Alhafidh, N., Khalaf, M., Mustafa, N. (2026). PCSK9 Relationship with LDL and LDLR: A Promising Method for Treatment of Dyslipidemia. , 23(1), 1-11. doi: 10.33899/iraqij.p.2025.159687.1149
Nour Nabeel Alhafidh; Musab Mohammed Khalaf; Nashaat Ghalib Mustafa. "PCSK9 Relationship with LDL and LDLR: A Promising Method for Treatment of Dyslipidemia". , 23, 1, 2026, 1-11. doi: 10.33899/iraqij.p.2025.159687.1149
Alhafidh, N., Khalaf, M., Mustafa, N. (2026). 'PCSK9 Relationship with LDL and LDLR: A Promising Method for Treatment of Dyslipidemia', , 23(1), pp. 1-11. doi: 10.33899/iraqij.p.2025.159687.1149
Alhafidh, N., Khalaf, M., Mustafa, N. PCSK9 Relationship with LDL and LDLR: A Promising Method for Treatment of Dyslipidemia. , 2026; 23(1): 1-11. doi: 10.33899/iraqij.p.2025.159687.1149

PCSK9 Relationship with LDL and LDLR: A Promising Method for Treatment of Dyslipidemia

Iraqi Journal of Pharmacy
Article 1, Volume 23, Issue 1, March 2026, Pages 1-11    PDF (802.07 K)
Document Type: Review Paper
DOI: 10.33899/iraqij.p.2025.159687.1149
Authors
Nour Nabeel Alhafidh* 1; Musab Mohammed Khalaf1; Nashaat Ghalib Mustafa2
1Department of Pharmacology and Toxicology, College of Pharmacy, University of Mosul, Mosul, Iraq
2Department of Physiology, Biochemistry, and Pharmacology, College of Veterinary Medicine, University of Mosul, Mosul, Iraq
Abstract
Background: One of the most significant risk factors for cardiovascular (CV) disease is dyslipidemia, exacerbated atherosclerosis, and premature mortality due to heart attack. Lipid disorders have several etiologies, categorized into primary and secondary types. PCSK9 serves as a crucial target for treating hyperlipidemia, not only because of its recent identification or the novel biological insights it has offered, but also due to significant scientific progress that has rapidly led to effective therapeutic applications. Hepatic PCSK9 is a significant circulating protein that regulates the half-life of both the VLDLR and the LDLR. Inhibiting it is considered to be one of the most cutting-edge and technologically advanced new treatment techniques for successfully decreasing LDL cholesterol levels. Statins are the drug of choice for most cases, even though some patients do not respond to statins even with high doses. Objective: The major aim of this study is to highlight the role of PCSK9 in regulating LDL and LDLR and the effect of statins, along with PCSK9 inhibitors, on LDL and LDLR and lipid profile in general. Method: To find pertinent trials regarding PCSK9’s relation to hyperlipidemia and statin therapy between 2000 and 2024, the search strategy used electronic databases such as PubMed, Web of Science, Springer, Google Scholar, and others. Conclusion: The main kinds of frequently administered lipid-lowering drugs have been shown to raise serum PCSK9 levels. These findings most likely explain why these medicines are not more successful in lowering LDL-C and indicate that research should be done to create novel drugs that lower LDL-C by either lowering or inhibiting PCSK9 or by not raising circulating PCSK9 levels.

Highlights

  • PCSK9 regulates LDL receptor degradation, making it a critical target in dyslipidemia treatment strategies.

  • Statins increase PCSK9 levels, which may counteract their LDL-lowering effects and require combination therapy.

  • PCSK9 inhibitors effectively enhance LDL clearance by preventing LDL receptor degradation.

  • Genetic mutations in PCSK9 influence cholesterol levels and cardiovascular risk outcomes.

  • Novel drugs like inclisiran and bempedoic acid offer promising alternatives to statins in lipid management.

Keywords
Dyslipidemia; PCSK9; LDLR; LDL
References
  1. Berberich AJ, Hegele RA. A Modern Approach to Dyslipidemia. Endocrine Reviews. 2022 ;43(4):611–53.
  2. Mosca S, Araújo G, Costa V, Correia J, Bandeira A, Martins E, et al. Dyslipidemia Diagnosis and Treatment: Risk Stratification in Children and Adolescents. Suzuki T, editor. Journal Nutrition and Metabolism. 2022;2022:1–10.
