{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,7,27]],"date-time":"2026-07-27T13:27:16Z","timestamp":1785158836882,"version":"3.55.0"},"reference-count":102,"publisher":"MDPI AG","issue":"17","license":[{"start":{"date-parts":[[2021,8,30]],"date-time":"2021-08-30T00:00:00Z","timestamp":1630281600000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Molecules"],"abstract":"<jats:p>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.<\/jats:p>","DOI":"10.3390\/molecules26175264","type":"journal-article","created":{"date-parts":[[2021,8,31]],"date-time":"2021-08-31T04:07:28Z","timestamp":1630382848000},"page":"5264","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":8,"title":["Mass Spectrometry for the Monitoring of Lipoprotein Oxidations by Myeloperoxidase in Cardiovascular Diseases"],"prefix":"10.3390","volume":"26","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-9555-1272","authenticated-orcid":false,"given":"Catherine","family":"Coremans","sequence":"first","affiliation":[{"name":"RD3-Pharmacognosy, Bioanalysis and Drug Discovery, Faculty of Pharmacy, Universit\u00e9 Libre de Bruxelles, 1050 Brussels, Belgium"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-7453-7028","authenticated-orcid":false,"given":"C\u00e9dric","family":"Delporte","sequence":"additional","affiliation":[{"name":"RD3-Pharmacognosy, Bioanalysis and Drug Discovery, Faculty of Pharmacy, Universit\u00e9 Libre de Bruxelles, 1050 Brussels, Belgium"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Fr\u00e9d\u00e9ric","family":"Cotton","sequence":"additional","affiliation":[{"name":"Laboratoire Hospitalier Universitaire de Bruxelles (LHUB-ULB), Department of Clinical Chemistry, Universit\u00e9 Libre de Bruxelles (ULB), 1000 Brussels, Belgium"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Phillipe","family":"Van De Borne","sequence":"additional","affiliation":[{"name":"Department of Cardiology Erasme Hospital, Universit\u00e9 Libre de Bruxelles, 1070 Brussels, Belgium"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Karim Zouaoui","family":"Boudjeltia","sequence":"additional","affiliation":[{"name":"Laboratory of Experimental Medicine (ULB 222 Unit), CHU-Charleroi, ISPPC H\u00f4pital V\u00e9sale, Universit\u00e9 Libre de Bruxelles, 6110 Montigny-Le-Tilleul, Belgium"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-4934-8863","authenticated-orcid":false,"given":"Pierre","family":"Van Antwerpen","sequence":"additional","affiliation":[{"name":"RD3-Pharmacognosy, Bioanalysis and Drug Discovery, Faculty of Pharmacy, Universit\u00e9 Libre de Bruxelles, 1050 Brussels, Belgium"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2021,8,30]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"209","DOI":"10.4331\/wjbc.v6.i3.209","article-title":"Inflammation, oxidative stress and renin angiotensin system in atherosclerosis","volume":"6","author":"Husain","year":"2015","journal-title":"World J. Biol. Chem."},{"key":"ref_2","doi-asserted-by":"crossref","first-page":"213","DOI":"10.1253\/circj.CJ-09-0706","article-title":"Inflammation in Atherosclerosis","volume":"74","author":"Libby","year":"2010","journal-title":"Circ. J."},{"key":"ref_3","doi-asserted-by":"crossref","first-page":"805","DOI":"10.1139\/o06-061","article-title":"Triggering of inflammatory response by myeloperoxidase-oxidized LDL","volume":"84","author":"Boudjeltia","year":"2006","journal-title":"Biochem. Cell Biol."},{"key":"ref_4","doi-asserted-by":"crossref","first-page":"867","DOI":"10.1002\/JLB.2A1017-407RR","article-title":"Oxidized LDL phagocytosis during foam cell formation in atherosclerotic plaques relies on a PLD2\u2013CD36 functional interdependence","volume":"103","author":"Ganesan","year":"2018","journal-title":"J. Leukoc. Biol."},{"key":"ref_5","doi-asserted-by":"crossref","first-page":"1048","DOI":"10.1021\/j100526a005","article-title":"Mechanism of the disproportionation of superoxide radicals","volume":"81","author":"Bielski","year":"1977","journal-title":"J. Phys. Chem."},{"key":"ref_6","doi-asserted-by":"crossref","first-page":"185","DOI":"10.1189\/jlb.0712349","article-title":"Myeloperoxidase: A front-line defender against phagocytosed microorganisms","volume":"93","author":"Klebanoff","year":"2013","journal-title":"J. Leukoc. Biol."