PCSK9 as a therapeutic target of dyslipidemia

Bibliography

• The world clock. 2008. Available from: http://www.peterrussell.com/Odds/WorldClock.php
   Google Scholar
• Briel M, Nordmann AJ, Bucher HC. Statin therapy for prevention and treatment of acute and chronic cardiovascular disease: update on recent trials and metaanalyses. Curr Opin Lipidol 2005;16:601-5
   PubMedGoogle Scholar
• The statin effects study. 2008. Available from: https://www.statineffects.com/info/
   Google Scholar
• Rennings AJ, Stalenhoef AF. JTT-705: is there still future for a CETP inhibitor after torcetrapib? Expert Opin Investig Drugs 2008;17:1589-97
   PubMed Web of Science ®Google Scholar
• Nissen SE, Tuzcu EM, Brewer HB, et al. Effect of ACAT inhibition on the progression of coronary atherosclerosis. N Engl J Med 2006;354:1253-63
   PubMed Web of Science ®Google Scholar
• Chandler CE, Wilder DE, Pettini JL, et al. CP-346086: an MTP inhibitor that lowers plasma cholesterol and triglycerides in experimental animals and in humans. J Lipid Res 2003;44:1887-901
   PubMed Web of Science ®Google Scholar
• Nishimoto T, Amano Y, Tozawa R, et al. Lipid-lowering properties of TAK-475, a squalene synthase inhibitor, in vivo and in vitro. Br J Pharmacol 2003;139:911-18
   PubMed Web of Science ®Google Scholar
• Brown MS, Goldstein JL. Biomedicine. Lowering LDL–not only how low, but how long? Science 2006;311:1721-3
   PubMed Web of Science ®Google Scholar
• Tall AR. Protease variants, LDL, and coronary heart disease. N Engl J Med 2006;354:1310-2
   PubMedGoogle Scholar
• Puente XS, Sanchez LM, Overall CM, Lopez-Otin C. Human and mouse proteases: a comparative genomic approach. Nat Rev Genet 2003;4:544-58
   PubMed Web of Science ®Google Scholar
• Overall CM, Kleifeld O. Towards third generation matrix metalloproteinase inhibitors for cancer therapy. Br J Cancer 2006;94:941-6
   PubMed Web of Science ®Google Scholar
• Seidah NG, Khatib AM, Prat A. The proprotein convertases and their implication in sterol and/or lipid metabolism. Biol Chem 2006;387:871-7
   PubMedGoogle Scholar
• Seidah NG, Chretien M. Proprotein and prohormone convertases: a family of subtilases generating diverse bioactive polypeptides. Brain Res 1999;848:45-62
   PubMed Web of Science ®Google Scholar
• Seidah NG, Prat A. Precursor convertases in the secretory pathway, cytosol and extracellular milieu. Essays Biochem 2002;38:79-94
   PubMedGoogle Scholar
• Seidah NG, Benjannet S, Wickham L, et al. The secretory proprotein convertase neural apoptosis-regulated convertase 1 (NARC-1): liver regeneration and neuronal differentiation. Proc Natl Acad Sci USA 2003;100:928-33
   PubMed Web of Science ®Google Scholar
• Seidah NG, Mowla SJ, Hamelin J, et al. Mammalian subtilisin/kexin isozyme SKI-1: A widely expressed proprotein convertase with a unique cleavage specificity and cellular localization. Proc Natl Acad Sci USA 1999;96:1321-6
   PubMed Web of Science ®Google Scholar
• Maxwell KN, Breslow JL. Adenoviral-mediated expression of Pcsk9 in mice results in a low-density lipoprotein receptor knockout phenotype. Proc Natl Acad Sci USA 2004;101:7100-5
   PubMed Web of Science ®Google Scholar
• Benjannet S, Rhainds D, Essalmani R, et al. NARC-1/PCSK9 and its natural mutants: zymogen cleavage and effects on the low density lipoprotein (LDL) receptor and LDL cholesterol. J Biol Chem 2004;279:48865-75
   PubMed Web of Science ®Google Scholar
• Park SW, Moon YA, Horton JD. Post-transcriptional regulation of low density lipoprotein receptor protein by proprotein convertase subtilisin/kexin type 9a in mouse liver. J Biol Chem 2004;279:50630-8
   PubMed Web of Science ®Google Scholar
• Maxwell KN, Fisher EA, Breslow JL. Overexpression of PCSK9 accelerates the degradation of the LDLR in a post-endoplasmic reticulum compartment. Proc Natl Acad Sci USA 2005;102:2069-74
   PubMed Web of Science ®Google Scholar