  3. Angeles-Agdeppa I, Sun Y, Tanda K V. Dietary pattern and nutrient intakes in association with non-communicable disease risk factors among Filipino adults: A cross-sectional study. Nutrition Journal. 2020;19(1):1–13.
  4. Huai P, Liu J, Ye X, Li WQ. Association of Central Obesity With All Cause and Cause-Specific Mortality in US Adults: A Prospective Cohort Study. Frontiers in Cardiovascular Medicine. 2022;9(January):1–12.
  5. Rosenson RS, Brewer HB, Chapman MJ, Fazio S, Hussain MM, Kontush A, et al. HDL measures, particle heterogeneity, proposed nomenclature, and relation to atherosclerotic cardiovascular events. Clinical Chemistry. 2011;57(3):392–410.
  6. Hegele RA. Plasma lipoproteins: Genetic influences and clinical implications. Nature Reviews Genetics. 2009;10(2):109–21.
  7. Parhofer KG, Laufs U. Lipid Profile and Lipoprotein (a) Testing. Deutsches Ärzteblatt International. 2023;120 (35-36):582–588. doi: 10.3238/arztebl.m2023.0150
  8. Feingold KR. Lipid and Lipoprotein Metabolism. Endocrinology and Metabolism Clinics of North America. 2022;51(3):437–58.
  9. Kamstrup PR. Lipoprotein(a) and Cardiovascular Disease. Clin Chem. 2021 Jan 8;67(1):154–66.
  10. Ramasamy I. Update on the molecular biology of dyslipidemias. Clinica Chimica Acta. 2016;454:143–85.
  11. Berberich AJ, Hegele RA. Review A Modern Approach to Dyslipidemia. 2022;43(4):611–53.
  12. Dybiec J, Baran W, Dąbek B, Fularski P, Młynarska E, Radzioch E, et al. Advances in Treatment of Dyslipidemia. International Journal of Molecular Sciences. 2023;24(17).
  13. Sulaiman RA. Inherited metabolic disorders and dyslipidaemia. Journal of Clinical Pathology. 2020;73(7):384–90.
  14. Natesan V, Kim SJ. Lipid metabolism, disorders and therapeutic drugs – Review. Biomolecules and Therapeutics. 2021;29(6):596–604.
  15. Stone NJ, Robinson JG, Lichtenstein AH, Bairey Merz CN, Blum CB, Eckel RH, et al. 2013 ACC/AHA Guideline on the Treatment of Blood Cholesterol to Reduce Atherosclerotic Cardiovascular Risk in Adults. Circulation. 2014;129(25_suppl_2).
  16. Vodnala D, Rubenfire M, Brook RD. Secondary causes of dyslipidemia. American Journal of Cardiology. 2012;110(6):823–5.
  17. Yanai H, Yoshida H. Secondary dyslipidemia: its treatments and association with atherosclerosis. Global Health and Medicine. 2021;3(1):15–23.
  18. Zhang T, Chen J, Tang X, Luo Q, Xu D, Yu B. Interaction between adipocytes and high-density lipoprotein:new insights into the mechanism of obesity-induced dyslipidemia and atherosclerosis. Lipids in Health and Disease. 2019;18(1):223.
  19. Furtado JD, Yamamoto R, Melchior JT, Andraski AB, Gamez-Guerrero M, Mulcahy P, et al. Distinct Proteomic Signatures in 16 HDL (High-Density Lipoprotein) Subspecies. Arteriosclerosis, Thrombosis, and Vascular Biology. 2018;38(12):2827–42.
  20. Vergeer M, Holleboom AG, Kastelein JJP, Kuivenhoven JA. The HDL hypothesis: Does high-density lipoprotein protect from atherosclerosis? Journal of Lipid Research. 2010;51(8):2058–73.
  21. Padró T, Cubedo J, Camino S, Béjar MT, Ben-Aicha S, Mendieta G, et al. Detrimental Effect of Hypercholesterolemia on High-Density Lipoprotein Particle Remodeling in Pigs. Journal of the American College of Cardiology. 2017;70(2):165–78.
  22. Loscalzo J. Nitric oxide insufficiency, platelet activation, and arterial thrombosis. Circulation Research. 2001;88(8):756–62.
  23. Jung UJ, Choi MS. Obesity and its metabolic complications: The role of adipokines and the relationship between obesity, inflammation, insulin resistance, dyslipidemia and nonalcoholic fatty liver disease. International Journal of Molecular Sciences. 2014;15(4):6184–223.
