Cited by 98

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Cholesterol in LDL receptor recycling and degradation

Yang, Hui-xian, Zhang, Min, Long, Shi-yin, Tuo, Qin-hui, Tian, Ying, Chen, Jian-xiong, Zhang, Cai-ping, Liao, Duan-fang·2020·Clinica Chimica Acta

Abstract

The SREBP2/LDLR pathway is sensitive to cholesterol content in the endoplasmic reticulum (ER), while membrane low-density lipoprotein receptor (LDLR) is influenced by sterol response element binding protein 2 (SREBP2), pro-protein convertase subtilisin/kexin type 9 (PCSK9) and inducible degrader of LDLR (IDOL). LDL-C, one of the risk factors in cardiovascular disease, is cleared through endocytosis recycling of LDLR. Therefore, we propose that a balance between LDLR endocytosis recycling and PCSK9-mediated and IDOL-mediated lysosomal LDLR degradation is responsible for cholesterol homeostasis in the ER. For statins that decrease serum LDL-C levels via cholesterol synthesis inhibition, the mechanism by which the statins increase the membrane LDLR may be regulated by cholesterol homeostasis in the ER.

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Crossref · 10.1016/j.cca.2019.09.022

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  • The acidic environment of the endosomal lumen induces complex dissociation, with LDL transported to the lysosome for hydrolysis, and free LDLR recycled back to the plasma membrane.

    “The acidic environment of the endosomal lumen induces complex dissociation, with LDL subsequently transported to the lysosome for hydrolysis, and free LDLR recycled back to the plasma membrane (8, 9).”

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Research works printed but not linked: 57