• Lambert G, Jarnoux AL, Pineau T, et al. Fasting induces hyperlipidemia in mice overexpressing proprotein convertase subtilisin kexin type 9: lack of modulation of very-low-density lipoprotein hepatic output by the low-density lipoprotein receptor. Endocrinology 2006;147:4985-95
   PubMed Web of Science ®Google Scholar
• Cheng D, Espenshade PJ, Slaughter CA, et al. Secreted site-1 protease cleaves peptides corresponding to luminal loop of sterol regulatory element-binding proteins. J Biol Chem 1999;274:22805-12
   PubMedGoogle Scholar
• Jin W, Fuki IV, Seidah NG, et al. Proprotein convertases are responsible for proteolysis and inactivation of endothelial lipase. J Biol Chem 2005;280:36551-9
   PubMed Web of Science ®Google Scholar
• Benjannet S, Rhainds D, Hamelin J, et al. The proprotein convertase PCSK9 is inactivated by furin and/or PC5/6A: Functional consequences of natural mutations and post-translational modifications. J Biol Chem 2006;281:30561-72
   PubMed Web of Science ®Google Scholar
• Jin W, Wang X, Millar JS, et al. Hepatic proprotein convertases modulate HDL metabolism. Cell Metab 2007;6:129-36
   PubMed Web of Science ®Google Scholar
• Attie AD. The mystery of PCSK9. Arterioscler Thromb Vasc Biol 2004;24:1337-9
   PubMedGoogle Scholar
• Abifadel M, Varret M, Rabes JP, et al. Mutations in PCSK9 cause autosomal dominant hypercholesterolemia. Nat Genet 2003;34:154-6
   PubMed Web of Science ®Google Scholar
• Leren TP. Mutations in the PCSK9 gene in Norwegian subjects with autosomal dominant hypercholesterolemia. Clin Genet 2004;65:419-22
   PubMed Web of Science ®Google Scholar
• Timms KM, Wagner S, Samuels ME, et al. A mutation in PCSK9 causing autosomal-dominant hypercholesterolemia in a Utah pedigree. Hum Genet 2004;114:349-53
   PubMed Web of Science ®Google Scholar
• Allard D, Amsellem S, Abifadel M, et al. Novel mutations of the PCSK9 gene cause variable phenotype of autosomal dominant hypercholesterolemia. Hum Mutat 2005;26:497-506
   PubMedGoogle Scholar
• Naoumova RP, Tosi I, Patel D, et al. Severe hypercholesterolemia in four British families with the D374Y mutation in the PCSK9 gene: long-term follow-up and treatment response. Arterioscler Thromb Vasc Biol 2005;25:2654-60
   PubMed Web of Science ®Google Scholar
• Cohen J, Pertsemlidis A, Kotowski IK, et al. Low LDL cholesterol in individuals of African descent resulting from frequent nonsense mutations in PCSK9. Nat Genet 2005;37:161-5
   PubMed Web of Science ®Google Scholar
• Kotowski IK, Pertsemlidis A, Luke A, et al. A spectrum of PCSK9 alleles contributes to plasma levels of low-density lipoprotein cholesterol. Am J Hum Genet 2006;78:410-22
   PubMed Web of Science ®Google Scholar
• Berge KE, Ose L, Leren TP. Missense mutations in the PCSK9 gene are associated with hypocholesterolemia and possibly increased response to statin therapy. Arterioscler Thromb Vasc Biol 2006;26:1094-100
   PubMed Web of Science ®Google Scholar
• Zhao Z, Tuakli-Wosornu Y, Lagace TA, et al. Molecular characterization of loss-of-function mutations in PCSK9 and identification of a compound heterozygote. Am J Hum Genet 2006;79:514-23
   PubMed Web of Science ®Google Scholar
• Homer VM, Marais AD, Charlton F, et al. Identification and characterization of two non-secreted PCSK9 mutants associated with familial hypercholesterolemia in cohorts from New Zealand and South Africa. Atherosclerosis 2008;196:659-66
   PubMed Web of Science ®Google Scholar
• Bourbon M, Alves AC, Medeiros AM, et al. Familial hypercholesterolaemia in Portugal. Atherosclerosis 2008;196:633-42
   PubMed Web of Science ®Google Scholar
• Kathiresan S, Melander O, Guiducci C, et al. Six new loci associated with blood low-density lipoprotein cholesterol, high-density lipoprotein cholesterol or triglycerides in humans. Nat Genet 2008;40:189-97
   PubMed Web of Science ®Google Scholar