  24. Catapano AL, Reiner Ž, De Backer G, Graham I, Taskinen MR, Wiklund O, et al. ESC/EAS Guidelines for the management of dyslipidaemias. The Task Force for the management of dyslipidaemias of the European Society of Cardiology (ESC) and the European Atherosclerosis Society (EAS). Atherosclerosis. 2011;217(1):3–46.
  25. Ference BA, Ginsberg HN, Graham I, Ray KK, Packard CJ, Bruckert E, et al. Low-density lipoproteins cause atherosclerotic cardiovascular disease. 1. Evidence from genetic, epidemiologic, and clinical studies. A consensus statement fromthe European Atherosclerosis Society Consensus Panel. European Heart Journal 2017;38(32):2459–72.
  26. Boarescu PM, Boarescu I, Pop RM, Roşan ŞH, Bocșan IC, Rus V, et al. Evaluation of Oxidative Stress Biomarkers, Pro-Inflammatory Cytokines, and Histological Changes in Experimental Hypertension, Dyslipidemia, and Type 1 Diabetes Mellitus. International Journal of Molecular Sciences. 2022;23(3).
  27. Carrasquilla GD, Christiansen MR, Kilpeläinen TO. The Genetic Basis of Hypertriglyceridemia. Current Atherosclerosis Reports. 2021;23(8).
  28. Mach F, Baigent C, Catapano AL, Koskinas KC, Casula M, Badimon L, et al. 2019 ESC/EAS Guidelines for the management of dyslipidaemias: lipid modification to reduce cardiovascular risk. European Heart Journal. 2020 Jan 1;41(1):111–88.
  29. Pearson GJ, Thanassoulis G, Anderson TJ, Barry AR, Couture P, Dayan N, et al. 2021 Canadian Cardiovascular Society Guidelines for the Management of Dyslipidemia for the Prevention of Cardiovascular Disease in Adults. Canadian Journal of Cardiology. 2021;37(8):1129–50.
  30. Aygun S, Tokgozoglu L. Comparison of Current International Guidelines for the Management of Dyslipidemia. Journal of Clinical Medicine. 2022;11(23).
  31. Grundy SM, Stone NJ, Bailey AL, Beam C, Birtcher KK, Blumenthal RS, et al. 2018 AHA/ACC/AACVPR/AAPA/ABC/ACPM/ADA/AGS/APhA/ASPC/NLA/PCNA Guideline on the Management of Blood Cholesterol: Executive Summary: A Report of the American College of Cardiology/American Heart Association Task Force on Clinical Practice Guidelines. Journal of the American College of Cardiology. 2019;73(24):3168–209.
  32. Jang AY, Lim S, Jo SH, Han SH, Koh KK. New trends in dyslipidemia treatment. Circulation Journal. 2021;85(6):759–68.
  33. Bao X, Liang Y, Chang H, Cai T, Feng B, Gordon K, et al. Targeting proprotein convertase subtilisin/kexin type 9 (PCSK9): from bench to bedside. Signal Transduction and Targeted Therapy. 2024;9(1).
  34. Oesterle A, Laufs U, Liao JK. Pleiotropic Effects of Statins on the Cardiovascular System. Circulation Research. 2017;229–43.
  35. Ramkumar S, Raghunath A, Raghunath S. Statin therapy: Review of safety and potential side effects. Acta Cardiologica Sinica. 2016;32(6):631–9.
  36. Cannon CP, Blazing MA, Giugliano RP, McCagg A, White JA, Theroux P, et al. Ezetimibe Added to Statin Therapy after Acute Coronary Syndromes. New England Journal of Medicine. 2015;372(25):2387–97.
  37. Robinson JG, Rosenson RS, Farnier M, Chaudhari U, Sasiela WJ, Merlet L, et al. Safety of Very Low Low-Density Lipoprotein Cholesterol Levels With Alirocumab: Pooled Data From Randomized Trials. Journal of the American College of Cardiology. 2017;69(5):471–82.
  38. Zhang B, Kuipers F, De Boer JF, Kuivenhoven JA. Modulation of bile acid metabolism to improve plasma lipid and lipoprotein profiles. Journal of Clinical Medicine. 2022;11(1).
  39. Fiorentino R, Chiarelli F. Treatment of dyslipidaemia in children. Biomedicines. 2021;9(9).
  40. Ferraro RA, Leucker T, Martin SS, Banach M, Jones SR, Toth PP. Contemporary Management of Dyslipidemia. Drugs. 2022;82(5):559–76.
