CoChat
Sign Up
Cited by 134Cholesterol and Lipid MetabolismDrug Transport and Resistance MechanismsLipoproteins and Cardiovascular Health

Molecular mechanisms for ABCA1-mediated cholesterol efflux

Open access
Chen, Lei, Zhao, Zhen-Wang, Zeng, Peng-Hui, Zhou, Ying-Jie, Yin, Wen-Jun·2022·Cell Cycle
DOI 10.1080/15384101.2022.2042777PMC PMC9103275
Open this paper in CoChat — free accountOpen PDF

Abstract

The maintenance of cellular cholesterol homeostasis is essential for normal cell function and viability. Excessive cholesterol accumulation is detrimental to cells and serves as the molecular basis of many diseases, such as atherosclerosis, Alzheimer's disease, and diabetes mellitus. The peripheral cells do not have the ability to degrade cholesterol. Cholesterol efflux is therefore the only pathway to eliminate excessive cholesterol from these cells. This process is predominantly mediated by ATP-binding cassette transporter A1 (ABCA1), an integral membrane protein. ABCA1 is known to transfer intracellular free cholesterol and phospholipids to apolipoprotein A-I (apoA-I) for generating nascent high-density lipoprotein (nHDL) particles. nHDL can accept more free cholesterol from peripheral cells. Free cholesterol is then converted to cholesteryl ester by lecithin:cholesterol acyltransferase to form mature HDL. HDL-bound cholesterol enters the liver for biliary secretion and fecal excretion. Although how cholesterol is transported by ABCA1 to apoA-I remains incompletely understood, nine models have been proposed to explain this effect. In this review, we focus on the current view of the mechanisms underlying ABCA1-mediated cholesterol efflux to provide an important framework for future investigation and lipid-lowering therapy.

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

A few free checks a day · papers already verified open instantly · results are public

Integrity signals

Registry

Crossref · 10.1080/15384101.2022.2042777

Cites

3 of 3 references verified0 citation errors · 0 not checkable

Statistics

Claims the paper makes

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

A few free checks a day · papers already verified open instantly · results are public

Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

  • ABCA1 is the main cholesterol efflux transporter in astrocytes and transfers cellular cholesterol and phospholipids onto lipid-poor apolipoproteins.

    “The main cholesterol efflux transporter in astrocytes is ATP-binding cassette transporter A1 (ABCA1), which transfers cellular cholesterol and PLs onto lipid-poor apolipoproteins that shuttle cholesterol8–10.”

    From An iPSC-derived astrocyte model of fragile X syndrome exhibits dysregulated cholesterol homeostasis (2023) · cites this paper as [10]

    The Introduction states that ABCA1 transports free cholesterol and phospholipids to apoA-I, and §3 calls it the most important transporter of intracellular cholesterol efflux. The paper notes ABCA1 expression in the brain but does not establish that it is the main efflux transporter specifically in astrocytes. (LLM, conf=0.86)

    Experimental — accuracy not yet measured

Self-check

Percentages, sums and reported differences re-computed from the paper’s own numbers.

The self-check needs the paper’s full text.