},{"key":"ref_7","doi-asserted-by":"crossref","first-page":"1429","DOI":"10.1161\/01.CIR.0000012917.74432.66","article-title":"Superoxide Production and Expression of Nox Family Proteins in Human Atherosclerosis","volume":"105","author":"Sorescu","year":"2002","journal-title":"Circulation"},{"key":"ref_8","doi-asserted-by":"crossref","first-page":"208","DOI":"10.1016\/j.atherosclerosis.2014.09.001","article-title":"Vascular oxidative stress, nitric oxide and atherosclerosis","volume":"237","author":"Li","year":"2014","journal-title":"Atherosclerosis"},{"key":"ref_9","doi-asserted-by":"crossref","first-page":"20","DOI":"10.1093\/cvr\/cvs026","article-title":"Endothelial-specific Nox2 overexpression increases vascular superoxide and macrophage recruitment in ApoE(\u2212\/\u2212) mice","volume":"94","author":"Douglas","year":"2012","journal-title":"Cardiovasc. Res."},{"key":"ref_10","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/S0014-5793(00)01397-1","article-title":"A central role for the endothelial NADPH oxidase in atherosclerosis","volume":"472","author":"Meyer","year":"2000","journal-title":"FEBS Lett."},{"key":"ref_11","doi-asserted-by":"crossref","first-page":"1489","DOI":"10.1161\/CIRCRESAHA.109.215392","article-title":"Nox4 is a novel inducible source of reactive oxygen species in monocytes and macrophages and mediates oxidized low density lipoprotein-induced macrophage death","volume":"106","author":"Lee","year":"2010","journal-title":"Circ. Res."},{"key":"ref_12","doi-asserted-by":"crossref","unstructured":"Tavora, F.R., Ripple, M., Li, L., and Burke, A.P. (2009). Monocytes and neutrophils expressing myeloperoxidase occur in fibrous caps and thrombi in unstable coronary plaques. BMC Cardiovasc. Disord., 9.","DOI":"10.1186\/1471-2261-9-27"},{"key":"ref_13","doi-asserted-by":"crossref","first-page":"47","DOI":"10.1016\/j.abb.2018.01.004","article-title":"Myeloperoxidase: Its role for host defense, inflammation, and neutrophil function","volume":"640","author":"Aratani","year":"2018","journal-title":"Arch. Biochem. Biophys."},{"key":"ref_14","doi-asserted-by":"crossref","unstructured":"Khan, A.A., Alsahli, M.A., and Rahmani, A.H. (2018). Myeloperoxidase as an Active Disease Biomarker: Recent Biochemical and Pathological Perspectives. Med. Sci., 6.","DOI":"10.20944\/preprints201802.0104.v1"},{"key":"ref_15","doi-asserted-by":"crossref","first-page":"1993","DOI":"10.1016\/j.jacc.2007.02.040","article-title":"Plasma Concentrations of Myeloperoxidase Predict Mortality After Myocardial Infarction","volume":"49","author":"Mocatta","year":"2007","journal-title":"J. Am. Coll. Cardiol."},{"key":"ref_16","doi-asserted-by":"crossref","first-page":"790","DOI":"10.3109\/10715762.2015.1027197","article-title":"An immunological method to combine the measurement of active and total myeloperoxidase on the same biological fluid, and its application in finding inhibitors which interact directly with the enzyme","volume":"49","author":"Franck","year":"2015","journal-title":"Free Radic. Res."},{"key":"ref_17","doi-asserted-by":"crossref","first-page":"134","DOI":"10.1038\/nri.2017.105","article-title":"Neutrophil extracellular traps in immunity and disease","volume":"18","author":"Papayannopoulos","year":"2017","journal-title":"Nat. Rev. Immunol."},{"key":"ref_18","doi-asserted-by":"crossref","first-page":"434","DOI":"10.1016\/j.bbrc.2004.10.049","article-title":"Oxidation of low density lipoproteins by myeloperoxidase at the surface of endothelial cells: An additional mechanism to subendothelium oxidation","volume":"325","author":"Moguilevsky","year":"2004","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"ref_19","doi-asserted-by":"crossref","first-page":"144","DOI":"10.1002\/(SICI)1097-4652(199601)166:1<144::AID-JCP17>3.0.CO;2-F","article-title":"Atherogenic levels of low-density lipoprotein increase hydrogen peroxide generation in cultured human endothelial cells: Possible mechanism of heightened endocytosis","volume":"166","author":"Holland","year":"1996","journal-title":"J. Cell. Physiol."},{"key":"ref_20","doi-asserted-by":"crossref","first-page":"61","DOI":"10.1006\/abbi.1999.1226","article-title":"Myeloperoxidase-Catalyzed Oxidation of Tyrosine","volume":"367","author":"Tien","year":"1999","journal-title":"Arch. Biochem. Biophys."},{"key":"ref_21","doi-asserted-by":"crossref","first-page":"2391","DOI":"10.1002\/pro.5560071116","article-title":"Identification of tryptophan oxidation products in bovine \u03b1-crystallin","volume":"7","author":"Finley","year":"1998","journal-title":"Protein Sci."