  41. Elkins C, Fruh S, Jones L, Bydalek K. Clinical Practice Recommendations for Pediatric Dyslipidemia. Journal of Pediatric Health Care. 2020;33(4):494–504.
  42. Muscoli S, Ifrim M, Russo M, Candido F, Sanseviero A, Milite M, et al. Current Options and Future Perspectives in the Treatment of Dyslipidemia. Journal of Clinical Medicine. 2022;11(16).
  43. Lamb YN. Inclisiran: First Approval. Drugs. 2021;81(3):389–95.
  44. Ruscica M, Sirtori CR, Carugo S, Banach M, Corsini A. Bempedoic Acid: for Whom and When. Current Atherosclerosis Reports. 2022;24(10):791–801.
  45. Bond JS. Proteases: History, discovery, and roles in health and disease. Journal of Biological Chemistry. 2019;294(5):1643–51.
  46. Turk V, Stoka V, Vasiljeva O, Renko M, Sun T, Turk B, et al. Cysteine cathepsins: From structure, function and regulation to new frontiers. Biochimica Et Biophysica Acta-Proteins and Proteomics. 2012;1824(1):68–88.
  47. Turk B, Turk D, Turk V. Protease signalling: The cutting edge. EMBO J. 2012;31(7):1630–43.
  48. Mehranzadeh E, Crende O, Badiola I, Garcia-Gallastegi P. What Are the Roles of Proprotein Convertases in the Immune Escape of Tumors? Biomedicines. 2022;10(12):1–14.
  49. Seidah NG, Mowla SJ, Hamelin J, Mamarbachi AM, Benjannet S, Touré BB, et al. Mammalian subtilisin/kexin isozyme SKI-1: A widely expressed proprotein convertase with a unique cleavage specificity and cellular localization. Proceedings of the National Academy of Sciences of the United States of America. 1999;96(4):1321–6.
  50. Seidah NG, Benjannet S, Wickham L, Marcinkiewicz J, Bélanger Jasmin S, Stifani S, et al. The secretory proprotein convertase neural apoptosis-regulated convertase 1 (NARC-1): Liver regeneration and neuronal differentiation. Proceedings of the National Academy of Sciences of the United States of America 2003;100(3):928–33.
  51. Horton JD, Cohen JC, Hobbs HH. PCSK9: A convertase that coordinates LDL catabolism. Journal of Lipid Research. 2009;50(SUPPL.):S172–7.
  52. Naureckiene S, Ma L, Sreekumar K, Purandare U, Lo CF, Huang Y, et al. Functional characterization of Narc 1, a novel proteinase related to proteinase K. Archives of Biochemistry and Biophysics. 2003;420(1):55–67.
  53. Piper DE, Jackson S, Liu Q, Romanow WG, Shetterly S, Thibault ST, et al. The Crystal Structure of PCSK9: A Regulator of Plasma LDL-Cholesterol. Structure. 2007;15(5):545–52.
  54. Ikemura H, Takagi H, Inouye M. Requirement of pro-sequence for the production of active subtilisin E in Escherichia coli. Journal of Biological Chemistry. 1987;262(16):7859–64.
  55. Fu X, Inouye M, Shinde U. Folding pathway mediated by an intramolecular chaperone. The inhibitory and chaperone functions of the subtilisin propeptide are not obligatorily linked. Journal of Biological Chemistry. 2000;275(22):16871–8.
  56. McNutt MC, Lagace TA, Horton JD. Catalytic activity is not required for secreted PCSK9 to reduce low density lipoprotein receptors in HepG2 cells. Journal of Biological Chemistry. 2007;282(29):20799–803.
  57. Welder G, Zineh I, Pacanowski MA, Troutt JS, Cao G, Konrad RJ. High-dose atorvastatin causes a rapid sustained increase in human serum PCSK9 and disrupts its correlation with LDL cholesterol. Journal of Lipid Research. 2010;51(9):2714–21.
  58. McNutt MC, Kwon HJ, Chen C, Chen JR, Horton JD, Lagace TA. Antagonism of secreted PCSK9 increases low density lipoprotein receptor expression in HepG2 cells. Journal of Biological Chemistry. 2009;284(16):10561–70.