Cites

Flagged first, then by citations

Research works printed but not linked: 116

  1. Yu XH, Fu YC, Zhang DW, et al. Foam cells in atherosclerosis. Clin Chim Acta. 2013;424:245-252.
  2. Ebara S, Marumo M, Yamabata C, et al. Inverse asso- ciations of HDL cholesterol and oxidized HDL with d-dimer in patients with type 2 diabetes mellitus. Thromb Res. 2017;155:12-15.
  3. Li G, Gu HM, Zhang DW. ATP-binding cassette trans- porters and cholesterol translocation. IUBMB Life. 2013;65(6):505-512.
  4. Gao JH, Zeng MY, Yu XH, et al. Visceral adipose tissue-derived serine protease inhibitor accelerates cho- lesterol efflux by up-regulating ABCA1 expression via the NF-kappaB/miR-33a pathway in THP-1 macropahge-derived foam cells. Biochem Biophys Res Commun. 2018;500(2):318-324.
  5. Kuang HJ, Zhao GJ, Chen WJ, et al. Hsp27 promotes ABCA1 expression and cholesterol efflux through the PI3K/PKCzeta/Sp1 pathway in THP-1 macrophages. Eur J Pharmacol. 2017;810:57-62.
  6. Li CH, Gong D, Chen LY, et al. Puerarin promotes ABCA1-mediated cholesterol efflux and decreases cel- lular lipid accumulation in THP-1 macrophages. Eur J Pharmacol. 2017;811:74-86.
  7. Zhang M, Li L, Xie W, et al. Apolipoprotein A-1 binding protein promotes macrophage cholesterol efflux by facilitating apolipoprotein A-1 binding to ABCA1 and preventing ABCA1 degradation. Atherosclerosis. 2016;248:149-159.
  8. Wang H, Liu Y, Zhu L, et al. 17beta-estradiol promotes cholesterol efflux from vascular smooth muscle cells through a liver X receptor alpha-dependent pathway. Int J Mol Med. 2014;33(3):550-558.
  9. Santamarina-Fojo S, Peterson K, Knapper C, et al. Complete genomic sequence of the human ABCA1 gene: analysis of the human and mouse ATP-binding cassette A promoter. Proc Natl Acad Sci U S A. 2000;97 (14):7987-7992.
  10. Bungert S, Molday LL, Molday RS. Membrane topol- ogy of the ATP binding cassette transporter ABCR and its relationship to ABC1 and related ABCA transpor- ters: identification of N-linked glycosylation sites. J Biol Chem. 2001;276(26):23539-23546.
  11. Kaminski WE, Piehler A, Wenzel JJ. ABC A-subfamily transporters: structure, function and disease. Biochim Biophys Acta. 2006;1762(5):510-524.
  12. Hozoji M, Kimura Y, Kioka N, et al. Formation of two intramolecular disulfide bonds is necessary for ApoA-I-dependent cholesterol efflux mediated by ABCA1. J Biol Chem. 2009;284(17):11293-11300.
  13. Dean M, Hamon Y, Chimini G. The human ATP-binding cassette (ABC) transporter superfamily. J Lipid Res. 2001;42(7):1007-1017.
  14. Hogue DL, Liu L, Ling V. Identification and character- ization of a mammalian mitochondrial ATP-binding cassette membrane protein. J Mol Biol. 1999;285 (1):379-389.
  15. Nagao K, Takahashi K, Azuma Y, et al. ATP hydrolysis-dependent conformational changes in the extracellular domain of ABCA1 are associated with apoA-I binding. J Lipid Res. 2012;53(1):126-136.
  16. Wang N, Chen W, Linsel-Nitschke P, et al. A PEST sequence in ABCA1 regulates degradation by calpain protease and stabilization of ABCA1 by apoA-I. J Clin Invest. 2003;111(1):99-107.
  17. Qian H, Zhao X, Cao P, et al. Structure of the Human Lipid Exporter ABCA1. Cell. 2017;169(7):1228-1239 e1210.
  18. van der Velde Ae. Reverse cholesterol transport: from classical view to new insights. World J Gastroenterol. 2010;16(47):5908-5915.
  19. Rader DJ, Alexander ET, Weibel GL, et al. The role of reverse cholesterol transport in animals and humans and relationship to atherosclerosis. J Lipid Res. 2009;50:S189-194.
  20. Phillips MC. Molecular mechanisms of cellular cho- lesterol efflux. J Biol Chem. 2014;289 (35):24020-24029.
  21. Zhao Y, Van Berkel TJ, Van Eck M. Relative roles of various efflux pathways in net cholesterol efflux from macrophage foam cells in atherosclerotic lesions. Curr Opin Lipidol. 2010;21(5):441-453.