},{"key":"ref_22","doi-asserted-by":"crossref","first-page":"2075","DOI":"10.1172\/JCI119379","article-title":"3-Chlorotyrosine, a specific marker of myeloperoxidase-catalyzed oxidation, is markedly elevated in low density lipoprotein isolated from human atherosclerotic intima","volume":"99","author":"Hazen","year":"1997","journal-title":"J. Clin. Investig."},{"key":"ref_23","doi-asserted-by":"crossref","first-page":"393","DOI":"10.1038\/34923","article-title":"Formation of nitric oxide-derived inflammatory oxidants by myeloperoxidase in neutrophils","volume":"391","author":"Eiserich","year":"1998","journal-title":"Nature"},{"key":"ref_24","doi-asserted-by":"crossref","first-page":"295","DOI":"10.1016\/S0014-5793(99)00677-8","article-title":"Hypochlorite modification of high density lipoprotein: Effects on cholesterol efflux from J774 macrophages","volume":"452","author":"Bergt","year":"1999","journal-title":"FEBS Lett."},{"key":"ref_25","doi-asserted-by":"crossref","first-page":"13032","DOI":"10.1073\/pnas.0405292101","article-title":"The myeloperoxidase product hypochlorous acid oxidizes HDL in the human artery wall and impairs ABCA1-dependent cholesterol transport","volume":"101","author":"Bergt","year":"2004","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_26","doi-asserted-by":"crossref","first-page":"720","DOI":"10.1161\/01.ATV.0000054662.44688.9A","article-title":"HDL Apolipoproteins and ABCA1","volume":"23","author":"Oram","year":"2003","journal-title":"Arterioscler. Thromb. Vasc. Biol."},{"key":"ref_27","doi-asserted-by":"crossref","first-page":"149","DOI":"10.2119\/molmed.2011.00183","article-title":"The interaction of ApoA-I and ABCA1 triggers signal transduction pathways to mediate efflux of cellular lipids","volume":"18","author":"Zhao","year":"2012","journal-title":"Mol. Med."},{"key":"ref_28","doi-asserted-by":"crossref","first-page":"2063","DOI":"10.1161\/ATVBAHA.108.173815","article-title":"Apolipoprotein A-I tryptophan substitution leads to resistance to myeloperoxidase-mediated loss of function","volume":"28","author":"Peng","year":"2008","journal-title":"Arterioscler. Thromb. Vasc. Biol."},{"key":"ref_29","doi-asserted-by":"crossref","first-page":"5983","DOI":"10.1074\/jbc.M411484200","article-title":"Tyrosine 192 in apolipoprotein A-I is the major site of nitration and chlorination by myeloperoxidase, but only chlorination markedly impairs","volume":"280","author":"Shao","year":"2005","journal-title":"J. Biol. Chem."},{"key":"ref_30","doi-asserted-by":"crossref","first-page":"345","DOI":"10.1042\/bj3460345","article-title":"Reagent or Myeloperoxidase-Generated Hypochlorite Affects Discrete Regions in Lipid-Free and Lipid-Associated Human Apolipoprotein A-I","volume":"346","author":"Bergt","year":"2000","journal-title":"Biochem. J."},{"key":"ref_31","doi-asserted-by":"crossref","first-page":"2609","DOI":"10.1161\/ATVBAHA.114.304587","article-title":"The Vascular Biology Unit, Queensland Research Centre for Peripheral Vascular Disease, School of Medicine and Dentistry","volume":"34","author":"Moran","year":"2014","journal-title":"Arter. Thromb Vasc Biol"},{"key":"ref_32","doi-asserted-by":"crossref","first-page":"7856","DOI":"10.1074\/jbc.M309046200","article-title":"Lysine residues direct the chlorination of tyrosines in YXXK motifs of apolipoprotein A-I when hypochlorous acid oxidizes high density lipoprotein","volume":"279","author":"Bergt","year":"2004","journal-title":"J. Biol. Chem."},{"key":"ref_33","doi-asserted-by":"crossref","first-page":"38","DOI":"10.1074\/jbc.M407019200","article-title":"Localization of nitration and chlorination sites on apolipoprotein A-I catalyzed by myeloperoxidase in human atheroma and associated oxidative impairment in","volume":"280","author":"Zheng","year":"2005","journal-title":"J. Biol. Chem."},{"key":"ref_34","doi-asserted-by":"crossref","first-page":"9001","DOI":"10.1074\/jbc.C600011200","article-title":"Myeloperoxidase impairs ABCA1-dependent cholesterol efflux through methionine oxidation and site-specific tyrosine chlorination of apolipoprotein A-I","volume":"281","author":"Shao","year":"2006","journal-title":"J. Biol. Chem."},{"key":"ref_35","doi-asserted-by":"crossref","first-page":"193","DOI":"10.1038\/nm.3459","article-title":"An abundant dysfunctional apolipoprotein A1 in human atheroma","volume":"20","author":"Huang","year":"2014","journal-title":"Nat. Med."