  59. Li J, Tumanut C, Gavigan JA, Huang WJ, Hampton EN, Tumanut R, et al. Secreted PCSK9 promotes LDL receptor degradation independently of proteolytic activity. Biochemical Journal. 2007;406(2):203–7.
  60. Cunningham D, Danley DE, Geoghegan KF, Griffor MC, Hawkins JL, Subashi TA, et al. Structural and biophysical studies of PCSK9 and its mutants linked to familial hypercholesterolemia. Nature Structural & Molecular Biology. 2007;14(5):413–9.
  61. Benjannet S, Rhainds D, Hamelin J, Nassoury N, Seidah NG. The proprotein convertase (PC) PCSK9 is inactivated by furin and/or PC5/6A: Functional consequences of natural mutations and post-translational modifications. Journal of Biological Chemistry. 2006;281(41):30561–72.
  62. Bottomley MJ, Cirillo A, Orsatti L, Ruggeri L, Fisher TS, Santoro JC, et al. Structural and biochemical characterization of the wild type PCSK9-EGF(AB) complex and natural familial hypercholesterolemia mutants. Journal of Biological Chemistry 2009;284(2):1313–23.
  63. Varret M, Rabès JP, Saint-Jore B, Cenarro A, Marinoni JC, Civeira F, et al. A third major locus for autosomal dominant hypercholesterolemia maps to 1p34.1-p32. American Journal of Human Genetics. 1999;64(5):1378–87.
  64. Benjannet S, Rhainds D, Essalmani R, Mayne J, Wickham L, Jin W, et al. NARC-1/PCSK9 and its natural mutants: Zymogen cleavage and effects on the low density lipoprotein (LDL) receptor and LDL cholesterol. Journal of Biological Chemistry. 2004;279(47):48865–75.
  65. Cohen JC 1, Boerwinkle E, Mosley Jr TH , Hobbs HH. Sequence variations in PCSK9, low LDL, and protection against coronary heart disease. The New England Journal of Medicine. 2006;354(12):1264-72. doi: 10.1056/NEJMoa054013
  66. Lee D, Kim J, Lee G. Simple methods to determine the dissociation constant, Kd. Molecules and Cells. 2024;47(10):100112.
  67. Fisher TS, Surdo P Lo, Pandit S, Mattu M, Santoro JC, Wisniewski D, et al. Effects of pH and low density lipoprotein (LDL) on PCSK9-dependent LDL receptor regulation. Journal of Biological Chemistry. 2007;282(28):20502–12.
  68. Zhang DW, Garuti R, Tang WJ, Cohen JC, Hobbs HH. Structural requirements for PCSK9-mediated degradation of the low-density lipoprotein receptor. Proceedings of the National Academy of Sciences of the United States of America. 2008;105(35):13045–50.
  69. Mousavi SA, Berge KE, Berg T, Leren TP. Affinity and kinetics of proprotein convertase subtilisin/kexin type 9 binding to low-density lipoprotein receptors on HepG2 cells. FEBS Journal. 2011;278(16):2938–50.
  70. Shapiro MD, Tavori H, Fazio S. PCSK9 from basic science discoveries to clinical trials. Circulation Research. 2018;122(10):1420–38.
  71. Qian YW, Schmidt RJ, Zhang Y, Chu S, Lin A, Wang H, et al. Secreted PCSK9 downregulates low density lipoprotein receptor through receptor-mediated endocytosis. Journal of Lipid Research. 2007;48(7):1488–98.
  72. Maxwell KN, Breslow JL. Adenoviral-mediated expression of Pcsk9 in mice results in a low-density lipoprotein receptor knockout phenotype. Proceedings of the National Academy of Sciences of the United States of America. 2004;101(18):7100–5.
  73. Hyun JJ, Lee HS, Kim KS, Kim YK, Yoon D, Sahng WP. Sterol-dependent regulation of proprotein convertase subtilisin/kexin type 9 expression by sterol-regulatory element binding protein-2. Journal of Lipid Research. 2008;49(2):399–409.
  74. Costet P, Cariou B, Lambert G, Lalanne F, Lardeux B, Jarnoux AL, et al. Hepatic PCSK9 expression is regulated by nutritional status via insulin and sterol regulatory element-binding protein 1c. Journal of Biological Chemistry. 2006;281(10):6211–8.
  75. Dubuc G, Chamberland A, Wassef H, Davignon J, Seidah NG, Bernier L, et al. Statins upregulate PCSK9, the gene encoding the proprotein convertase neural apoptosis-regulated convertase-1 implicated in familial hypercholesterolemia. Arteriosclerosis, Thrombosis, and Vascular Biology. 2004;24(8):1454–9.
