Abstract
High-density lipoprotein (HDL) is a lipid and protein complex that consists of apolipoproteins and lower level HDL-associated enzymes. HDL dysfunction is a factor in atherosclerosis and decreases patient survival. Mass spectrometry- (MS-) based proteomics provides a high throughput approach for analyzing the composition and modifications of complex HDL proteins in diseases. HDL can be separated according to size, surface charge, electronegativity, or apoprotein composition. MS-based proteomics on subfractionated HDL then allows investigation of lipoprotein roles in diseases. Herein, we review recent developments in MS-based quantitative proteomic techniques, HDL proteomics and lipoprotein modifications in diseases, and HDL subfractionation studies. We also discuss future directions and perspectives in MS-based proteomics on HDL.
Highlights
High-density lipoprotein (HDL) is a heterogeneous complex of differing size, density, surface charge, and lipoprotein content [1]
Low plasma HDL-C has long been known as a significant independent risk factor of atherosclerosis in patients with coronary artery disease (CAD), diabetes [48, 49], and uremia [20]; it persists even after adjustment for obesity and hypertriglyceridemia [50]
HDL proteomics have been extensively reviewed [13, 76, 77]; in this review, we focus on recently published papers (Table 1)
Summary
High-density lipoprotein (HDL) is a heterogeneous complex of differing size, density, surface charge, and lipoprotein content [1]. Serum HDL level is thought to be inversely related with atherosclerotic vascular disease (ASVD) risk [2, 3]. Several clinical studies using therapeutic serum HDL-elevating agents failed to demonstrate their clinical benefits [7]. Recent studies have shown that HDL protein oxidation, glycation, carbamylation, and other modifications can compromise HDL function and result in increased ASVD risk [8,9,10]. Protein composition changes or modifications on HDL can act as biomarkers for ASVD. With the improvement in subfractionation of HDL complexes and the advance in MS-based proteomic approaches, it is feasible to analyze HDL proteome and their modifications, giving a global view of biological processes and molecular functions of HDL proteins in diseases
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