Refine your search
Collections
Co-Authors
Journals
A B C D E F G H I J K L M N O P Q R S T U V W X Y Z All
Venkataraman, Krishnan
- Oxidized Lipoproteins as the Diagnostic Target for Cardiovascular Diseases
Abstract Views :224 |
PDF Views:86
Authors
Affiliations
1 Pushpagiri Research Centre, Pushpagiri Institute of Medical Sciences and Research Centre, Thiruvalla 689 101, IN
2 The CHILDS Trust Medical Research Foundation, Chennai 600 034, IN
3 Centre for Bio-separation Technology, VIT University, Vellore 632 014, IN
1 Pushpagiri Research Centre, Pushpagiri Institute of Medical Sciences and Research Centre, Thiruvalla 689 101, IN
2 The CHILDS Trust Medical Research Foundation, Chennai 600 034, IN
3 Centre for Bio-separation Technology, VIT University, Vellore 632 014, IN
Source
Current Science, Vol 115, No 7 (2018), Pagination: 1276-1286Abstract
Low HDL-cholesterol and high LDL-cholesterol in plasma have long been associated with cardiovascular disease (CVD) risk. The quantity of cholesterol associated with these lipoproteins is being traditionally used to predict CVD risk. However, recent studies have suggested that the quality and functionality of these lipoproteins are more important. The lipoproteins - HDL and LDL - undergo both enzymatic and non-enzymatic modifications which impair their functional capability and hence, test of such modification which reflects the quality of HDL can be a good predictor of CVD risk. The present article discusses oxidation- associated dysfunctionality of lipoproteins and their potential in laboratory diagnosis of CVD.Keywords
Cardiovascular Disease, Cholesterol, Diagnostic Target, Oxidized Lipoproteins.References
- Benjamin, E. J. et al., American heart association statistics committee and stroke statistics subcommittee. Heart disease and stroke statistics - 2017 update: a report from the American Heart Association. Circulation, 2017, 135(10), e146-e603; doi: 10.1161/CIR.0000000000000485.
- Fuster, V. and Kelly, B. B. (eds), Institute of Medicine (US) Committee on Preventing the Global Epidemic of Cardiovascular Disease: Meeting the Challenges in Developing Countries, Promoting Cardiovascular Health in the Developing World: a Critical Challenge to Achieve Global Health, National Academic Press (US), Washington, DC, 2010.
- Gupta, R., Mohan, I. and Narula, J., Trends in coronary heart disease epidemiology in India. Ann. Glob. Health, 2016, 82(2), 307315; doi:10.1016/j.aogh.2016.04.002. Review. PubMed PMID: 27372534.
- Gupta, R., Guptha, S., Sharma, K. K., Gupta, A. and Deedwania, P., Regional variations in cardiovascular risk factors in India: India heart watch. World J. Cardiol., 2012, 4(4), 112-120; doi:10.4330/wjc.v4.i4.112.
- Folsom, A. R., Classical and novel biomarkers for cardiovascular risk prediction in the United States. J. Epidemiol., 2013, 23(3), 158-162; doi:10.2188/jea.JE20120157.
- Paynter, N. P., Everett, B. M. and Cook, N. R., Cardiovascular disease risk prediction in women: is there a role for novel biomarkers? Clin. Chem., 2014, 60(1), 88-97; doi: 10.1373/clinchem.2013.202796. Review. PubMed PMID: 24100805; PubMed Central PMCID: PMC3877731.
- Fisher, W. R., The structure of the lower-density lipoproteins of human plasma: newer concepts derived from studies with the analytical ultracentrifuge. Ann. Clin. Lab. Sci., 1972, 2, 198-208.
- Brown, M. S., Kovanen, P. T. and Goldstein, J. L., Regulation of plasma cholesterol by lipoprotein receptors. Science, 1981, 212, 628-635.
- Hegele, R. A., Plasma lipoproteins: genetic influences and clinical implications. Nature Rev. Genet., 2009, 10, 109-121.
- Ben, J., Zhu, X., Zhang, H. and Chen, Q., Class A1 scavenger receptors in cardiovascular diseases. Br. J. Pharmacol., 2015, 172(23), 5523-5530; doi:10.1111/bph.13105.
- Witztum, J. L. and Steinberg, D., Role of oxidized low density lipoprotein in atherogenesis. J. Clin. Invest., 1991, 88(6), 1785-1792. Review. PubMed PMID: 1752940; PubMed Central PMCID: PMC295745.
- Castelao, J. E. and Gago-Dominguez, M., Risk factors for cardiovascular disease in women: relationship to lipid peroxidation and oxidative stress. Med. Hypotheses, 2008, 71(1), 39-44.
- Parthasarathy, S., Raghavamenon, A., Garelnabi, M. O. and Santanam, N., Oxidized low-density lipoprotein. Methods Mol. Biol., 201, 610, 403-417; doi:10.1007/978-1-60327-029-8_24.
- Noguchi, N., Novel insights into the molecular mechanisms of the antiatherosclerotic properties of antioxidants: the alternatives to radical scavenging. Free Radic. Biol. Med., 2002, 33(11), 1480-1489. Review. PubMed PMID: 12446205.