  76. Lebeau PF, Byun JH, Platko K, Saliba P, Sguazzin M, MacDonald ME, et al. Caffeine blocks SREBP2-induced hepatic PCSK9 expression to enhance LDLR-mediated cholesterol clearance. Nature Communications. 2022;13(1): 1-17.
  77. Horton JD, Shah NA, Warrington JA, Anderson NN, Park SW, Brown MS, et al. Combined analysis of oligonucleotide microarray data from transgenic and knockout mice identifies direct SREBP target genes. Proceedings of the National Academy of Sciences of the United States of America. 2003;100(21):12027–32.
  78. Careskey HE, Davis RA, Alborn WE, Troutt JS, Cao G, Konrad RJ. Atorvastatin increases human serum levels of proprotein convertase subtilisin/kexin type 9. Journal of Lipid Research. 2008;49(2):394–8.
  79. Nozue T. Lipid lowering therapy and circulating PCSK9 concentration. Journal of Atherosclerosis and Thrombosis. 2017;24(9):895–907.
  80. Humphries SE, Neely RDG, Whittall RA, Troutt JS, Konrad RJ, Scartezini M, et al. Healthy individuals carrying the PCSK9 p.R46L variant and familial hypercholesterolemia patients carrying PCSK9 p.D374Y exhibit lower plasma concentrations of PCSK9. Clinical Chemistry. 2009;55(12):2153–61.
  81. Konrad RJ, Troutt JS, Cao G. Effects of currently prescribed LDL-C-lowering drugs on PCSK9 and implications for the next generation of LDL-C-lowering agents. Lipids in Health and Disease. 2011;10:1–10.
  82. Cariou B, Ouguerram K, Zaïr Y, Guerois R, Langhi C, Kourimate S, et al. PCSK9 dominant negative mutant results in increased LDL catabolic rate and familial hypobetalipoproteinemia. Arteriosclerosis, Thrombosis, and Vascular Biology. 2009;29(12):2191–7.
  83. Nozue T, Hattori H, Ogawa K, Kujiraoka T, Iwasaki T, Hirano T, et al. Correlation between serum levels of proprotein convertase subtilisin/kexin type 9 (PCSK9) and atherogenic lipoproteins in patients with coronary artery disease. Lipids in Health and Disease. 2016;15(1):1–7.
  84. Phan BAP, Dayspring TD, Toth PP. Ezetimibe therapy: Mechanism of action and clinical update. Vascular Health and Risk Management. 2012;8(1):415–27.
  85. Ballantyne CM, Houri J, Notarbartolo A, Melani L, Lipka LJ, Suresh R, et al. Effect of ezetimibe coadministered with atorvastatin in 628 patients with primary hypercholesterolemia: A prospective, randomized, double-blind trial. Circulation. 2003;107(19):2409–15.
  86. Nozue T, Michishita I, Mizuguchi I. Effects of ezetimibe on remnant-like particle cholesterol, lipoprotein (a), and oxidized low-density lipoprotein in patients with dyslipidemia. Journal of Atherosclerosis and Thrombosis. 2010;17(1):37–44.
  87. Alkhayyat SS, Al-kuraishy HM, Al-Gareeb AI, El-Bouseary MM, AboKamer AM, Batiha GES, et al. Fenofibrate for COVID-19 and related complications as an approach to improve treatment outcomes: the missed key for Holy Grail. Inflammation Research. 2022;71(10–11):1159–67.
  88. Mayne J, Dewpura T, Raymond A, Cousins M, Chaplin A, Lahey KA, et al. Plasma PCSK9 levels are significantly modified by statins and fibrates in humans. Lipids in Health and Disease. 2008;7(1):1–9.
  89. Troutt JS, Alborn WE, Cao G, Konrad RJ. Fenofi brate treatment increases human serum proprotein convertase subtilisin kexin type 9 levels. Journal of Lipid Research. 2010;51(2):345–51.
  90. Lukasova M, Hanson J, Tunaru S, Offermanns S. Nicotinic acid (niacin): New lipid-independent mechanisms of action and therapeutic potentials. Trends in Pharmacological Sciences. 2011;32(12):700–7.
Statistics
Article View: 625
PDF Download: 324


Journal Management System. Powered by iJournalPro.com