  1. Bays, 2016, National lipid association annual summary of clinical lipidology 2016, J. Clin. Lipidol., 10, S1, 10.1016/j.jacl.2015.08.002 · DOI · Paper page
  2. Vega, 2019, Current trends in non-HDL cholesterol and LDL cholesterol levels in adults with atherosclerotic cardiovascular disease, J. Clin. Lipidol., 10.1016/j.jacl.2019.05.012 · DOI
  3. Jacobson, 2014, National Lipid Association recommendations for patient-centered management of dyslipidemia: part 1 - executive summary, J. Clin. Lipidol., 8, 473, 10.1016/j.jacl.2014.07.007 · DOI
  4. Jeon, 2005, Structure and physiologic function of the low-density lipoprotein receptor, Annu. Rev. Biochem., 74, 535, 10.1146/annurev.biochem.74.082803.133354 · DOI · Paper page
  5. Schluter, 1994, An 87 bp deletion in exon 5 of the LDL receptor gene in a mother and her son with familial hypercholesterolemia, Clin. Genet., 45, 84, 10.1111/j.1399-0004.1994.tb03999.x · DOI
  6. Radhakrishnan, 2008, Switch-like control of SREBP-2 transport triggered by small changes in ER cholesterol: a delicate balance, Cell Metab., 8, 512, 10.1016/j.cmet.2008.10.008 · DOI · Paper page
  7. Park, 2004, Post-transcriptional regulation of low density lipoprotein receptor protein by proprotein convertase subtilisin/kexin type 9a in mouse liver, J. Biolog. Chem., 279, 50630, 10.1074/jbc.M410077200 · DOI · Paper page
  8. Zelcer, 2009, LXR regulates cholesterol uptake through Idol-dependent ubiquitination of the LDL receptor, Science (New York, N.Y.), 325, 100, 10.1126/science.1168974 · DOI · Paper page
  9. Dong, 2010, Strong induction of PCSK9 gene expression through HNF1alpha and SREBP2: mechanism for the resistance to LDL-cholesterol lowering effect of statins in dyslipidemic hamsters, J. Lipid Res., 51, 1486, 10.1194/jlr.M003566 · DOI
  10. Brown, 1997, The SREBP pathway: regulation of cholesterol metabolism by proteolysis of a membrane-bound transcription factor, Cell, 89, 331, 10.1016/S0092-8674(00)80213-5 · DOI · Paper page
  11. Adams, 2004, Cholesterol and 25-hydroxycholesterol inhibit activation of SREBPs by different mechanisms, both involving SCAP and Insigs, J. Biolog. Chem., 279, 52772, 10.1074/jbc.M410302200 · DOI
  12. Sun, 2007, Sterol-regulated transport of SREBPs from endoplasmic reticulum to Golgi: Insig renders sorting signal in Scap inaccessible to COPII proteins, PNAS, 104, 6519, 10.1073/pnas.0700907104 · DOI
  13. Sun, 2005, Insig required for sterol-mediated inhibition of Scap/SREBP binding to COPII proteins in vitro, J. Biolog. Chem., 280, 26483, 10.1074/jbc.M504041200 · DOI · Paper page
  14. Dubuc, 2004, Statins upregulate PCSK9, the gene encoding the proprotein convertase neural apoptosis-regulated convertase-1 implicated in familial hypercholesterolemia, Arterioscler. Thromb. Vasc. Biol., 24, 1454, 10.1161/01.ATV.0000134621.14315.43 · DOI · Paper page
  15. Lee, 2019, Pooled RCTs: Lowering LDL-C levels using statins reduces major vascular events in all age groups, Ann Intern Med, 170, JC65, 10.7326/ACPJ201906180-065 · DOI
  16. Briggs, 1993, Nuclear protein that binds sterol regulatory element of low density lipoprotein receptor promoter. I. Identification of the protein and delineation of its target nucleotide sequence, J. Biolog. Chem., 268, 14490, 10.1016/S0021-9258(19)85265-1 · DOI · Paper page
  17. Lamon-Fava, 2013, Statins and lipid metabolism: an update, Curr. Opin. Lipidol., 24, 221, 10.1097/MOL.0b013e3283613b8b · DOI
  18. Scharnagl, 2001, Effect of atorvastatin, simvastatin, and lovastatin on the metabolism of cholesterol and triacylglycerides in HepG2 cells, Biochem. Pharmacol., 62, 1545, 10.1016/S0006-2952(01)00790-0 · DOI
  19. Abifadel, 2003, Mutations in PCSK9 cause autosomal dominant hypercholesterolemia, Nat. Genet., 34, 154, 10.1038/ng1161 · DOI · Paper page
  20. Noguchi, 2010, The E32K variant of PCSK9 exacerbates the phenotype of familial hypercholesterolaemia by increasing PCSK9 function and concentration in the circulation, Atherosclerosis, 210, 166, 10.1016/j.atherosclerosis.2009.11.018 · DOI
  21. Timms, 2004, A mutation in PCSK9 causing autosomal-dominant hypercholesterolemia in a Utah pedigree, Hum. Genet., 114, 349, 10.1007/s00439-003-1071-9 · DOI
  22. Leren, 2004, Mutations in the PCSK9 gene in Norwegian subjects with autosomal dominant hypercholesterolemia, Clin. Genet., 65, 419, 10.1111/j.0009-9163.2004.0238.x · DOI
  23. Maxwell, 2004, Adenoviral-mediated expression of Pcsk9 in mice results in a low-density lipoprotein receptor knockout phenotype, PNAS, 101, 7100, 10.1073/pnas.0402133101 · DOI · Paper page
  24. Berge, 2006, Missense mutations in the PCSK9 gene are associated with hypocholesterolemia and possibly increased response to statin therapy, Arterioscler. Thromb. Vasc. Biol., 26, 1094, 10.1161/01.ATV.0000204337.81286.1c · DOI · Paper page
  25. Naoumova, 2005, 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., 25, 2654, 10.1161/01.ATV.0000190668.94752.ab · DOI
  26. Cameron, 2006, Effect of mutations in the PCSK9 gene on the cell surface LDL receptors, Hum. Mol. Genet., 15, 1551, 10.1093/hmg/ddl077 · DOI · Paper page
  27. Jeong, 2008, Sterol-dependent regulation of proprotein convertase subtilisin/kexin type 9 expression by sterol-regulatory element binding protein-2, J. Lipid Res., 49, 399, 10.1194/jlr.M700443-JLR200 · DOI · Paper page
  28. Langhi, 2008, Activation of the farnesoid X receptor represses PCSK9 expression in human hepatocytes, FEBS Lett., 582, 949, 10.1016/j.febslet.2008.02.038 · DOI
  29. McNutt, 2007, Catalytic activity is not required for secreted PCSK9 to reduce low density lipoprotein receptors in HepG2 cells, J. Biolog. Chem., 282, 20799, 10.1074/jbc.C700095200 · DOI · Paper page