},{"key":"ref_36","doi-asserted-by":"crossref","first-page":"129","DOI":"10.1016\/j.ab.2010.11.039","article-title":"Optimization of apolipoprotein-B-100 sequence coverage by liquid chromatography-tandem mass spectrometry for the future study of its posttranslational modifications","volume":"411","author":"Delporte","year":"2011","journal-title":"Anal. Biochem."},{"key":"ref_37","doi-asserted-by":"crossref","first-page":"262","DOI":"10.1016\/j.eururo.2006.08.040","article-title":"Presence of LDL Modified by Myeloperoxidase in the Penis in Patients with Vascular Erectile Dysfunction: A Preliminary Study","volume":"51","author":"Roumeguere","year":"2007","journal-title":"Eur. Urol."},{"key":"ref_38","doi-asserted-by":"crossref","first-page":"1223","DOI":"10.1016\/j.bbrc.2004.08.220","article-title":"Monoclonal antibodies against LDL progressively oxidized by myeloperoxidase react with ApoB-100 protein moiety and human atherosclerotic lesions","volume":"323","author":"Moguilevsky","year":"2004","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"ref_39","doi-asserted-by":"crossref","first-page":"82","DOI":"10.1016\/S0891-5849(96)00624-7","article-title":"Oxidative modifications of apoB-100 by exposure of low density lipoproteins to HOCL in vitro","volume":"23","author":"Yang","year":"1997","journal-title":"Free Radic. Biol. Med."},{"key":"ref_40","doi-asserted-by":"crossref","first-page":"1891","DOI":"10.1016\/S0022-2275(20)31515-7","article-title":"Selective oxidation in vitro by myeloperoxidase of the N-terminal amine in apolipoprotein B-100","volume":"42","author":"Yang","year":"2001","journal-title":"J. Lipid Res."},{"key":"ref_41","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/j.abb.2008.07.026","article-title":"LDL protein nitration: Implication for LDL protein unfolding","volume":"479","author":"Hamilton","year":"2008","journal-title":"Arch. Biochem. Biophys."},{"key":"ref_42","doi-asserted-by":"crossref","first-page":"109","DOI":"10.1016\/j.ab.2010.05.005","article-title":"Mapping oxidations of apolipoprotein B-100 in human low-density lipoprotein by liquid chromatography\u2013tandem mass spectrometry","volume":"404","author":"Chakraborty","year":"2010","journal-title":"Anal. Biochem."},{"key":"ref_43","doi-asserted-by":"crossref","first-page":"747","DOI":"10.1194\/jlr.M047449","article-title":"Impact of myeloperoxidase-LDL interactions on enzyme activity and subsequent posttranslational oxidative modifications of apoB-100","volume":"55","author":"Delporte","year":"2014","journal-title":"J. Lipid Res."},{"key":"ref_44","doi-asserted-by":"crossref","first-page":"2132","DOI":"10.1002\/pmic.200700111","article-title":"Analysis of modified apolipoprotein B-100 structures formed in oxidized low-density lipoprotein using LC-MS\/MS","volume":"7","author":"Obama","year":"2007","journal-title":"Proteomics"},{"key":"ref_45","doi-asserted-by":"crossref","first-page":"2999","DOI":"10.1093\/eurheartj\/ehw272","article-title":"2016 ESC\/EAS Guidelines for the Management of Dyslipidaemias","volume":"37","author":"Catapano","year":"2016","journal-title":"Eur. Heart J."},{"key":"ref_46","doi-asserted-by":"crossref","first-page":"85","DOI":"10.7326\/0003-4819-90-1-85","article-title":"Cholesterol in the prediction of atherosclerotic disease. New perspectives based on the Framingham study","volume":"90","author":"Kannel","year":"1979","journal-title":"Ann. Intern. Med."},{"key":"ref_47","doi-asserted-by":"crossref","first-page":"S49","DOI":"10.1161\/01.cir.0000437741.48606.98","article-title":"2013 ACC\/AHA Guideline on the Assessment of Cardiovascular Risk","volume":"129","author":"Goff","year":"2014","journal-title":"Circulation"},{"key":"ref_48","doi-asserted-by":"crossref","first-page":"NP1","DOI":"10.1177\/2047487316653709","article-title":"2016 European Guidelines on cardiovascular disease prevention in clinical practice","volume":"23","author":"Piepoli","year":"2016","journal-title":"Eur. J. Prev. Cardiol."},{"key":"ref_49","doi-asserted-by":"crossref","first-page":"111","DOI":"10.1093\/eurheartj\/ehz455","article-title":"2019 ESC\/EAS Guidelines for the management of dyslipidaemias: Lipid modification to reduce cardiovascular risk","volume":"41","author":"Mach","year":"2020","journal-title":"Eur. Heart J."