- Yoshida, H. and Kisugi, R., Mechanisms of LDL oxidation. Clin. Chim. Acta, 2010, 411(23-24), 875-882; doi:10.1016/j.cca.2010.08.038. Review. PubMed PMID: 20816951.
- Malle, E., Marsche, G., Arnhold, J. and Davies, M. J., Modification of low-density lipoprotein by myeloperoxidase-derived oxidants and reagent hypochlorous acid. Biochim. Biophys. Acta, 2006, 1761(4), 392-415. PubMed PMID: 16698314.
- Delporte, C. et al., Impact of myeloperoxidase-LDL interactions on enzyme activity and subsequent posttranslational oxidative modifications of apoB-100. J. Lipid Res., 2014, 55(4), 747-757; doi:10.1194/jlr.M047449. PubMed PMID: 24534704.
- Reaven, P. D. and Witztum, J. L., Oxidized low density lipoproteins in atherogenesis: role of dietary modification. Annu. Rev. Nutr., 1996, 16, 51-71. Review. PubMed PMID: 8839919.
- Miller, Y. I., Choi, S. H., Fang, L. and Tsimikas, S., Lipoprotein modification and macrophage uptake: role of pathologic cholesterol transport in atherogenesis. Subcell. Biochem., 2010, 51, 229-251; doi: 10.1007/978-90-481-8622-8_8. Review. PubMed PMID: 20213546.
- Hoff, H. F., Zyromski, N., Armstrong, D. and O’Neil, J., Aggregation as well as chemical modification of LDL during oxidation is responsible for poor processing in macrophages. J. Lipid Res., 1993, 34(11), 1919-1929. PubMed PMID: 8263416.
- Delporte, C., Van Antwerpen, P., Vanhamme, L., Roumeguere, T. and Zouaoui Boudjeltia, K., Low-density lipoprotein modified by myeloperoxidase in inflammatory pathways and clinical studies. Mediat. Inflamm, 2013, 2013, 971579; doi:10.1155/2013/971579. Review. PubMed PMID: 23983406; PubMed Central PMCID: PMC3742028.
- Oram, J. F. and Heinecke, J. W., ATP-binding cassette transporter A1: a cell cholesterol exporter that protects against cardiovascular disease. Physiol. Rev., 2005, 85, 1343-1372.
- Navab, M., Hama, S. Y., Hough, G. P., Subbanagounder, G., Reddy, S. T. and Fogelman, A. M., A cell-free assay for detecting HDL that is dysfunctional in preventing the formation of or inactivating oxidized phospholipids. J. Lipid Res., 2001, 42(8), 1308-1317.
- Vaziri, N. D., Moradi, H., Pahl, M. V., Fogelman, A. M. and Navab, M., In vitro stimulation of HDL anti-inflammatory activity and inhibition of LDL pro-inflammatory activity in the plasma of patients with end-stage renal disease by an ApoA-1 mimetic peptide. Kidney Int., 2009, 76(4), 437-444; doi:10.1038/ki.2009.177.
- Florentin, M., Liberopoulos, E. N., Wierzbicki, A. S. and Mikhailidis, D. P., Multiple actions of high-density lipoprotein. Curr. Opin. Cardiol., 2008, 23(4), 370-378; doi: 10.1097/HC0.0b013e3283043806. Review. PubMed PMID: 18520722.
- Hao, W. and Friedman, A., The LDL-HDL profile determines the risk of atherosclerosis: a mathematical model. PLoS ONE, 2014, 9(3), e90497; doi:10.1371/journal.pone.0090497. PubMed PMID: 24621857.
- Ferretti, G., Bacchetti, T., Negre-Salvayre, A., Salvayre, R., Dousset, N. and Curatola, G., Structural modifications of HDL and functional consequences. Atherosclerosis, 2006, 184, 1-7. PubMed PMID: 16157342.
- Francis, G. A., High density lipoprotein oxidation: in vitro susceptibility and potential in vivo consequences. Biochim. Biophys. Acta, 2000, 1483, 217-235. PubMed PMID: 10634938.
- Heinecke, J. W., Rosen, H. and Chait, A., Iron and copper promote modification of low density lipoprotein by human arterial smooth muscle cells in culture. J. Clin. Invest., 1984, 74(5), 1890-1894.
- Lamb, D. J., Mitchinson, M. J. and Leake, D. S., Transition metal ions within human atherosclerotic lesions can catalyse the oxidation of low density lipoprotein by macrophages. FEBS Lett., 1995, 374(1), 12-16. PubMed PMID: 7589497.
- Arai, H., Berlett, B. S., Chock, P. B. and Stadtman, E. R., Effect of bicarbonate on iron-mediated oxidation of low-density lipoprotein. Proc. Natl. Acad. Sci. USA, 2005, 102(30), 10472-10477. PubMed PMID: 16027354; PubMed Central PMCID: PMC1176232.
- Morgan, J. and Leake, D. S., Oxidation of low density lipoprotein by iron or copper at acidic pH. J. Lipid Res., 1995, 36(12), 2504-2512. PubMed PMID: 8847477.