  22. Yancey PG, de la Llera-moya M, Swarnakar S, et al. High density lipoprotein phospholipid composition is a major determinant of the bi-directional flux and net movement of cellular free cholesterol mediated by sca- venger receptor BI. J Biol Chem. 2000;275 (47):36596-36604.
  23. Yu XH, Zhang DW, Zheng XL, et al. Cholesterol trans- port system: an integrated cholesterol transport model involved in atherosclerosis. Prog Lipid Res. 2019;73:65-91.
  24. Adorni MP, Zimetti F, Billheimer JT, et al. The roles of different pathways in the release of cholesterol from macrophages. J Lipid Res. 2007;48(11):2453-2462.
  25. Oram JF. Tangier disease and ABCA1. Biochim Biophys Acta. 2000;1529(1-3):321-330.
  26. van Eck M, Bos IS, Kaminski WE, et al. Leukocyte ABCA1 controls susceptibility to atherosclerosis and macrophage recruitment into tissues. Proc Natl Acad Sci U S A. 2002;99(9):6298-6303.
  27. Wang MD, Franklin V, Marcel YL. In vivo reverse cholesterol transport from macrophages lacking ABCA1 expression is impaired. Arterioscler Thromb Vasc Biol. 2007;27(8):1837-1842.
  28. Zhao ZW, Zhang M, Chen LY, et al. Heat shock pro- tein 70 accelerates atherosclerosis by downregulating the expression of ABCA1 and ABCG1 through the JNK/Elk-1 pathway. Biochim Biophys Acta Mol Cell Biol Lipids. 2018;1863(8):806-822.
  29. Lv YC, Tang YY, Zhang P, et al. Histone methyltrans- ferase enhancer of zeste homolog 2-Mediated ABCA1 promoter DNA methylation contributes to the progres- sion of atherosclerosis. PLoS One. 2016;11(6): e0157265.
  30. Lv YC, Tang YY, Peng J, et al. MicroRNA-19b pro- motes macrophage cholesterol accumulation and aortic atherosclerosis by targeting ATP-binding cassette transporter A1. Atherosclerosis. 2014;236(1):215-226.
  31. Tang SL, Zhao ZW, Liu SM, et al. Pregnancy- associated plasma protein-a accelerates atherosclerosis by regulating reverse cholesterol transport and inflammation. Circ J. 2019;83(3):515-523.
  32. Van Eck M, Singaraja RR, Ye D, et al. Macrophage ATP-binding cassette transporter A1 overexpression inhibits atherosclerotic lesion progression in low-density lipoprotein receptor knockout mice. Arterioscler Thromb Vasc Biol. 2006;26(4):929-934.
  33. Zhang M, Zhao GJ, Yao F, et al. AIBP reduces athero- sclerosis by promoting reverse cholesterol transport and ameliorating inflammation in apoE(-/-) mice. Atherosclerosis. 2018;273:122-130.
  34. Lv YC, Yang J, Yao F, et al. Diosgenin inhibits athero- sclerosis via suppressing the MiR-19b-induced down- regulation of ATP-binding cassette transporter A1. Atherosclerosis. 2015;240(1):80-89.
  35. Yvan-Charvet L, Welch C, Pagler TA, et al. Increased inflammatory gene expression in ABC transporter-deficient macrophages: free cholesterol accumulation, increased signaling via toll-like recep- tors, and neutrophil infiltration of atherosclerotic lesions. Circulation. 2008;118(18):1837-1847.
  36. Stamatikos A, Dronadula N, Ng P, et al. ABCA1 over- expression in endothelial cells in vitro enhances apoai-Mediated cholesterol efflux and decreases inflammation. Hum Gene Ther. 2019;30(2):236-248.
  37. Zhang M, Zhao GJ, Yin K, et al. Apolipoprotein A-1 binding protein inhibits inflammatory signaling path- ways by binding to apolipoprotein a-1 in THP-1 macrophages. Circ J. 2018;82(5):1396-1404.
  38. Yin K, Deng X, Mo ZC, et al. Tristetraprolin- dependent post-transcriptional regulation of inflamma- tory cytokine mRNA expression by apolipoprotein A-I: role of ATP-binding membrane cassette transporter A1 and signal transducer and activator of transcription 3. J Biol Chem. 2011;286(16):13834-13845.