},{"key":"ref_50","doi-asserted-by":"crossref","first-page":"1289","DOI":"10.1001\/jama.2016.13985","article-title":"Association between lowering LDL-C and cardiovascular risk reduction among different therapeutic interventions: A systematic review and meta-analysis","volume":"316","author":"Silverman","year":"2016","journal-title":"JAMA J. Am. Med. Assoc."},{"key":"ref_51","doi-asserted-by":"crossref","first-page":"2313","DOI":"10.1093\/eurheartj\/ehz962","article-title":"Low-density lipoproteins cause atherosclerotic cardiovascular disease: Pathophysiological, genetic, and therapeutic insights: A consensus statement from the European Atherosclerosis Society Consensus Panel","volume":"41","author":"Krauss","year":"2020","journal-title":"Eur. Heart J."},{"key":"ref_52","first-page":"2499","article-title":"Lipid-related markers and cardiovascular disease prediction","volume":"307","author":"Gao","year":"2012","journal-title":"JAMA J. Am. Med. Assoc."},{"key":"ref_53","doi-asserted-by":"crossref","first-page":"1933","DOI":"10.1056\/NEJMoa1609581","article-title":"Evacetrapib and Cardiovascular Outcomes in High-Risk Vascular Disease","volume":"376","author":"Lincoff","year":"2017","journal-title":"N. Engl. J. Med."},{"key":"ref_54","doi-asserted-by":"crossref","first-page":"539","DOI":"10.1093\/eurheartj\/eht571","article-title":"Mendelian randomization of blood lipids for coronary heart disease","volume":"36","author":"Holmes","year":"2015","journal-title":"Eur. Heart J."},{"key":"ref_55","unstructured":"Carbonneil, C., Benedittini, D., Cecchin, M., Lascols, S., and Tuil, L.A. (2019, April 07). Place des Dosages des Apolipoproteines a1 et b Dans le Bilan Lipidique. Available online: https:\/\/www.has-sante.fr\/portail\/upload\/docs\/application\/pdf\/2008-12\/texte_court_apolipoa1b.pdf."},{"key":"ref_56","doi-asserted-by":"crossref","first-page":"1065","DOI":"10.1016\/j.jacl.2017.05.005","article-title":"Evaluating the atherogenic burden of individuals with a Friedewald-estimated low-density lipoprotein cholesterol <70 mg\/dL compared with a novel low-density lipoprotein estimation method","volume":"11","author":"Whelton","year":"2017","journal-title":"J. Clin. Lipidol."},{"key":"ref_57","first-page":"593","article-title":"\u00c9valuation d\u2019une m\u00e9thode de dosage direct du LDL-cholest\u00e9rol et de son impact potentiel en termes de prise en charge th\u00e9rapeutique","volume":"72","author":"Reignier","year":"2014","journal-title":"Ann. Biol. Clin."},{"key":"ref_58","doi-asserted-by":"crossref","first-page":"51","DOI":"10.1007\/978-1-4939-2742-5_5","article-title":"Indirect ELISA","volume":"1318","author":"Lin","year":"2015","journal-title":"Methods Mol. Biol."},{"key":"ref_59","doi-asserted-by":"crossref","first-page":"1006","DOI":"10.1373\/clinchem.2018.287037","article-title":"Quantifying Atherogenic Lipoproteins: Current and Future Challenges in the Era of Personalized Medicine and Very Low Concentrations of LDL Cholesterol. A Consensus Statement from EAS and EFLM","volume":"64","author":"Langlois","year":"2018","journal-title":"Clin. Chem."},{"key":"ref_60","doi-asserted-by":"crossref","first-page":"804","DOI":"10.1016\/j.amjcard.2016.06.048","article-title":"Low-Density Lipoprotein Cholesterol, Non\u2013High-Density Lipoprotein Cholesterol, Triglycerides, and Apolipoprotein B and Cardiovascular Risk in Patients With Manifest Arterial Disease","volume":"118","author":"Visseren","year":"2016","journal-title":"Am. J. Cardiol."},{"key":"ref_61","doi-asserted-by":"crossref","first-page":"444","DOI":"10.1016\/j.atherosclerosis.2012.08.039","article-title":"Discordance analysis of Apolipoprotein B and non-high density lipoprotein cholesterol as markers of cardiovascular risk in the INTERHEART study","volume":"225","author":"Sniderman","year":"2012","journal-title":"Atherosclerosis"},{"key":"ref_62","doi-asserted-by":"crossref","first-page":"24","DOI":"10.1373\/clinchem.2007.097360","article-title":"Inflammation in Atherosclerosis: From Vascular Biology to Biomarker Discovery and Risk Prediction","volume":"54","author":"Packard","year":"2007","journal-title":"Clin. Chem."},{"key":"ref_63","doi-asserted-by":"crossref","first-page":"169","DOI":"10.1016\/j.atherosclerosis.2018.11.001","article-title":"ApoB in clinical care: Pro and Con","volume":"282","author":"Sniderman","year":"2019","journal-title":"Atherosclerosis"},{"key":"ref_64","doi-asserted-by":"crossref","first-page":"483","DOI":"10.1016\/j.redox.2013.07.006","article-title":"Biological markers of oxidative stress: Applications to cardiovascular research and practice","volume":"1","author":"Ho","year":"2013","journal-title":"Redox Biol."