- Leake, D. S., Does an acidic pH explain why low density lipoprotein is oxidised in atherosclerotic lesions? Atherosclerosis, 1997, 129(2), 149-157. Review. PubMed PMID: 9105556.
- Yoshida, H. and Kisugi, R., Mechanisms of LDL oxidation. Clin. Chim. Acta, 2010, 411(23-24), 1875-1882; doi:10.1016/j.cca.2010.08.038. PubMed PMID: 20816951.
- Boullier, A. et al., Minimally oxidized LDL offsets the apoptotic effects of extensively oxidized LDL and free cholesterol in macrophages. Arterioscler. Thromb. Vasc. Biol., 2006, 26(5), 1169-1176. PubMed PMID: 16484596.
- Yamamoto, S., Mammalian lipoxygenases: molecular structures and functions. Biochim. Biophys. Acta, 1992, 1128(2-3), 117-131. PubMed PMID: 1420284.
- Parthasarathy, S., Wieland, E. and Steinberg, D., A role for endothelial cell lipoxygenase in the oxidative modification of low density lipoprotein. Proc. Natl. Acad. Sci. USA, 1989, 86, 1046-1050.
- Huo, Y. et al., Critical role of macrophage 12/15-lipoxygenase for atherosclerosis in apolipoprotein E-deficient mice. Circulation, 2004, 110(14), 2024-2031. PubMed PMID: 15451785.
- Kuhn, H., Romisch, I. and Belkner, J., The role of lipoxygenaseisoforms in atherogenesis. Mol. Nutr. Food Res., 2005, 49(11), 1014-1029. PubMed PMID: 16270276.
- Shen, J. et al., Macrophage-mediated 15-lipoxygenase expression protects against atherosclerosis development. J. Clin. Invest., 1996, 98(10), 2201-2208.
- Shen, J., Kuhn, H., Petho-Schramm, A. and Chan, L., Transgenic rabbits with the integrated human 15-lipoxygenase gene driven by a lysozyme promoter: macrophage-specific expression and variable positional specificity of the transgenic enzyme. FASEB J., 1995, 9(15), 1623-1631. PubMed PMID: 8529842.]
- Merched, A. J., Ko, K., Gotlinger, K. H., Serhan, C. N. and Chan, L., Atherosclerosis: evidence for impairment of resolution of vascular inflammation governed by specific lipid mediators. FASEB J., 2008, 22(10), 3595-3606; doi:10.1096/fj.08-112201.
- George, J. et al., 12/15-Lipoxygenase gene disruption attenuates atherogenesis in LDL receptor-deficient mice. Circulation, 2001, 104(14), 1646-1650. PubMed PMID: 11581143.
- Cyrus, T. et al., Absence of 12/15-lipoxygenase expression decreases lipid peroxidation and atherogenesis in apolipoprotein e-deficient mice. Circulation, 2001, 103(18), 2277-2282. PubMed PMID: 11342477.
- Sukhanov, S. et al., Insulin-like growth factor I reduces lipid oxidation and foam cell formation via downregulation of 12/15lipoxygenase. Atherosclerosis, 2015, 238(2), 313-320; doi: 10.1016/j.atherosclerosis.2014.12.024.
- Wuest, S. J., Crucet, M., Gemperle, C., Loretz, C. and Hersberger, M. Expression and regulation of 12/15-lipoxygenases in human primary macrophages. Atherosclerosis, 2015, 225(1), 121-127; doi:10.1016/j.atherosclerosis.2012. 07.022.
- Schindhelm, R. K., van der Zwan, L. P., Teerlink, T. and Scheffer, P. G., Myeloperoxidase: a useful biomarker for cardiovascular disease risk stratification? Clin. Chem., 2009, 55, 1462-1470; doi: 10.1373/clinchem.2009.126029. Review. PubMed PMID: 19556446.
- Meuwese, M. C. et al., Serum myeloperoxidase levels are associated with the future risk of coronary artery disease in apparently healthy individuals: the EPIC-Norfolk prospective population study. J. Am. Coll. Cardiol., 2007, 50(2), 159-165. PubMed PMID: 17616301.
- Baldus, S. et al., Myeloperoxidase serum levels predict risk in patients with acute coronary syndromes. Circulation, 2003, 108(12), 1440-1445. PubMed PMID: 12952835.
- Carr, A. C., Myzak, M. C., Stocker, R., McCall, M. R. and Frei, B., Myeloperoxidase binds to low-density lipoprotein: potential implications for atherosclerosis. FEBS Lett., 2000, 487, 176-180.
- Carr, A. C., McCall, M. R. and Frei, B., Oxidation of LDL by myeloperoxidase and reactive nitrogen species: reaction pathways and antioxidant protection. Arterioscler. Thromb. Vasc. Biol., 2000, 20, 1716-1723.
- Chakraborty, S., Cai, Y. and Tarr, M. A., In vitro oxidative foot printing provides insight into apolipoprotein B-100 structure in low-density lipoprotein. Proteomics, 2014, 14(21-22), 2614-2622; doi:10.1002/pmic.201300174. PubMed PMID: 25176030.
- Vicca, S. et al., New insights into the effects of the protein moiety of oxidized LDL (oxLDL). Kidney Int. Suppl., 2003, 84, S125-S127. Review. PubMed PMID: 12694326.