  39. Li L, Xu L, Chen W, et al. Reduced annexin a1 secre- tion by ABCA1 causes retinal inflammation and gang- lion cell apoptosis in a murine glaucoma model. Front Cell Neurosci. 2018;12:347.
  40. Aguirre-Portoles C, Feliu J, Reglero G, et al. ABCA1 overexpression worsens colorectal cancer prognosis by facilitating tumour growth and caveolin-1-dependent invasiveness, and these effects can be ameliorated using the BET inhibitor apabetalone. Mol Oncol. 2018;12 (10):1735-1752.
  41. Lhermusier T, Severin S, Van Rothem J, et al. ATP- binding cassette transporter 1 (ABCA1) deficiency decreases platelet reactivity and reduces thromboxane A2 production independently of hematopoietic ABCA1. J Thromb Haemost. 2016;14(3):585-595.
  42. Lyu J, Imachi H, Fukunaga K, et al. Angiotensin II induces cholesterol accumulation and impairs insulin secretion by regulating ABCA1 in beta cells. J Lipid Res. 2018;59(10):1906-1915.
  43. Oram JF, Heinecke JW. ATP-binding cassette trans- porter A1: a cell cholesterol exporter that protects against cardiovascular disease. Physiol Rev. 2005;85 (4):1343-1372.
  44. Fielding PE, Nagao K, Hakamata H, et al. A two-step mechanism for free cholesterol and phospholipid efflux from human vascular cells to apolipoprotein A-1. Biochemistry. 2000;39(46):14113-14120.
  45. Wang N, Silver DL, Thiele C, et al. ATP-binding cas- sette transporter A1 (ABCA1) functions as a cholesterol efflux regulatory protein. J Biol Chem. 2001;276(26):23742-23747.
  46. Chen J, Sharma S, Quiocho FA, et al. Trapping the transition state of an ATP-binding cassette transporter: evidence for a concerted mechanism of maltose transport. Proc Natl Acad Sci U S A. 2001;98 (4):1525-1530.
  47. Smith JD, Le Goff W, Settle M, et al. ABCA1 mediates concurrent cholesterol and phospholipid efflux to apo- lipoprotein A-I. J Lipid Res. 2004;45(4):635-644.
  48. Murata M, Peranen J, Schreiner R, et al. VIP21/caveo- lin is a cholesterol-binding protein. Proc Natl Acad Sci U S A. 1995;92(22):10339-10343.
  49. Fielding CJ, Bist A, Fielding PE. Caveolin mRNA levels are up-regulated by free cholesterol and down-regulated by oxysterols in fibroblast monolayers. Proc Natl Acad Sci U S A. 1997;94 (8):3753-3758.
  50. Hailstones D, Sleer LS, Parton RG, et al. Regulation of caveolin and caveolae by cholesterol in MDCK cells. J Lipid Res. 1998;39(2):369-379.
  51. Truong TQ, Aubin D, Falstrault L, et al. CD36, and caveolin-1 contribute positively to cholesterol efflux in hepatic cells. Cell Biochem Funct. 2010;28(6):480-489.
  52. Fu Y, Hoang A, Escher G, et al. Expression of caveolin-1 enhances cholesterol efflux in hepatic cells. J Biol Chem. 2004;279(14):14140-14146.
  53. Hu Q, Zhang XJ, Liu CX, et al. PPARgamma1-induced caveolin-1 enhances cholesterol efflux and attenuates atherosclerosis in apolipoprotein E-deficient mice. J Vasc Res. 2010;47(1):69-79.
  54. Lin YC, Ma C, Hsu WC, et al. Molecular interaction between caveolin-1 and ABCA1 on high-density lipoprotein-mediated cholesterol efflux in aortic endothelial cells. Cardiovasc Res. 2007;75(3):575-583.
  55. Kuo CY, Lin YC, Yang JJ, et al. Interaction abolish- ment between mutant caveolin-1(Delta 62-100) and ABCA1 reduces HDL-mediated cellular cholesterol efflux. Biochem Biophys Res Commun. 2011;414 (2):337-343.
  56. Chroni A, Liu T, Fitzgerald ML, et al. Cross-linking and lipid efflux properties of apoA-I mutants suggest direct association between apoA-I helices and ABCA1. Biochemistry. 2004;43(7):2126-2139.
  57. Fitzgerald ML, Morris AL, Chroni A, et al. ABCA1 and amphipathic apolipoproteins form high-affinity mole- cular complexes required for cholesterol efflux. J Lipid Res. 2004;45(2):287-294.
  58. Yamauchi Y, Hayashi M, Abe-Dohmae S, et al. Apolipoprotein A-I activates protein kinase C alpha signaling to phosphorylate and stabilize ATP binding cassette transporter A1 for the high density lipopro- tein assembly. J Biol Chem. 2003;278 (48):47890-47897.
