions with cell surface receptors on different cell types. To characterize and better under-stand the functional interplay between HDL particles and tissue, we analyzed the sur-faceome-residing receptor neighborhoods with which HDL potentially interacts. We applied a combination of chemoproteomic technologies including automated cell surface capturing (au-to-CSC) and HATRIC-based ligand–receptor capturing (HATRIC-LRC) on four different cellular model systems mimicking tissues relevant for RCT. The surfaceome analysis of EA.hy926, HEPG2, foam cells, and human aortic endothelial cells (HAECs) revealed the main currently known HDL scavenger receptor B1 (SCRB1), as well as 155 shared cell surface receptors repre-senting potential HDL-receptor interaction candidates . Since vascular endotheli-al growth factor A (VEGF-A) was recently found as a regulatory factor of transendothelial transport of HDL, we next analyzed the VEGF-modulated surfaceome of HAEC using the au-to-CSC technology. VEGF-A treatment led to the remodeling of the surfaceome of HAEC cells, including the previously reported higher surfaceome abundance of SCRB1. In total, 165 addition-al receptors were found on HAEC upon VEGF-A treatment representing SCRB1 co-regulated re-ceptors potentially involved in HDL function. Using the HATRIC-LRC technology on human endothelial cells, we specifically aimed for the identification of other bona fide (co-)receptors of HDL beyond SCRB1. HATRIC-LRC enabled, next to SCRB1, the identification of the receptor ty-rosine-protein kinase Mer (MERTK). Through RNA interference, we revealed its contribution to endothelial HDL binding and uptake. Furthermore, subsequent proximity ligation assays (PLAs) demonstrated the spatial vicinity of MERTK and SCRB1 on the endothelial cell surface. The data shown provide direct evidence for a complex and dynamic HDL receptome and that receptor nanoscale organization may influence binding and uptake of HDL.

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Quantitative S-nitrosylation proteome reveals the susceptibility of translational machinery to oxidized low-density lipoprotein in vascular endothelial cells

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