- Heinecke, J. W., Mass spectrometric quantification of amino acid oxidation products in proteins: insights into pathways that promote LDL oxidation in the human artery wall. FASEB J., 1999, 13(10), 1113-1120. Review. PubMed PMID: 10385603.
- Hazen, S. L. and Heinecke, J. W., 3-Chlorotyrosine, a specific marker of myeloperoxidase-catalyzed oxidation, is markedly elevated in low density lipoprotein isolated from human atherosclerotic intima. J. Clin. Invest., 1997, 99, 2075-2081.
- Malle, E., Marsche, G., Arnhold, J. and Davies, M. J., Modification of low-density lipoprotein by myeloperoxidase-derived oxidants and reagent hypochlorous acid. Biochim. Biophys. Acta, 2006, 1761(4), 392-415.
- Kotani, K., Maekawa, M., Kanno, T., Kondo, A., Toda, N. and Manabe, M., Distribution of immunoreactive malondialdehydemodified low-density lipoprotein in human serum. Biochim. Biophys. Acta, 1994, 1215(1-2), 121-125.
- Delporte, C. et al., Impact of myeloperoxidase-LDL interactions on enzyme activity and subsequent posttranslational oxidative modifications of ApoB-100. J. Lipid Res., 2014, 55(4), 747-557.
- Cuchel, M. and Rader, D. J., Macrophage reverse cholesterol transport: key to the regression of atherosclerosis? Circulation, 2006, 113(21), 2548-2555. PubMed PMID: 16735689.
- Oram, J. F. and Lawn, R. M., ABCA1. The gatekeeper for eliminating excess tissue cholesterol. J. Lipid Res., 2001, 42(8), 1173-1179. PubMed PMID: 11483617.
- Khera, A. V. et al., Cholesterol efflux capacity, high-density lipoprotein function, and atherosclerosis. N. Engl. J. Med., 2011, 364, 127-135; doi:10.1056/NEJMoa1001689.
- Rohatgi, A. et al., HDL cholesterol efflux capacity and incident cardiovascular events. N. Engl. J. Med., 2014, 371, 2383-2393; doi:10.1056/NEJMoa1409065.
- Heinecke, J. W., Small HDL promotes cholesterol efflux by the ABCA1 pathway in macrophages: implications for therapies targeted to HDL. Circ. Res., 2015, 116(7), 1101-1103; doi:10.1161/CIRCRESAHA.115.306052. PubMed PMID: 25814677.
- Florentin, M., Liberopoulos, E. N., Wierzbicki, A. S. and Mikhailidis, D. P., Multiple actions of high-density lipoprotein. Curr. Opin. Cardiol., 2008, 23(4), 370-378; doi: 10.1097/HC0.0b013e3283043806. Review. PubMed PMID: 18520722.
- Ansell, B. J. et al., Inflammatory/anti-inflammatory properties of high-density lipoprotein distinguish patients from control subjects better than high-density lipoprotein cholesterol levels and are favourably affected by simvastatin treatment. Circulation, 2003, 108, 2751-2756. PubMed: 14638544.
- Aviram, M., Rosenblat, M., Bisgaier, C. L., Newton, R. S., PrimoParmo, S. L. and La Du, B. N., Paraoxonase inhibits high-density lipoprotein oxidation and preserves its functions. a possible peroxidative role for paraoxonase. J. Clin. Invest., 1998, 101(8), 1581-1590.
- Shih, D. M. et al., Mice lacking serum paraoxonase are susceptible to organophosphate toxicity and atherosclerosis. Nature, 1998, 394(6690), 284-287.
- Rosenblat, M., Volkova, N. and Aviram, M., Injection of paraoxonase 1 (P0N1) to mice stimulates their HDL and macrophage antiatherogenicity. Biofactors, 2011, 37(6), 462-467; doi:10.1002/biof.188. PubMed PMID: 22162319.
- Fridman, O., Gariglio, L., Riviere, S., Porcile, R., Fuchs, A. and Potenzoni, M., Paraoxonase 1 gene polymorphisms and enzyme activities in coronary artery disease and its relationship to serum lipids and glycemia. Arch. Cardiol. Mex., 2016, 86(4), 350-357; doi:10.1016/j.acmx.2016.08.001. PubMed PMID: 27640339.
- Shuhei, N., Soderlund, S., Jauhiainen, M. and Taskinen, M.-R., Effect of HDL composition and particle size on the resistance of HDL to the oxidation. Lipids Health Dis., 2010, 9, 104; doi:10.1186/1476-511X-9-104.
- Vivekanandan-Giri, A. et al., High density lipoprotein is targeted for oxidation by myeloperoxidase in rheumatoid arthritis. Ann. Rheum. Dis., 2013, 72(10), 1725-1731; doi: 10.1136/annrheumdis-2012-202033.
- Bergt, C., Oram, J. F. and Heinecke, J. W., Oxidized HDL: the paradoxidation of lipoproteins. Arterioscler. Thromb. Vasc. Biol., 2003, 23(9), 1488-1490. Review. PubMed PMID: 12972461.