},{"key":"ref_65","doi-asserted-by":"crossref","first-page":"70","DOI":"10.3109\/10408363.2014.992063","article-title":"Oxidized low-density lipoprotein as a biomarker of cardiovascular diseases","volume":"52","author":"Trpkovic","year":"2015","journal-title":"Crit. Rev. Clin. Lab. Sci."},{"key":"ref_66","doi-asserted-by":"crossref","first-page":"1337","DOI":"10.1161\/CIRCRESAHA.107.151704","article-title":"Low density lipoprotein undergoes oxidation within lysosomes in cells","volume":"100","author":"Wen","year":"2007","journal-title":"Circ. Res."},{"key":"ref_67","doi-asserted-by":"crossref","first-page":"39","DOI":"10.1089\/ars.2009.2733","article-title":"Oxidized LDL: Diversity, Patterns of Recognition, and Pathophysiology","volume":"13","author":"Levitan","year":"2010","journal-title":"Antioxid. Redox Signal."},{"key":"ref_68","doi-asserted-by":"crossref","first-page":"2253","DOI":"10.1172\/JCI115261","article-title":"Minimally modified low density lipoprotein is biologically active in vivo in mice","volume":"87","author":"Liao","year":"1991","journal-title":"J. Clin. Investig."},{"key":"ref_69","doi-asserted-by":"crossref","first-page":"973","DOI":"10.1016\/j.jacc.2006.03.057","article-title":"Is Plasma Oxidized Low-Density Lipoprotein, Measured With the Widely Used Antibody 4E6, an Independent Predictor of Coronary Heart Disease Among U.S. Men and Women?","volume":"48","author":"Wu","year":"2006","journal-title":"J. Am. Coll. Cardiol."},{"key":"ref_70","first-page":"750742","article-title":"Myeloperoxidase-dependent LDL modifications in bloodstream are mainly predicted by angiotensin II, adiponectin, and myeloperoxidase activity: A cross-sectional study in men","volume":"2013","author":"Boudjeltia","year":"2013","journal-title":"Mediators Inflamm."},{"key":"ref_71","doi-asserted-by":"crossref","unstructured":"Huang, J., Yancey, P.G., Tao, H., Borja, M.S., Smith, L.E., Kon, V., Davies, S.S., and Linton, M.F. (2020). Reactive dicarbonyl scavenging effectively reduces mpo-mediated oxidation of hdl and restores pon1 activity. Nutrients, 12.","DOI":"10.3390\/nu12071937"},{"key":"ref_72","doi-asserted-by":"crossref","first-page":"1245","DOI":"10.1159\/000494579","article-title":"Entire Peroxidation Reaction System of Myeloperoxidase Correlates with Progressive Low-Density Lipoprotein Modifications via Reactive Aldehydes in Atherosclerotic Patients with Hypertension","volume":"50","author":"Liu","year":"2018","journal-title":"Cell. Physiol. Biochem."},{"key":"ref_73","doi-asserted-by":"crossref","first-page":"393","DOI":"10.4172\/2155-9899.1000393","article-title":"Role of Serum Biomarkers in Early Detection of Non-Alcoholic Steatohepatitis and Fibrosis in West Virginian Children","volume":"7","author":"Sodhi","year":"2016","journal-title":"J. Clin. Cell. Immunol."},{"key":"ref_74","doi-asserted-by":"crossref","first-page":"33775","DOI":"10.1074\/jbc.M504092200","article-title":"Tyrosine Modification Is Not Required for Myeloperoxidase-induced Loss of Apolipoprotein A-I Functional Activities","volume":"280","author":"Peng","year":"2005","journal-title":"J. Biol. Chem."},{"key":"ref_75","first-page":"391","article-title":"Evaluation of the Cholestech LDX desktop analyser for cholesterol, HDL-cholesterol, and triacylglycerols in heparinized venous blood","volume":"32","author":"Cobbaert","year":"1994","journal-title":"Clin. Chem. Lab. Med."},{"key":"ref_76","first-page":"1809","article-title":"Evolution of Methods for Measurement of HDL-Cholesterol: From Ultracentrifugation to Homogeneous Assays","volume":"43","author":"Warnick","year":"2001","journal-title":"Clin. Chem."},{"key":"ref_77","doi-asserted-by":"crossref","first-page":"310","DOI":"10.1016\/0009-9120(94)90035-3","article-title":"Immunoturbidimetry of serum apolipoproteins A-I and B on the Cobas Bio centrifugal analyzer: Method validation and reference values","volume":"27","author":"Eugui","year":"1994","journal-title":"Clin. Biochem."