• Willer CJ, Sanna S, Jackson AU, et al. Newly identified loci that influence lipid concentrations and risk of coronary artery disease. Nat Genet 2008;40:161-9
   PubMed Web of Science ®Google Scholar
• Schadt EE, Molony C, Chudin E, et al. Mapping the genetic architecture of gene expression in human liver. PLoS Biol 2008; published online 6 May 2008, doi:10.1371/journal.pbio.0060107
   PubMedGoogle Scholar
• Dubuc G, Chamberland A, Wassef H, et al. Statins upregulate PCSK9, the gene encoding the proprotein convertase neural apoptosis-regulated convertase-1 implicated in familial hypercholesterolemia. Arterioscler Thromb Vasc Biol 2004;24:1454-9
   PubMed Web of Science ®Google Scholar
• Attie AD, Seidah NG. Dual regulation of the LDL receptor–some clarity and new questions. Cell Metab 2005;1:290-2
   PubMedGoogle Scholar
• Rashid S, Curtis DE, Garuti R, et al. Decreased plasma cholesterol and hypersensitivity to statins in mice lacking Pcsk9. Proc Natl Acad Sci USA 2005;102:5374-9
   PubMed Web of Science ®Google Scholar
• Zaid A, Roubtsova A, Essalmani R, et al. Proprotein convertase subtilisin/kexin type 9 (PCSK9): Hepatocyte-specific low-density lipoprotein receptor degradation and critical role in mouse liver regeneration. Hepatology 2008;48:646-54
   PubMed Web of Science ®Google Scholar
• Lagace TA, Curtis DE, Garuti R, et al. Secreted PCSK9 decreases the number of LDL receptors in hepatocytes and inlivers of parabiotic mice. J Clin Invest 2006;116:2995-3005
   PubMed Web of Science ®Google Scholar
• Horton JD, Cohen JC, Hobbs HH. Molecular biology of PCSK9: its role in LDL metabolism. Trends Biochem Sci 2007;32:71-7
   PubMed Web of Science ®Google Scholar
• Lilly SM, Rader DJ. New targets and emerging therapies for reducing LDL cholesterol. Curr Opin Lipidol 2007;18:650-5
   PubMed Web of Science ®Google Scholar
• Lambert G. Unravelling the functional significance of PCSK9. Curr Opin Lipidol 2007;18:304-9
   PubMed Web of Science ®Google Scholar
• Seidah NG, Prat A. The proprotein convertases are potential targets in the treatment of dyslipidemia. J Mol Med 2007;85:685-96
   PubMed Web of Science ®Google Scholar
• Chretien M, Seidah NG, Basak A, Mbikay M. Proprotein convertases as therapeutic targets. Expert Opin Ther Targets 2008;12:1289-300
   PubMed Web of Science ®Google Scholar
• Seidah NG, Mayer G, Zaid A, et al. The activation and physiological functions of the proprotein convertases. Int J Biochem Cell Biol 2008;40:1111-25
   PubMed Web of Science ®Google Scholar
• Lopez D. Inhibition of PCSK9 as a novel strategy for the treatment of hypercholesterolemia. Drug News Perspect 2008;21:323-30
   PubMedGoogle Scholar
• Lopez D. PCSK9: an enigmatic protease. Biochim Biophys Acta 2008;1781:184-91
   PubMed Web of Science ®Google Scholar
• Lambert G, Charlton F, Rye KA, Piper DE. Molecular basis of PCSK9 function. Atherosclerosis 2008; published online 20 June 2008, doi:10.1016/j.atherosclerosis.2008.06.010
   Google Scholar
• McNutt MC, Lagace TA, Horton JD. Catalytic activity is not required for secreted PCSK9 to reduce low density lipoprotein receptors in HepG2 cells. J Biol Chem 2007;282:20799-803
   PubMed Web of Science ®Google Scholar
• Li J, Tumanut C, Gavigan JA, et al. Secreted PCSK9 promotes LDL receptor degradation independently of proteolytic activity. Biochem J 2007;406:203-7
   PubMed Web of Science ®Google Scholar
• Cunningham D, Danley DE, Geoghegan KF, et al. Structural and biophysical studies of PCSK9 and its mutants linked to familial hypercholesterolemia. Nat Struct Mol Biol 2007;14:413-9
   PubMed Web of Science ®Google Scholar
• Zhang DW, Lagace TA, Garuti R, et al. Binding of proprotein convertase subtilisin/kexin type 9 to epidermal growth factor-like repeat a of low density lipoprotein receptor decreases receptor recycling and increases degradation. J Biol Chem 2007;282:18602-12
   PubMed Web of Science ®Google Scholar