- Thomson, L., 3-Nitrotyrosine modified proteins in atherosclerosis. Dis. Markers, 2015, 2015, 8; doi:10.1155/2015/708282.
- Panzenbock, U. and Stocker, R., Formation of methionine sulfoxidecontaining specific forms of oxidized high-density lipoproteins. Biochim. Biophys. Acta, 2005, 1703(2), 171-181. PubMed PMID: 15680225.
- Holzer, M. et al., Protein carbamylation renders high-density lipoprotein dysfunctional. Antioxid. Redox Signal., 2011, 14(12), 2337-2346; doi: 10.1089/ars.2010.3640. PubMed PMID: 21235354.
- Smith, J. D., Dysfunctional HDL as a diagnostic and therapeutic target. Arterioscler. Thromb. Vasc. Biol., 2010, 30(2), 151-155; doi:10.1161/ATVBAHA. 108.179226. PubMed PMID: 19679832.
- Navab, M., Reddy, S. T., Van Lenten, B. J. and Fogelman, A. M., HDL and cardiovascular disease: atherogenic and atheroprotective mechanisms. Nature Rev. Cardiol., 2011, 8, 222-232; doi:10.1038/nrcardio.2010.222.
- Bergt, C. et al., The myeloperoxidase product hypochlorous acid oxidizes HDL in the human artery wall and impairs ABCA1dependent cholesterol transport. Proc. Natl. Acad. Sci. USA, 2004, 101(35), 13032-13037. PubMed PMID: 15326314.
- DiDonato, J. A. et al., Site-specific nitration of apolipoprotein AI at tyrosine 166 is both abundant within human atherosclerotic plaque and dysfunctional. J. Biol. Chem., 2014, 289(15), 10276-10292.
- Huang, Y. et al., An abundant dysfunctional apolipoprotein A1 in human atheroma. Nature Med., 2014, 20(2), 193-203.
- Ali, M. et al., Myeloperoxidase inhibition improves ventricular function and remodelling after experimental myocardial infarction. JACC Basic Transl. Sci., 2016, 1(7), 633-643; https://doi.org/10.1016/j.jacbts.2016.09.004.
- Brennan, M. L. et al., Increased atherosclerosis in myeloperoxidasedeficient mice. J. Clin. Invest., 2001, 107(4), 419-430. PubMed PMID: 11181641.
- McMillen, T. S., Heinecke, J. W. and LeBoeuf, R. C., Expression of human myeloperoxidase by macrophages promotes atherosclerosis in mice. Circulation, 2005, 111(21), 2798-2804.
- Castellani, L. W., Chang, J. J., Wang, X., Lusis, A. J. and Reynolds, W. F., Transgenic mice express human MPO-463G/A alleles at atherosclerotic lesions, developing hyperlipidemia and obesity in -463G males. J. Lipid Res., 2006, 47(7), 1366-1377. PubMed PMID: 16639078.
- Jia, G., Hill, M. A. and Sowers, J. R., Diabetic cardiomyopathy: an update of mechanisms contributing to this clinical entity. Circ. Res., 2018, 122(4), 624-638.
- Bugger, H. and Abel, E. D., Molecular mechanisms of diabetic cardiomyopathy. Diabetologia, 2014, 57(4), 660-671.
- Global Report on Diabetes by World Health Organization. Publications by the World Health Organization, 2016, pp. 1-88.
- Arundgovind, G., Kamalanathan, A. S. and Venkataraman, K., Atherogenic dyslipoprotenemia in type 2 diabetes. In Mechanisms o f Vascular Defects in Diabetes Mellitus (eds Kartha, C. C., Ramachandran, S. and Pillai, R. M.), Advances in Biochemistry in Health and Diseases, Springer Press, Cham, 2017, pp. 451-467.
- Hasanally, D., Edel, A., Chaudhary, R. and Ravandi, A., Identification of oxidized phosphatidylinositols present in OxLDL and human atherosclerotic plaque. Lipids, 2017, 52(1), 11-26; doi: 10.1007/s11745-016-4217-y.
- Iqbal, J., Walsh, M. T., Hammad, S. M. and Hussain, M. M., Sphingolipids and lipoproteins in health and metabolic disorders. Trends Endocrinol. Metab., 2017, 28(7), 506-518.
- Levkau, B., HDL-S1P: cardiovascular functions, disease-associated alterations, and therapeutic applications. Front. Pharmacol., 2015, 6, 243.
- Saini-Chohan, H. K., Mitchell, R. W., Vaz, F. M., Zelinski, T. and Hatch, G. M., Delineating the role of alterations in lipid metabolism to the pathogenesis of inherited skeletal and cardiac muscle disorders: thematic review series: genetics of human lipid diseases. J. Lipid Res., 2012, 53(1), 4-27.
- Platt, F. M., Sphingolipid lysosomal storage disorders. Nature, 2014, 510(7503), 68-75.
- Feitosa, M. F. et al., Genetic analysis of long-lived families reveals novel variants influencing high density-lipoprotein cholesterol. Front. Genet, 2014, 5, 159; doi:10.3389/fgene.2014.00159.