  59. Vedhachalam C, Ghering AB, Davidson WS, et al. ABCA1-induced cell surface binding sites for ApoA-I. Arterioscler Thromb Vasc Biol. 2007;27(7):1603-1609.
  60. Vedhachalam C, Duong PT, Nickel M, et al. Mechanism of ATP-binding cassette transporter A1-mediated cellular lipid efflux to apolipoprotein A-I and formation of high density lipoprotein particles. J Biol Chem. 2007;282(34):25123-25130.
  61. Lin G, Oram JF. Apolipoprotein binding to protruding membrane domains during removal of excess cellular cholesterol. Atherosclerosis. 2000;149(2):359-370.
  62. Iatan I, Bailey D, Ruel I, et al. Membrane microdo- mains modulate oligomeric ABCA1 function: impact on apoAI-mediated lipid removal and phosphatidyl- choline biosynthesis. J Lipid Res. 2011;52 (11):2043-2055.
  63. Tanaka M, Dhanasekaran P, Nguyen D, et al. Contributions of the N-and C-terminal helical seg- ments to the lipid-free structure and lipid interaction of apolipoprotein A-I. Biochemistry. 2006;45 (34):10351-10358.
  64. Duong PT, Collins HL, Nickel M, et al. Characterization of nascent HDL particles and micro- particles formed by ABCA1-mediated efflux of cellular lipids to apoA-I. J Lipid Res. 2006;47(4):832-843.
  65. Davidson WS, Hazlett T, Mantulin WW, et al. The role of apolipoprotein AI domains in lipid binding. Proc Natl Acad Sci U S A. 1996;93(24):13605-13610.
  66. Silva RA, Hilliard GM, Li L, et al. A mass spectrometric determination of the conformation of dimeric apolipo- protein A-I in discoidal high density lipoproteins. Biochemistry. 2005;44(24):8600-8607.
  67. Wang S, Gulshan K, Brubaker G, et al. ABCA1 med- iates unfolding of apolipoprotein AI N terminus on the cell surface before lipidation and release of nascent high-density lipoprotein. Arterioscler Thromb Vasc Biol. 2013;33(6):1197-1205.
  68. Mazhab-Jafari MT, Rohou A, Schmidt C, et al. Atomic model for the membrane-embedded VO motor of a eukaryotic V-ATPase. Nature. 2016;539 (7627):118-122.
  69. McGuire C, Stransky L, Cotter K, et al. Regulation of V-ATPase activity. Front Biosci (Landmark Ed). 2017;22(4):609-622.
  70. Xia Y, Liu N, and Xie X, et al. The macrophage-specific V-ATPase subunit ATP6V0D2 restricts inflammasome activation and bacterial infection by facilitating autophagosome-lysosome fusion. Autophagy. 2019;15 (6):960-975.
  71. Rao VK, Zavala G, Deb Roy A, et al. A pH-sensitive luminal His-cluster promotes interaction of PAM with V-ATPase along the secretory and endocytic pathways of peptidergic cells. J Cell Physiol. 2019;234 (6):8683-8697.
  72. Martins BX, Arruda RF, Costa GA, et al. Myrtenal- induced V-ATPase inhibition -A toxicity mechanism behind tumor cell death and suppressed migration and invasion in melanoma. Biochim Biophys Acta Gen Subj. 2019;1863:1-12.
  73. Fukuda M, Nakano M, Miyazaki M, et al. Conformational change of apolipoprotein A-I and HDL formation from model membranes under intra- cellular acidic conditions. J Lipid Res. 2008;49 (11):2419-2426.
  74. Nguyen SD, Oorni K, Lee-Rueckert M, et al. Spontaneous remodeling of HDL particles at acidic pH enhances their capacity to induce cholesterol efflux from human macrophage foam cells. J Lipid Res. 2012;53(10):2115-2125.
  75. Lorkowski SW, Brubaker G, Gulshan K, et al. V-ATPase (vacuolar ATPase) activity required for ABCA1 (ATP-binding cassette protein A1)-Mediated cholesterol efflux. Arterioscler Thromb Vasc Biol. 2018;38(11):2615-2625.
  76. Gursky O, Jones MK, Mei X, et al. Structural basis for distinct functions of the naturally occurring Cys mutants of human apolipoprotein A-I. J Lipid Res. 2013;54(12):3244-3257.