• Hampton EN, Knuth MW, Li J, et al. The self-inhibited structure of full-length PCSK9 at 1.9 Å reveals structural homology with resistin within the C-terminal domain. Proc Natl Acad Sci USA 2007;104:14604-9
   PubMed Web of Science ®Google Scholar
• Nassoury N, Blasiole DA, Tebon OA, et al. The cellular trafficking of the secretory proprotein convertase PCSK9 and its dependence on the LDLR. Traffic 2007;8:718-32
   PubMed Web of Science ®Google Scholar
• Mayer G, Poirier S, Seidah NG. Annexin A2 is a C-terminal PCSK9 binding protein that regulates endogenous LDL receptor levels. J Biol Chem 2008;283(46):31791-801
   PubMed Web of Science ®Google Scholar
• Horton JD, Shah NA, Warrington JA, et al. Combined analysis of oligonucleotide microarray data from transgenic and knockout mice identifies direct SREBP target genes. Proc Natl Acad Sci USA 2003;100:12027-32
   PubMed Web of Science ®Google Scholar
• Maxwell KN, Soccio RE, Duncan EM, et al. Novel putative SREBP and LXR target genes identified by microarray analysis in liver of cholesterol-fed mice. J Lipid Res 2003;44:2109-19
   PubMed Web of Science ®Google Scholar
• Jeong HJ, Lee HS, Kim KS, et al. Sterol-dependent regulation of proprotein convertase subtilisin/kexin type 9 expression by sterol-regulatory element binding protein-2. J Lipid Res 2008;49:399-409
   PubMed Web of Science ®Google Scholar
• Costet P, Cariou B, Lambert G, et al. Hepatic PCSK9 expression is regulated by nutritional status via insulin and sterol regulatory-element binding protein 1c. J Biol Chem 2006;281:6211-8
   PubMed Web of Science ®Google Scholar
• Graham MJ, Lemonidis KM, Whipple CP, et al. Antisense inhibition of proprotein convertase subtilisin/kexin type 9 reduces serum LDL in hyperlipidemic mice. J Lipid Res 2007;48:763-7
   PubMed Web of Science ®Google Scholar
• Kastelein JJ, Wedel MK, Baker BF, et al. Potent reduction of apolipoprotein B and low-density lipoprotein cholesterol by short-term administration of an antisense inhibitor of apolipoprotein B. Circulation 2006;114:1729-35
   PubMed Web of Science ®Google Scholar
• Ito MK. ISIS 301012 gene therapy for hypercholesterolemia: sense, antisense, or nonsense? Ann Pharmacother 2007;41:1669-78
   PubMed Web of Science ®Google Scholar
• Akdim F, Stroes ES, Kastelein JJ. Antisense apolipoprotein B therapy: where do we stand? Curr Opin Lipidol 2007;18:397-400
   PubMed Web of Science ®Google Scholar
• Frank-Kamenetsky M, Grefhorst A, Anderson NN, et al. Therapeutic RNAi targeting PCSK9 acutely lowers plasma cholesterol in rodents and LDL cholesterol in nonhuman primates. Proc Natl Acad Sci USA 2008;105:11915-20
   PubMed Web of Science ®Google Scholar
• Elmen J, Lindow M, Silahtaroglu A, et al. Antagonism of microRNA-122 in mice by systemically administered LNA-antimiR leads to up-regulation of a large set of predicted target mRNAs in the liver. Nucleic Acids Res 2008;36:1153-62
   PubMed Web of Science ®Google Scholar
• Elmen J, Lindow M, Schutz S, et al. LNA-mediated microRNA silencing in non-human primates. Nature 2008;452:896-9
   PubMed Web of Science ®Google Scholar
• Straarup EM, Nielson NF, Hansen JB, et al. The potential of locked nucleic acid oligonucleotides in treatment of hyperlipidemia [27, abstract P170]. Arterioscler Thromb Vasc Biol 2007
   Google Scholar
• Alborn WE, Cao G, Careskey HE, et al. Serum proprotein convertase subtilisin kexin type 9 is correlated directly with serum LDL cholesterol. Clin Chem 2007;53:1814-9
   PubMed Web of Science ®Google Scholar
• Mayne J, Raymond A, Chaplin A, et al. Plasma PCSK9 levels correlate with cholesterol in men but not in women. Biochem Biophys Res Commun 2007;361:451-6
   PubMedGoogle Scholar
• Dewpura T, Raymond A, Hamelin J, et al. PCSK9 is phosphorylated by a Golgi casein kinase-like kinase ex vivo and circulates as a phosphoprotein in humans. FEBS J 2008;275:3480-93
   PubMedGoogle Scholar