- Brennan, M.-L. et al., Prognostic value of myeloperoxidase in patients with chest pain. N. Engl. J. Med., 2003, 349, 1595-1604 [PubMed:14573731].
- Zhang, R. et a l., Association between myeloperoxidase levels and risk of coronary artery disease. J. Am. Med. Assoc., 2001, 286, 2136-2142. PubMed: 11694155.
- Zheng, L. et al., Apolipoprotein A-I is a selective target for myeloperoxidasecatalyzed oxidation and functional impairment in subjects with cardiovascular disease. J. Clin. Invest., 2004, 114, 529-541. PubMed: 15314690.
- Rosenson, R. S., et al., Dysfunctional HDL and atherosclerotic cardiovascular disease. Nature Rev. Cardiol., 2016, 13(1), 48-60.
- Lokeshwaran, K. and Venkataraman, K., Development of monoclonal antibody against chlorinated 192tyrosine containing ApoAI peptide to screen quality of human high density lipoprotein (HDL). Protein Pept. Lett., 2016, 23(10), 905-912. PubMed PMID: 27468813.
- Zheng, L., Settle, M., Brubaker, G., Schmitt, D., Hazen, S. L., Smith, J. D. and Kinter, M., Localization of nitration and chlorination sites on apolipoprotein A-I catalyzed by myeloperoxidase in human atheroma and associated oxidative impairment in ABCA1-dependent cholesterol efflux from macrophages. J. Biol. Chem., 2005, 280(1), 38-47.
- Shao, B. et al., Myeloperoxidase impairs ABCA1-dependent cholesterol efflux through methionine oxidation and site-specific tyrosine chlorination of apolipoprotein A-I. J. Biol. Chem., 2006, 281(14), 9001-9004.
- Shao, B., Oda, M. N., Oram, J. F. and Heinecke, J. W., Myeloperoxidase: an oxidative pathway for generating dysfunctional high-density lipoprotein. Chem. Res. Toxicol., 2010, 23(3), 447^54.
- Smith, J. D., Dysfunctional HDL as a diagnostic and therapeutic target. Arterioscler. Thromb. Vasc. Biol., 2010, 30(2), 151-155.
- Holzer, M. et al., Myeloperoxidase-derived chlorinating species induce protein carbamylation through decomposition of thiocyanate and urea: novel pathways generating dysfunctional high-density lipoprotein. Antioxid. Redox Signal., 2012, 17(8), 1043-1052.
- Interleukin-6, a major player of cytokine storm in COVID-19 and its alleviation by therapeutic antibodies
Abstract Views :154 |
PDF Views:80
Authors
Affiliations
1 Centre for BioSeparation Technology, Vellore Institute of Technology, Vellore 632 014, India
1 Centre for BioSeparation Technology, Vellore Institute of Technology, Vellore 632 014, India
Source
Current Science, Vol 123, No 6 (2022), Pagination: 745-753Abstract
Interleukin-6 (IL-6) is an important cytokine that plays a vital role in immune response and inflamma-tion. Here, the signalling functions of IL-6 through its receptors, physiological and pathological roles, espe-cially its contribution to various autoimmune diseases, cancers and severe COVID-19/SARS-CoV2 infections are described. It is reported that in severe COVID-19 infection and auto-immune diseases, the patients expe-rience cytokine storms due to hyper-activation of the IL-6 receptor pathway leading to detrimental effects. Blocking IL-6 receptor action by therapeutic antibodies has been considered an attractive strategy of treat-ment. The latest findings on the application of anti-IL-6 therapeutic antibodies in COVID-19 patients are also discussed.Keywords
COVID-19 infection, cytokine storm, im-mune response, interleukin-6, therapeutic antibodies.References
- Kumar, P. and Mina, U., Life Sciences: Fundamentals and Practice-1 (Fifth Edition), Pathfinder Publication, New Delhi, 2015, pp. 459–534.
- World Health Organization, WHO coronavirus (COVID-19) dash-board with vaccination data; https://covid19.who.int/ (accessed on 10 June 2022).
- Tang, Y. et al., Cytokine storm in COVID-19: the current evidence and treatment strategies. Front. Immunol., 2020, 11, 1708.
- Atal, S. and Fatima, Z., IL-6 inhibitors in the treatment of serious COVID-19: a promising therapy? Pharma. Med., 2020, 34, 223– 231.
- Fajgenbaum, D. C. and June, C. H., Cytokine storm. N. Engl. J. Med., 2020, 383, 2255–2273.
- Chen, L. Y. C., Hoiland, R. L., Stukas, S., Wellington, C. L. and Sekhon, M. S., Confronting the controversy: interleukin-6 and the COVID-19 cytokine storm syndrome. Eur. Respir. J., 2020, 56, 2003006.
- Velazquez-Salinas, L., Verdugo-Rodriguez, A., Rodriguez, L. L. and Borca, M. V., The role of interleukin-6 during viral infections. Front. Microbiol., 2019, 10, 1057.
- Wojdasiewicz, P., Poniatowski, A. A. and Szukiewicz, D., The role of inflammatory and anti-inflammatory cytokines in the patho-genesis of osteoarthritis. Med. Inflamm., 2014, 2014, 561459; doi: 10.1155/2014/561459.
