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Cell-free Biochemical Fluorometric Enzymatic Assay for High-throughput Measurement of Lipid Peroxidation in High Density Lipoprotein
Published on: October 12, 2017
Proteomic analysis of high-density lipoprotein
Farhad Rezaee1, Bruno Casetta, J Han M Levels
1Department of Vascular Medicine, Academic Medical Center, University of Amsterdam, The Netherlands. f.rezaee@amc.uva.nl
Insights
High-density lipoprotein (HDL) carries many proteins involved in lipid metabolism and atherosclerosis. This study identified 56 HDL-associated proteins using advanced proteomic techniques, enhancing our molecular understanding.
Area of Science:
- Proteomics
- Biochemistry
- Cardiovascular Science
Background:
- Plasma high-density lipoprotein (HDL) transports diverse proteins.
- Understanding HDL-associated proteins is crucial for lipid metabolism, thrombosis, inflammation, and atherosclerosis research.
Purpose of the Study:
- To comprehensively identify proteins associated with human HDL.
- To utilize advanced proteomic approaches for HDL protein profiling.
Main Methods:
- Employed a combination of proteomic techniques: 1-DE, 2-DE MALDI-TOF, isotope-coded affinity tag, and Western blot analysis.
- Utilized a one-step ultracentrifugation technique for HDL isolation to minimize protein loss.
- Confirmed HDL quality using nephelometry, high-performance gel chromatography, and Western blot analysis.
Main Results:
- Identified 56 HDL-associated proteins, including all known apolipoproteins and lipid transport proteins.
- Detected proteins involved in hemostasis, thrombosis, and the immune/complement systems.
- Found growth factors, receptors, and hormone-associated proteins linked to HDL.
Conclusions:
- The integrated proteomic approach effectively identified a large number of HDL-associated proteins.
- This comprehensive identification advances the molecular understanding of HDL functions in health and disease.
Abstract:
Plasma lipoproteins, such as high-density lipoprotein (HDL), can serve as carriers for a wide range of proteins that are involved in processes such as lipid metabolism, thrombosis, inflammation and atherosclerosis. The identification of HDL-associated proteins is essential with regards to understanding these processes at the molecular level. In this study, a combination of proteomic approaches including 1-DE and 2-DE MALDI-TOF, isotope-coded affinity tag and Western blot analysis were employed to identify proteins associated with human HDL. To minimize potential losses of HDL-associated proteins during isolation, a one-step ultracentrifugation technique was applied and the quality of purified HDL was confirmed by nephelometry, high-performance gel chromatography, and Western blot analysis. MS analysis revealed the presence of 56 HDL-associated proteins including all known apolipoproteins and lipid transport proteins. Furthermore, proteins involved in hemostasis and thrombosis, the immune and complement system were found. In addition, growth factors, receptors, hormone-associated proteins and many other proteins were found to be associated with HDL. Our approach thus resulted in the identification of a large number of proteins associated with HDL. The combination of proteomic technologies proved to be a powerful and comprehensive tool for the identification of proteins on HDL.