• Lambert G, Ancellin N, Charlton F, et al. Plasma PCSK9 concentrations correlate with LDL and total cholesterol in diabetic patients and are decreased by fenofibrate treatment. Clin Chem 2008;54:1038-45
   PubMed Web of Science ®Google Scholar
• Cameron J, Ranheim T, Kulseth MA, et al. Berberine decreases PCSK9 expression in HepG2 cells. Atherosclerosis 2008; published online 15 February 2008, doi:10.1016/j.atherosclerosis.2008.02.004
   Google Scholar
• Kourimate S, Le May C, Langhi C, et al. Dual mechanisms for the fibrate-mediated repression of proprotein convertase subtilisin/kexin type 9. J Biol Chem 2008;283:9666-73
   PubMed Web of Science ®Google Scholar
• Mayne J, Dewpura T, Raymond A, et al. Plasma PCSK9 levels are significantly modified by statins and fibrates in humans. Lipids Health Dis 2008;7:22. Published online 11 June 2008, doi:10.1186/1476-511X-7-22
   PubMed Web of Science ®Google Scholar
• Piper DE, Jackson S, Liu Q, et al. The crystal structure of PCSK9: A regulator of plasma LDL-cholesterol. Structure 2007;15:545-52
   PubMed Web of Science ®Google Scholar
• Kwon HJ, Lagace TA, McNutt MC, et al. Molecular basis for LDL receptor recognition by PCSK9. Proc Natl Acad Sci USA 2008;105:1820-5
   PubMed Web of Science ®Google Scholar
• Fisher TS, Lo SP, Pandit S, et al. PCSK9-dependent LDL receptor regulation: Effects of pH and LDL. J Biol Chem 2007;282:20502-12
   PubMedGoogle Scholar
• Kim PS, Arvan P. Endocrinopathies in the family of endoplasmic reticulum (ER) storage diseases: disorders of protein trafficking and the role of ER molecular chaperones. Endocr Rev 1998;19:173-202
   PubMed Web of Science ®Google Scholar
• Gregor MF, Hotamisligil GS. Thematic review series: Adipocyte Biology. Adipocyte stress: the endoplasmic reticulum and metabolic disease. J Lipid Res 2007;48:1905-14
   PubMed Web of Science ®Google Scholar
• Ali BR, Jeffery S, Patel N, et al. Novel Robinow syndrome causing mutations in the proximal region of the frizzled-like domain of ROR2 are retained in the endoplasmic reticulum. Hum Genet 2007;122:389-95
   PubMedGoogle Scholar
• Zhang DW, Garuti R, Tang WJ, et al. Structural requirements for PCSK9-mediated degradation of the low-density lipoprotein receptor. Proc Natl Acad Sci USA 2008;105:13045-50
   PubMed Web of Science ®Google Scholar
• Poirier S, Mayer G, Benjannet S, et al. The proprotein convertase PCSK9 induces the degradation of low density lipoprotein receptor (LDLR) and its closest family members VLDLR and ApoER2. J Biol Chem 2008;283:2363-72
   PubMed Web of Science ®Google Scholar
• Ling Q, Jacovina AT, Deora A, et al. Annexin II regulates fibrin homeostasis and neoangiogenesis in vivo. J Clin Invest 2004;113:38-48
   PubMed Web of Science ®Google Scholar
• Cohen JC, Boerwinkle E, Mosley TH Jr, Hobbs HH. Sequence variations in PCSK9, low LDL, and protection against coronary heart disease. N Engl J Med 2006;354:1264-72
   PubMed Web of Science ®Google Scholar
• Hooper AJ, Marais AD, Tanyanyiwa DM, Burnett JR. The C679X mutation in PCSK9 is present and lowers blood cholesterol in a Southern African population. Atherosclerosis 2007;193:445-8
   PubMed Web of Science ®Google Scholar
• Ding K, Kullo IJ. Molecular population genetics of PCSK9: a signature of recent positive selection. Pharmacogenet Genomics 2008;18:169-79
   PubMedGoogle Scholar
• Cameron J, Holla OL, Berge KE, et al. Investigations on the evolutionary conservation of PCSK9 reveal a functionally important protrusion. FEBS J 2008;275:4121-33
   PubMedGoogle Scholar
• Mbikay M, Mayne J, Seidah NG, Chretien M. Of PCSK9, cholesterol homeostasis and parasitic infections: Possible survival benefits of loss-of-function PCSK9 genetic polymorphisms. Med Hypotheses 2007;69:1010-7
   PubMedGoogle Scholar
• Sirois F, Gbeha E, Sanni A, et al. Ethnic differences in the frequency of the cardioprotective C679X PCSK9 mutation in a West African population. Genet Test 2008;12:377-80
   PubMedGoogle Scholar