- Chalaris, A., Garbers, C., Rabe, B., Rose-John, S. and Scheller, J., The soluble interleukin-6 receptor: generation and role in inflam-mation and cancer. Eur. J. Cell Biol., 2011, 90, 484–494.
- Brocke-Heidrich, K. et al., Interleukin-6-dependent gene expres-sion profiles in multiple myeloma INA-6 cells reveal a Bcl-2 family-independent survival pathway closely associated with Stat3 activation. Blood, 2004, 103, 242–251.
- Wongchana, W. and Palaga, T., Direct regulation of interleukin-6 expression by Notch signaling in macrophages. Cell. Mol. Immu-nol., 2012, 9, 155–162.
- Jones, S. A. and Jenkins, B. J., Recent insights into targeting the IL-6 cytokine family in inflammatory diseases and cancer. Nature Rev. Immunol., 2018, 18, 773–789.
- Kang, S., Narazaki, M., Metwally, H. and Kishimoto, T., Historical overview of the interleukin-6 family cytokine. J. Exp. Med., 2020, 217, 20190347.
- Murakami, M. and Hirano, T., The pathological and physiological roles of IL-6 amplifier activation. Int. J. Biol. Sci., 2012, 8, 1267–1280.
- Ohsugi, Y., The immunobiology of humanized Anti-IL6 receptor antibody: from basic research to breakthrough medicine. J. Transl. Autoimmun., 2020, 3, 100030.
- Mihara, M., Hashizume, M., Yoshida, H., Suzuki, M. and Shiina, M., IL-6/IL-6 receptor system and its role in physiological and pathological conditions. Clin. Sci., 2012, 122, 143–159.
- Castell, J. V. et al., Interleukin-6 is the major regulator of acute phase protein synthesis in adult human hepatocytes. FEBS Lett., 1989, 242, 237–239.
- Ebrabem, Q., Minamoto, A., Hoppe, G., Anand-Apte, B. and Sears, J. E., Triamcinolone acetonide inhibits IL-6- and VEGF-induced angiogenesis downstream of the IL-6 and VEGF receptors. Invest. Ophthalmol. Vis. Sci., 2006, 47, 4935–4941.
- Fielding, C. A. et al., IL-6 regulates neutrophil trafficking during acute inflammation via STAT3. J. Immunol., 2008, 181, 2189–2195.
- Tanaka, T., Narazaki, M. and Kishimoto, T., IL-6 in inflammation, immunity, and disease. Cold Spring Harbour Perspect. Biol., 2014, 6, 1–16.
- Väänänen, H. K. and Härkönen, P. L., Estrogen and bone meta-bolism. Maturitas, 1996, 23, S65–S69.
- Poli, V. et al., Interleukin-6 deficient mice are protected from bone loss caused by estrogen depletion. EMBO J., 1994, 13, 1189–1196.
- Nakajima, S. et al., Interleukin-6 inhibits early differentiation of ATDC5 chondrogenic progenitor cells. Cytokine, 2009, 47, 91–97.
- Tsuchida, A. I. et al., Interleukin-6 is elevated in synovial fluid of patients with focal cartilage defects and stimulates cartilage matrix production in an in vitro regeneration model. Arthritis Res. Ther., 2012, 14, R262.
- Feldmann, M., Brennan, F. M. and Maini, R. N., Role of cytokines in rheumatoid arthritis. Annu. Rev. Immunol., 1996, 14, 397–440.
- Kishimoto, T., Kang, S. and Tanaka, T., IL-6: a new era for the treatment of autoimmune inflammatory diseases. In Innovative Medicine, Springer, Japan, 2015, pp. 131–147; doi:10.1007/978-4-431-55651-0_11.
- Dougados, M. et al., Adding tocilizumab or switching to tocili-zumab monotherapy in methotrexate inadequate responders: 24-week symptomatic and structural results of a 2-year randomised controlled strategy trial in rheumatoid arthritis (ACT-RAY). Ann. Rheum. Dis., 2013, 72, 43–50.
- Sandborg, C. and Mellins, E. D., A new era in the treatment of systemic juvenile idiopathic arthritis. N. Engl. J. Med., 2012, 367, 2439–2440.
- Tackey, E., Lipsky, P. E. and Illei, G. G., Rationale for interleukin-6 blockade in systemic lupus erythematosus. Lupus, 2004, 13, 339–343.
- Krei, K., Fredrikson, S., Fontana, A. and Link, H., Interleukin-6 is elevated in plasma in multiple sclerosis. J. Neuroimmunol., 1991, 31, 147–153.
- Ashtari, F., Madanian, R., Shaygannejad, V., Zarkesh, S. H. and Ghadimi, K., Serum levels of IL-6 and IL-17 in multiple sclerosis, neuromyelitis optica patients and healthy subjects. Int. J. Physiol. Pathophysiol. Pharmacol., 2019, 11, 267.
- Masjedi, A. et al., The significant role of interleukin-6 and its signaling pathway in the immunopathogenesis and treatment of breast cancer. Biomed. Pharmacother., 2018, 108, 1415–1424.