  77. Takahashi Y, Smith JD. Cholesterol efflux to apolipo- protein AI involves endocytosis and resecretion in a calcium-dependent pathway. Proc Natl Acad Sci U S A. 1999;96(20):11358-11363.
  78. Chen W, Sun Y, Welch C, et al. Preferential ATP-binding cassette transporter A1-mediated choles- terol efflux from late endosomes/lysosomes. J Biol Chem. 2001;276(47):43564-43569.
  79. Sorci-Thomas MG, Owen JS, Fulp B, et al. Nascent high density lipoproteins formed by ABCA1 resemble lipid rafts and are structurally organized by three apoA-I monomers. J Lipid Res. 2012;53(9):1890-1909.
  80. Pomorski T, Menon AK. Lipid flippases and their biological functions. Cell Mol Life Sci. 2006;63 (24):2908-2921.
  81. Mu L, Tu Z, Miao L, et al. A phosphatidylinositol 4,5-bisphosphate redistribution-based sensing mechan- ism initiates a phagocytosis programing. Nat Commun. 2018;9(1):4259.
  82. Walter AM, Muller R, and Tawfik B, et al. Phosphatidylinositol 4,5-bisphosphate optical uncaging potentiates exocytosis. Elife. 2017;6:e30203.
  83. Egea-Jimenez AL, Gallardo R, Garcia-Pino A, et al. Frizzled 7 and PIP2 binding by syntenin PDZ2 domain supports Frizzled 7 trafficking and signalling. Nat Commun. 2016;7(1):12101.
  84. Shi A, Grant BD. Interactions between Rab and Arf GTPases regulate endosomal phosphatidylinositol-4,5-bisphosphate during endocy- tic recycling. Small GTPases. 2013;4(2):106-109.
  85. Rohrbach TD, Shah N, Jackson WP, et al. The effector domain of marcks is a nuclear localization signal that regulates cellular PIP2 levels and nuclear PIP2 localization. PLoS One. 2015;10(10):e0140870.
  86. Gerber PP, Cabrini M, Jancic C, et al. Rab27a controls HIV-1 assembly by regulating plasma membrane levels of phosphatidylinositol 4,5-bisphosphate. J Cell Biol. 2015;209(3):435-452.
  87. Singaraja RR, Visscher H, James ER, et al. Specific mutations in ABCA1 have discrete effects on ABCA1 function and lipid phenotypes both in vivo and in vitro. Circ Res. 2006;99(4):389-397.
  88. Nagao K, Zhao Y, Takahashi K, et al. Sodium taurocholate-dependent lipid efflux by ABCA1: effects of W590S mutation on lipid translocation and apoli- poprotein A-I dissociation. J Lipid Res. 2009;50 (6):1165-1172.
  89. Gulshan K, Brubaker G, Wang S, et al. Sphingomyelin depletion impairs anionic phospholipid inward trans- location and induces cholesterol efflux. J Biol Chem. 2013;288(52):37166-37179.
  90. Gulshan K, Brubaker G, Conger H, et al. PI(4,5)P2 Is Translocated by ABCA1 to the Cell Surface Where It Mediates Apolipoprotein A1 Binding and Nascent HDL Assembly. Circ Res. 2016;119(7):827-838.
  91. Denis M, Haidar B, Marcil M, et al. Characterization of oligomeric human ATP binding cassette transporter A1. Potential implications for determining the struc- ture of nascent high density lipoprotein particles. J Biol Chem. 2004;279(40):41529-41536.
  92. Nagata KO, Nakada C, Kasai RS, et al. ABCA1 dimer-monomer interconversion during HDL gen- eration revealed by single-molecule imaging. Proc Natl Acad Sci U S A. 2013;110(13):5034-5039.
  93. Ishigami M, Ogasawara F, Nagao K, et al. Temporary sequestration of cholesterol and phosphatidylcholine within extracellular domains of ABCA1 during nascent HDL generation. Sci Rep. 2018;8(1):6170.
  94. Fitzgerald ML, Morris AL, Rhee JS, et al. Naturally occurring mutations in the largest extracellular loops of ABCA1 can disrupt its direct interaction with apo- lipoprotein A-I. J Biol Chem. 2002;277 (36):33178-33187.
  95. Oram JF, Lawn RM, Garvin MR, et al. ABCA1 is the cAMP-inducible apolipoprotein receptor that mediates cholesterol secretion from macrophages. J Biol Chem. 2000;275(44):34508-34511.
  96. Mei X, Atkinson D. Crystal structure of C-terminal truncated apolipoprotein A-I reveals the assembly of high density lipoprotein (HDL) by dimerization. J Biol Chem. 2011;286(44):38570-38582.