},{"key":"ref_78","doi-asserted-by":"crossref","unstructured":"Cobbaert, C., Zwang, L., Ceriotti, F., Modenese, A., Cremer, P., Herrmann, W., Hoss, G., Jarausch, J., T\u00fc, R., and M\u00e4, W. (2019, January 08). Reference Standardization and Triglyceride Interference of a New Homogeneous HDL-Cholesterol Assay Compared with a Former Chemical Precipitation Assay Lipids and Lipoproteins. Available online: http:\/\/clinchem.aaccjnls.org\/content\/clinchem\/44\/4\/779.full.pdf.","DOI":"10.1093\/clinchem\/44.4.779"},{"key":"ref_79","doi-asserted-by":"crossref","unstructured":"Nauck, M., Graziani, M.S., Bruton, D., Cobbaert, C., Cole, T.G., Lefevre, F., Riesen, W., Bachorik, P.S., and Rifai, N. (2019, January 08). Analytical and Clinical Performance of a Detergent-based Homogeneous LDL-Cholesterol Assay: A Multicenter Evaluation. Available online: http:\/\/clinchem.aaccjnls.org\/content\/clinchem\/46\/4\/506.full.pdf.","DOI":"10.1093\/clinchem\/46.4.506"},{"key":"ref_80","doi-asserted-by":"crossref","first-page":"1641","DOI":"10.1093\/clinchem\/44.8.1641","article-title":"Apolipoprotein B and A-I values in 147576 Swedish males and females, standardized according to the World Health Organization-International Federation of Clinical Chemistry First International Reference Materials","volume":"44","author":"Jungner","year":"1998","journal-title":"Clin. Chem."},{"key":"ref_81","doi-asserted-by":"crossref","first-page":"3","DOI":"10.1016\/j.jim.2009.06.003","article-title":"The fundamental flaws of immunoassays and potential solutions using tandem mass spectrometry","volume":"347","author":"Hoofnagle","year":"2009","journal-title":"J. Immunol. Methods"},{"key":"ref_82","doi-asserted-by":"crossref","first-page":"1683","DOI":"10.1002\/pmic.200800562","article-title":"The detection, correlation, and comparison of peptide precursor and product ions from data independent LC-MS with data dependant LC-MS\/MS","volume":"9","author":"Geromanos","year":"2009","journal-title":"Proteomics"},{"key":"ref_83","doi-asserted-by":"crossref","unstructured":"Rogier, E., Plucinski, M., Lucchi, N., Mace, K., Chang, M., Lemoine, J.F., Candrinho, B., Colborn, J., Dimbu, R., and Fortes, F. (2017). Bead-based immunoassay allows sub-picogram detection of histidine-rich protein 2 from Plasmodium falciparum and estimates reliability of malaria rapid diagnostic tests. PLoS ONE, 12.","DOI":"10.1371\/journal.pone.0172139"},{"key":"ref_84","doi-asserted-by":"crossref","first-page":"3151","DOI":"10.1007\/s00216-019-01787-1","article-title":"Picogram per liter quantification of pyrethroid and organophosphate insecticides in surface waters: A result of large enrichment with liquid-liquid extraction and gas chromatography coupled to mass spectrometry using atmospheric pressure chemical ionization","volume":"411","author":"Beck","year":"2019","journal-title":"Anal. Bioanal. Chem."},{"key":"ref_85","doi-asserted-by":"crossref","first-page":"120304","DOI":"10.1016\/j.talanta.2019.120304","article-title":"Automation of mass spectrometric detection of analytes and related workflows: A review","volume":"208","author":"Elpa","year":"2019","journal-title":"Talanta"},{"key":"ref_86","doi-asserted-by":"crossref","first-page":"1700107","DOI":"10.1002\/prca.201700107","article-title":"Comparison of Targeted Mass Spectrometry Techniques with an Immunoassay: A Case Study for HSP90\u03b1","volume":"12","author":"Govorukhina","year":"2018","journal-title":"PROTEOMICS-Clin. Appl."},{"key":"ref_87","doi-asserted-by":"crossref","first-page":"636","DOI":"10.1021\/jasms.0c00379","article-title":"The Time Has Come for Quantitative Protein Mass Spectrometry Tests That Target Unmet Clinical Needs","volume":"32","author":"Smit","year":"2021","journal-title":"J. Am. Soc. Mass Spectrom."},{"key":"ref_88","unstructured":"Fda (2021, August 05). Cder Bioanalytical Method Validation Guidance for Industry Biopharmaceutics Bioanalytical Method Validation Guidance for Industry Biopharmaceutics Contains Nonbinding Recommendations, Available online: http:\/\/www.fda.gov\/Drugs\/GuidanceComplianceRegulatoryInformation\/Guidances\/default.htmand\/orhttp:\/\/www.fda.gov\/AnimalVeterinary\/GuidanceComplianceEnforcement\/GuidanceforIndustry\/default.htm."},{"key":"ref_89","doi-asserted-by":"crossref","first-page":"74","DOI":"10.1016\/j.ymeth.2015.03.001","article-title":"Quantification of serum apolipoproteins A-I and B-100 in clinical samples using an automated SISCAPA-MALDI-TOF-MS workflow","volume":"81","author":"Nouta","year":"2015","journal-title":"Methods"},{"key":"ref_90","doi-asserted-by":"crossref","first-page":"629","DOI":"10.4155\/bio-2019-0032","article-title":"Protein quantification by LC-MS: A decade of progress through the pages of Bioanalysis","volume":"11","year":"2019","journal-title":"Bioanalysis"},{"key":"ref_91","doi-asserted-by":"crossref","first-page":"32","DOI":"10.1016\/j.microc.2012.02.011","article-title":"Mass Spectrometry-Based Multiplexing for the Analysis of Biomarkers in Drug Development and Clinical Diagnostics- How Much is too Much?","volume":"105","author":"Christians","year":"2012","journal-title":"Microchem. J."