- Bromberg, J. and Wang, T. C., Inflammation and cancer: IL-6 and STAT3 complete the link. Cancer Cell, 2009, 15, 79–80.
- Yang, X. et al., Clinical course and outcomes of critically ill patients with SARS-CoV-2 pneumonia in Wuhan, China: a single-centered, retrospective, observational study. Lancet Respir. Med., 2020, 8, 475–481.
- Abbasifard, M. and Khorramdelazad, H., The bio-mission of inter-leukin-6 in the pathogenesis of COVID-19: a brief look at potential therapeutic tactics. Life Sci., 2020, 257, 118097.
- Huang, C. et al., Clinical features of patients infected with 2019 novel coronavirus in Wuhan, China. Lancet, 2020, 395, 497–506.
- Conti, P. et al., Induction of pro-inflammatory cytokines (IL-1 and IL-6) and lung inflammation by coronavirus-19 (COVID-19 or SARS-CoV-2): anti-inflammatory strategies. J. Biol. Regul. Homeost. Agents, 2020, 34, 327–331.
- Martinez, N. E. et al., Regulatory T cells and Th17 cells in viral infections: implications for multiple sclerosis and myocarditis. Future Virol., 2012, 7, 593–608.
- Lauder, S. N. et al., Interleukin-6 limits influenza-induced inflam-mation and protects against fatal lung pathology. Eur. J. Immunol., 2013, 43, 2613–2625.
- Hashizume, M., Outlook of IL-6 signaling blockade for COVID-19 pneumonia. Inflamm. Regen., 2020, 40, 24.
- Scherger, S., Henao-Martínez, A., Franco-Paredes, C. and Shapiro, L., Rethinking interleukin-6 blockade for treatment of COVID-19. Med. Hypotheses, 2020, 144, 110053.
- US National Library of Medicine, Anti-IL6 treatment of serious COVID-19 disease with threatening respiratory failure, sponsored by Henriksen, M., 2020; https://www.clinicaltrials.gov/ct2/show/NCT- 04322773
- Luo, P. et al., Tocilizumab treatment in COVID-19: a single center experience. J. Med. Virol., 2020, 92, 814–818.
- Samaee, H., Mohsenzadegan, M., Ala, S., Maroufi, S. S. and Mora-dimajd, P., Tocilizumab for treatment patients with COVID-19: recommended medication for novel disease. Int. Immunopharmacol., 2020, 89, 107018.
- Stone, J. H. et al., Efficacy of tocilizumab in patients hospitalized with COVID-19. N. Engl. J. Med., 2020, 383, 2333–2344.
- Salama, C. et al., Tocilizumab in patients hospitalized with COVID-19 pneumonia. N. Engl. J. Med., 2021, 384, 20–30.
- Lomakin, N. V. et al., The efficacy and safety of levilimab in severely ill COVID-19 patients not requiring mechanical ventilation: results of a multicenter randomized double-blind placebo-controlled phase III CORONA clinical study. Inflamm. Res., 2021, 70(10–12), 1233–1246.
- Reichert, J., Anti-IL-6R levilimab registered as COVID-19 treatment in Russia – The Antibody Society, 2020; https://www.antibody-society.org/approvals/anti-il-6r-levilimab-registered-as-covid-19-treat-ment-in-russia/
- Basu, M., Russia approves levilimab for treating severe Covid-19 patients, says it reduces death risk, 2020; https://theprint.in/ health/russia-approves-levilimab-for-treating-severe-covid-19-pati-ents-says-it-reduces-death-risk/439094/
- Shaw, S. et al., Discovery and characterization of olokizumab: a humanized antibody targeting interleukin-6 and neutralizing gp130-signaling. MAbs, 2014, 6, 773.
- Antonov, V. N. et al., Experience of olokizumab use in COVID-19 patients. Тherapeutic Archive, 2020, 92, 148–154.
- Della-Torre, E. et al., Interleukin-6 blockade with sarilumab in severe COVID-19 pneumonia with systemic hyperinflammation: an open-label cohort study. Ann. Rheum. Dis., 2020, 79, 1277–1285.
- Genovese, M. C. et al., Sarilumab plus methotrexate in patients with active rheumatoid arthritis and inadequate response to methotrexate: results of a phase III study. Arthritis Rheumatol., 2015, 67, 1424–1437.
- US National Library of Medicine, A study to evaluate the efficacy and safety of sirukumab in confirmed severe or critical confirmed coronavirus disease (COVID-19), sponsored by Janssen Biophar-maceuticals, 2021; https://www.clinicaltrials.gov/ct2/show/study/ NCT04380961
- Luo, P. et al., Tocilizumab treatment in COVID-19: a single center experience. J. Med. Virol., 2020, 92(7), 814–818.
- US National Library of Medicine, Study of the efficacy and safety of a single administration of olokizumab and RPH-104 with standard therapy in patients with severe acute respiratory syndrome corona-virus 2 (SARS-CoV-2) infection (COVID-19), sponsored by R-Pharma International, LLC, 2022; https://clinicaltrials.gov/ct2/show/ NCT04380519
- US National Library of Medicine, Sarilumab COVID-19, sponsored by Sanofi, 2021; https://clinicaltrials.gov/ct2/show/NCT04327388