  97. Liu M, Mei X, Herscovitz H, et al. N-terminal mutation of apoA-I and interaction with ABCA1 reveal mechan- isms of nascent HDL biogenesis. J Lipid Res. 2019;60 (1):44-57.
  98. Rached FH, Chapman MJ, Kontush A. HDL particle subpopulations: focus on biological function. Biofactors. 2015;41(2):67-77.
  99. Mulya A, Lee JY, Gebre AK, et al. Minimal lipidation of pre-beta HDL by ABCA1 results in reduced ability to interact with ABCA1. Arterioscler Thromb Vasc Biol. 2007;27(8):1828-1836.
  100. Prospective Studies C, Lewington S, Whitlock G, et al. Blood cholesterol and vascular mortality by age, sex, and blood pressure: a meta-analysis of individual data from 61 prospective studies with 55,000 vascular deaths. Lancet. 2007;370:1829-1839.
  101. Du XM, Kim MJ, Hou L, et al. HDL particle size is a critical determinant of ABCA1-mediated macrophage cellular cholesterol export. Circ Res. 2015;116 (7):1133-1142.
  102. Mukherjee S, Zha X, Tabas I, et al. Cholesterol distri- bution in living cells: fluorescence imaging using dehy- droergosterol as a fluorescent cholesterol analog. Biophys J. 1998;75(4):1915-1925.
  103. Neufeld EB, Remaley AT, Demosky SJ, et al. Cellular localization and trafficking of the human ABCA1 transporter. J Biol Chem. 2001;276(29):27584-27590.
  104. Schmitz G, Robenek H, Lohmann U, et al. Interaction of high density lipoproteins with cholesteryl ester-laden macrophages: biochemical and morpholo- gical characterization of cell surface receptor binding, endocytosis and resecretion of high density lipopro- teins by macrophages. EMBO J. 1985;4(3):613-622.
  105. Azuma Y, Takada M, Shin HW, et al. Retroendocytosis pathway of ABCA1/apoA-I contributes to HDL formation. Genes Cells. 2009;14(2):191-204.
  106. Chen W, Wang N, Tall AR. A PEST deletion mutant of ABCA1 shows impaired internalization and defective cholesterol efflux from late endosomes. J Biol Chem. 2005;280(32):29277-29281.
  107. Faulkner LE, Panagotopulos SE, Johnson JD, et al. An analysis of the role of a retroendocytosis pathway in ABCA1-mediated cholesterol efflux from macrophages. J Lipid Res. 2008;49(6):1322-1332.
  108. Denis M, Landry YD, Zha X. ATP-binding cassette A1-mediated lipidation of apolipoprotein A-I occurs at the plasma membrane and not in the endocytic compartments. J Biol Chem. 2008;283(23):16178-16186.
  109. Oram JF. The ins and outs of ABCA. J Lipid Res. 2008;49:1150-1151.
  110. Lu R, Arakawa R, Ito-Osumi C, et al. ApoA-I facilitates ABCA1 recycle/accumulation to cell surface by inhibiting its intracellular degradation and increases HDL generation. Arterioscler Thromb Vasc Biol. 2008;28 (10):1820-1824.
  111. Mukhamedova N, Hoang A, Cui HL, et al. Small GTPase ARF6 regulates endocytic pathway leading to degradation of ATP-binding cassette transporter A1. Arterioscler Thromb Vasc Biol. 2016;36(12):2292-2303.
  112. Yu XH, Jiang N, Yao PB, et al. NPC1, intracellular cholesterol trafficking and atherosclerosis. Clin Chim Acta. 2014;429:69-75.
  113. Linder MD, Uronen RL, Holtta-Vuori M, et al. Rab8- dependent recycling promotes endosomal cholesterol removal in normal and sphingolipidosis cells. Mol Biol Cell. 2007;18(1):47-56.
  114. Linder MD, Mayranpaa MI, Peranen J, et al. Rab8 regulates ABCA1 cell surface expression and facilitates cholesterol efflux in primary human macrophages. Arterioscler Thromb Vasc Biol. 2009;29(6):883-888.
  115. Charollais J, Van Der Goot FG. Palmitoylation of membrane proteins (Review). Mol Membr Biol. 2009;26(1-2):55-66.
  116. Singaraja RR, Kang MH, Vaid K, et al. Palmitoylation of ATP-binding cassette transporter A1 is essential for its trafficking and function. Circ Res. 2009;105(2):138-147.