},{"key":"ref_92","doi-asserted-by":"crossref","first-page":"143","DOI":"10.1016\/j.jprot.2014.06.015","article-title":"Metrological traceability in mass spectrometry-based targeted protein quantitation: A proof-of-principle study for serum apolipoproteins A-I and B100","volume":"109","author":"Smit","year":"2014","journal-title":"J. Proteom."},{"key":"ref_93","doi-asserted-by":"crossref","first-page":"378","DOI":"10.3390\/biom5020378","article-title":"Mass Spectrometry-Based Methods for Identifying Oxidized Proteins in Disease: Advances and Challenges","volume":"5","author":"Verrastro","year":"2015","journal-title":"Biomolecules"},{"key":"ref_94","doi-asserted-by":"crossref","first-page":"155","DOI":"10.1016\/j.jpba.2016.02.011","article-title":"The pros and cons of increased trypsin-to-protein ratio in targeted protein analysis","volume":"123","author":"Egeland","year":"2016","journal-title":"J. Pharm. Biomed. Anal."},{"key":"ref_95","doi-asserted-by":"crossref","first-page":"7636","DOI":"10.1021\/acs.analchem.5b00866","article-title":"Insight into Trypsin Miscleavage: Comparison of Kinetic Constants of Problematic Peptide Sequences","volume":"87","author":"Gilar","year":"2015","journal-title":"Anal. Chem."},{"key":"ref_96","doi-asserted-by":"crossref","first-page":"3575","DOI":"10.1021\/ac5001477","article-title":"Effects of calibration approaches on the accuracy for LC-MS targeted quantification of therapeutic protein","volume":"86","author":"Zhang","year":"2014","journal-title":"Anal. Chem."},{"key":"ref_97","first-page":"418","article-title":"Noise and baseline filtration in mass spectrometry","volume":"Volume 9044","author":"Urban","year":"2015","journal-title":"Proceedings of the International Work-Conference on Bioinformatics and Biomedical Engineering, IWBBIO 2015"},{"key":"ref_98","first-page":"188","article-title":"Automated Multiplex LC-MS\/MS Assay for Quantifying Serum Apolipoproteins A-I, B, C-I, C-II, C-III, and E with Qualitative Apolipoprotein E Phenotyping","volume":"62","author":"Romijn","year":"2015","journal-title":"Clin. Chem."},{"key":"ref_99","doi-asserted-by":"crossref","first-page":"919","DOI":"10.1515\/cclm-2012-0723","article-title":"Quantitative Clinical Chemistry Proteomics (qCCP) using mass spectrometry: General characteristics and application","volume":"51","author":"Lehmann","year":"2013","journal-title":"Clin. Chem. Lab. Med."},{"key":"ref_100","doi-asserted-by":"crossref","first-page":"794","DOI":"10.1002\/prca.201300034","article-title":"Quantification of seven apolipoproteins in human plasma by proteotypic peptides using fast LC-MS\/MS","volume":"7","author":"Ceglarek","year":"2013","journal-title":"Proteom. Clin. Appl."},{"key":"ref_101","doi-asserted-by":"crossref","first-page":"2585","DOI":"10.1002\/rcm.3130","article-title":"The application of ultra-performance liquid chromatography\/tandem mass spectrometry to the detection and quantitation of apolipoproteins in human serum","volume":"21","author":"Kay","year":"2007","journal-title":"Rapid Commun. Mass Spectrom."},{"key":"ref_102","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/S0009-8981(00)00187-X","article-title":"Distribution of serum apolipoproteins A-I and B and lipoprotein(a) in European elderly: The SENECA study","volume":"295","author":"Contois","year":"2000","journal-title":"Clin. Chim. Acta"}],"container-title":["Molecules"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.mdpi.com\/1420-3049\/26\/17\/5264\/pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2025,10,11]],"date-time":"2025-10-11T06:55:55Z","timestamp":1760165755000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.mdpi.com\/1420-3049\/26\/17\/5264"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2021,8,30]]},"references-count":102,"journal-issue":{"issue":"17","published-online":{"date-parts":[[2021,9]]}},"alternative-id":["molecules26175264"],"URL":"https:\/\/doi.org\/10.3390\/molecules26175264","relation":{},"ISSN":["1420-3049"],"issn-type":[{"value":"1420-3049","type":"electronic"}],"subject":[],"published":{"date-parts":[[2021,8,30]]}}}