  30. Lopez, 2008, Inhibition of PCSK9 as a novel strategy for the treatment of hypercholesterolemia, Drug News Perspect., 21, 323, 10.1358/dnp.2008.21.6.1246795 · DOI · Paper page
  31. Seidah, 2009, PCSK9 as a therapeutic target of dyslipidemia, Exp. Opin. Therap. Targ., 13, 19, 10.1517/14728220802600715 · DOI · Paper page
  32. McNutt, 2009, Antagonism of secreted PCSK9 increases low density lipoprotein receptor expression in HepG2 cells, J. Biolog. Chem., 284, 10561, 10.1074/jbc.M808802200 · DOI
  33. Chan, 2009, A proprotein convertase subtilisin/kexin type 9 neutralizing antibody reduces serum cholesterol in mice and nonhuman primates, PNAS, 106, 9820, 10.1073/pnas.0903849106 · DOI · Paper page
  34. Cicero, 2014, Efficacy and safety profile of evolocumab (AMG145), an injectable inhibitor of the proprotein convertase subtilisin/kexin type 9: the available clinical evidence, Expert Opin. Biol. Ther., 14, 863, 10.1517/14712598.2014.902929 · DOI
  35. Desai, 2013, Circulation, 128, 962, 10.1161/CIRCULATIONAHA.113.001969 · DOI
  36. Robinson, 2015, Efficacy and safety of alirocumab in reducing lipids and cardiovascular events, New England J. Med., 372, 1489, 10.1056/NEJMoa1501031 · DOI · Paper page
  37. Roth, 2014, Monotherapy with the PCSK9 inhibitor alirocumab versus ezetimibe in patients with hypercholesterolemia: results of a 24 week, double-blind, randomized Phase 3 trial, Int. J. Cardiol., 176, 55, 10.1016/j.ijcard.2014.06.049 · DOI
  38. Giugliano, 2012, Lancet (London, England), 380, 2007, 10.1016/S0140-6736(12)61770-X · DOI
  39. Markham, 2015, Alirocumab: first global approval, Drugs, 75, 1699, 10.1007/s40265-015-0469-8 · DOI
  40. Markham, 2015, Evolocumab: first global approval, Drugs, 75, 1567, 10.1007/s40265-015-0460-4 · DOI
  41. Orringer, 2017, Update on the use of PCSK9 inhibitors in adults: recommendations from an expert panel of the national lipid association, J. Clin. Lipidol., 11, 880, 10.1016/j.jacl.2017.05.001 · DOI
  42. Wilson, 2019, Systematic Review for the 2018 AHA/ACC/AACVPR/AAPA/ABC/ACPM/ADA/AGS/APhA/ASPC/NLA/PCNA Guideline on the management of blood cholesterol: a report of the American college of cardiology/American heart association task force on clinical practice guidelines, Circulation, 139, e1144, 10.1161/CIR.0000000000000626 · DOI
  43. Olsson, 1999, MIR is a novel ERM-like protein that interacts with myosin regulatory light chain and inhibits neurite outgrowth, J. Biolog. Chem., 274, 36288, 10.1074/jbc.274.51.36288 · DOI · Paper page
  44. Bornhauser, 2003, Functional activities and cellular localization of the ezrin, radixin, moesin (ERM) and RING zinc finger domains in MIR, FEBS Lett., 553, 195, 10.1016/S0014-5793(03)01010-X · DOI
  45. Calkin, 2011, FERM-dependent E3 ligase recognition is a conserved mechanism for targeted degradation of lipoprotein receptors, PNAS, 108, 20107, 10.1073/pnas.1111589108 · DOI · Paper page
  46. Dong, 2011, Suppression of Idol expression is an additional mechanism underlying statin-induced up-regulation of hepatic LDL receptor expression, Int. J. Mol. Med., 27, 103
  47. Scotti, 2011, Targeted disruption of the idol gene alters cellular regulation of the low-density lipoprotein receptor by sterols and liver x receptor agonists, Mol. Cell. Biol., 31, 1885, 10.1128/MCB.01469-10 · DOI · Paper page
  48. van Loon, 2018, Inactivation of the E3 Ubiquitin Ligase IDOL Attenuates Diet-Induced Obesity and Metabolic Dysfunction in Mice, Arterioscler. Thromb. Vasc. Biol., 38, 1785, 10.1161/ATVBAHA.118.311168 · DOI · Paper page
  49. Dhyani, 2015, IDOL N342S Variant, Atherosclerosis Progression and Cardiovascular Disorders in the Italian General Population, PLoS ONE, 10, e0122414, 10.1371/journal.pone.0122414 · DOI
  50. Lindholm, 2009, Mylip makes an Idol turn into regulation of LDL receptor, Cell. Mol. Life Sci.: CMLS, 66, 3399, 10.1007/s00018-009-0127-y · DOI
  51. Blom, 2016, PCSK9 inhibition in the management of hyperlipidemia: focus on evolocumab, Vascul. Health Risk Manag., 12, 185, 10.2147/VHRM.S102564 · DOI
  52. Schulman, 2009, Cholesterol worships a new idol, J. Mol. Cell. Biol., 1, 75, 10.1093/jmcb/mjp022 · DOI
  53. Zhang, 2016, IDOL, inducible degrader of low-density lipoprotein receptor, serves as a potential therapeutic target for dyslipidemia, Med. Hypotheses, 86, 138, 10.1016/j.mehy.2015.11.010 · DOI · Paper page
  54. Brown, 2016, Foiling IDOL to Help Control Cholesterol, Circ. Res., 118, 371, 10.1161/CIRCRESAHA.116.308191 · DOI
  55. Brown, 1983, Recycling receptors: the round-trip itinerary of migrant membrane proteins, Cell, 32, 663, 10.1016/0092-8674(83)90052-1 · DOI · Paper page
  56. Zhang, 2008, Niemann-Pick C1 protects against atherosclerosis in mice via regulation of macrophage intracellular cholesterol trafficking, J. Clin. Investig., 118, 2281
  57. Cullen, 2018, To degrade or not to degrade: mechanisms and significance of endocytic recycling, Nat Rev Mol Cell Biol, 19, 679, 10.1038/s41580-018-0053-7 · DOI · Paper page

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Metadata

Authors
Yang, H.-X., Zhang, M., Long, S.-Y., Tuo, Q.-H., Tian, Y., Chen, J.-X., Zhang, C.-P., & Liao, D.-F.
Venue
Clinica Chimica Acta
Publisher
Elsevier BV
Published
2020-01
Volume
500
Pages
81-86
ISSN
0009-8981
Cited by
98
References
6
Language
en
Funders
  • Construct Program of the Key Discipline in Hunan Province
  • National Natural Science Foundation of China-Yunnan Joint Fund (81670268, 31871169, 81600291, 81673722)

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