Cited by

Sorted by citations

Authors
Chen, L., Zhao, Z.-W., Zeng, P.-H., Zhou, Y.-J., & Yin, W.-J.
Affiliations
  • Hainan Medical University (CN)
  • University of South China (CN)
  • First Affiliated Hospital of University of South China (CN)
  • Department of Clinical Laboratory, The First Affiliated Hospital, Hengyang Medical School, University of South China, Hengyang, Hunan, China
Corresponding author
Yin, Wen-Jun
ORCID
Venue
Cell Cycle
Publisher
Informa UK Limited
Published
2022-02-22
Volume
21
Issue
11
Pages
1121-1139
ISSN
  • 1538-4101 (ISSN-L)
  • 1551-4005
DOI
10.1080/15384101.2022.2042777
PMC
PMC9103275
OpenAlex
W4212900905
Cited by
134
References
3
Citations by year
2026: 35 · 2025: 45 · 2024: 27 · 2023: 21 · 2022: 6
FWCI
5.88
Type
journal article
Language
en
Open access
Locations
  • Cell Cycle (publishedVersion)
  • PubMed Central (publishedVersion)
  • PubMed (publishedVersion)
Funders
  • This work was supported
  • National Natural Science Foundation of China (82103782)
Topics
  • Health Sciences › Medicine › Surgery › Cholesterol and Lipid Metabolism
  • Health Sciences › Medicine › Oncology › Drug Transport and Resistance Mechanisms
  • Health Sciences › Medicine › Surgery › Lipoproteins and Cardiovascular Health
Keywords
ABCA1, cholesterol efflux, cholesterol homeostasis, apolipoprotein A-I, HDL maturation, lecithin:cholesterol acyltransferase, cholesterol esters, free cholesterol, atherosclerosis, lipid-lowering therapy
MeSH terms
Biological Transport, Cholesterol, Phosphatidylcholine-Sterol O-Acyltransferase, Lipoproteins, HDL, Cholesterol, HDL, Apolipoprotein A-I, ATP Binding Cassette Transporter 1

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review