Mass Spectrometry for the Monitoring of Lipoprotein Oxidations by Myeloperoxidase in Cardiovascular Diseases.
Catherine CoremansCédric DelporteFrédéric CottonPhillipe Van De BorneKarim Zouaoui BoudjeltiaPierre Van AntwerpenPublished in: Molecules (Basel, Switzerland) (2021)
Oxidative modifications of HDLs and LDLs by myeloperoxidase (MPO) are regularly mentioned in the context of atherosclerosis. The enzyme adsorbs on protein moieties and locally produces oxidizing agents to modify specific residues on apolipoproteins A-1 and B-100. Oxidation of lipoproteins by MPO (Mox) leads to dysfunctional Mox-HDLs associated with cholesterol-efflux deficiency, and Mox-LDLs that are no more recognized by the LDL receptor and become proinflammatory. Several modification sites on apoA-1 and B-100 that are specific to MPO activity are described in the literature, which seem relevant in patients with cardiovascular risk. The most appropriate analytical method to assess these modifications is based on liquid chromatography coupled with tandem mass spectrometry (LC-MS/MS). It enables the oxidized forms of apoA-1and apoB-100 to be quantified in serum, in parallel to a quantification of these apolipoproteins. Current standard methods to quantify apolipoproteins are based on immunoassays that are well standardized with good analytical performances despite the cost and the heterogeneity of the commercialized kits. Mass spectrometry can provide simultaneous measurements of quantity and quality of apolipoproteins, while being antibody-independent and directly detecting peptides carrying modifications for Mox-HDLs and Mox-LDLs. Therefore, mass spectrometry is a potential and reliable alternative for apolipoprotein quantitation.
Keyphrases
- liquid chromatography
- mass spectrometry
- tandem mass spectrometry
- ultra high performance liquid chromatography
- low density lipoprotein
- high resolution mass spectrometry
- high performance liquid chromatography
- gas chromatography
- simultaneous determination
- cardiovascular disease
- solid phase extraction
- capillary electrophoresis
- high resolution
- systematic review
- binding protein
- single cell
- type diabetes
- hydrogen peroxide
- quality improvement
- liquid chromatography tandem mass spectrometry
- replacement therapy
- human health
- protein protein
- climate change
- ms ms
- coronary artery disease