Cholesterol efflux from macrophages and other cells

Current Opinion in Lipidology

Volumn 7, Issue 5, 1996, Pages 308-319

  Von Eckardstein, Arnold ^a  

^a UNIVERSITY OF MÜNSTER   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

APOLIPOPROTEIN A1; APOLIPOPROTEIN E; CHOLESTEROL; CHOLESTEROL ACYLTRANSFERASE; CHOLESTEROL ESTERASE; HIGH DENSITY LIPOPROTEIN; PHOSPHATIDYLCHOLINE STEROL ACYLTRANSFERASE;

ATHEROSCLEROTIC PLAQUE; CELL MEMBRANE; CHOLESTEROL TRANSPORT; ESTERIFICATION; EXTRACELLULAR SPACE; FOAM CELL; GOLGI COMPLEX; LIPID STORAGE; MACROPHAGE; MONOCYTE; NONHUMAN; PRIORITY JOURNAL; REVIEW; SIGNAL TRANSDUCTION;

EID: 0029834032     PISSN: 09579672     EISSN: None     Source Type: Journal    
DOI: 10.1097/00041433-199610000-00009     Document Type: Review

References (122)

1. Libby P, Clinton SK: The role of macrophages in atherogenesis. Curr Opin Lipidol 1993, 4:355-363.
2. Tabas I: The stimulation of the cholesterol esterification pathway by atherogenic lipoproteins. Curr Opin Lipidol 1995, 6:260-268. An excellent review on trafficking and esterification of cholesterol in MΦs.
3. Liscum L, Dahl NK: Intracellular cholesterol transport. J Lipid Res 1992, 33:1239-1254.
4. Pentchev PG, Vanier MT, Suzuki K, Patterson MC: Niemann Pick disease type C: a cellular cholesterol lipoidosis. In The metabolic and molecular basis of inherited disease edn 7. Edited by Scriver C, Beaudet A, Sly W, Valle D. New York: McGraw-Hill; 1995:2625-2639. An excellent review of our current knowledge on Niemann-Pick disease type C that contains valuable information on intracellular cholesterol transport.
5. Myers JN, Tabas I, Jones NL, Maxfield FR: b-Very low density lipoprotein is sequestered in surface-connected tubules in mouse peritoneal macrophages. J Cell Biol 1993, 123:1389-1402.
6. Kruth HS, Skarlatos SI, Lilly K, Chang J, Ifrim I: Sequestration of acetylated LDL and cholesterol crystals by human monocyte-derived macrophages. J Cell Biol 1995, 129:133-145. Human monocyte-derived MΦs were observed to sequester cholesterol crystals and acetyl-LDL in cytosolic compartments that are connected with the plasma membrane without catabolizing this material by the endosomal-lysosomal route. From this compartment UC can be transferred to lysosomes, to cytosolic lipid droplets or, after removal of cholesterol from the medium, into the extracellular compartment. Interestingly, the surface-connected compartments also contain apoE. The authors hypothesize that sequestration enables MΦs to remove cholesterol for example from lipid cores and discharge it after having left the atherosclerotic plaque.
7. Huang Y, von Eckardstein A, Assmann G: Cell-derived unesterified cholesterol recycles between low density lipoproteins and different high density lipoproteins for its effective esterification. Arteriosclerosis Thromb 1993, 13:445-458.
8. 1Lp(AI). The authors also provide data that cholesterol is first interiorized into intracellular pools by a mechanism that is sensitive towards N-ethylmaleimide but insensitive, for example, towards progesterone. It is concluded that this pathway helps to equilibrate plasma membrane cholesterol levels against efflux and influx caused by HDL and LDL, respectively.
9. Uelmen P, Oka K, Sullivan M, Chang CCY, Chang TY, Chan L: Tissue specific expression and cholesterol regulation of acylcoenzyme A: cholesterol acyltransferase (ACAT) in mice. Molecular cloning of mouse ACAT cDNA, chromosomal localization, and regulation of ACAT in vivo and in vitro. J Biol Chem 1995, 270:26192-26201. Sequence and chromosomal localization of mouse ACAT complementary DNA as well as regulation of ACAT mRNA and ACAT activity are described. In-vitro ACAT and in-vivo ACAT was regulated by at least two distinct mechanisms. Fat feeding upregulated ACAT mRNA expression in the liver but not in MΦs, adrenals and intestine. Post-transcriptionally, ACAT activity was regulated by the availability of UC.
10. Tabas I, Zha X, Beatini N, Myers JN, Maxfield FR: The actin cytoskeleton is important for the stimulation of cholesterol esterification in macrophages. J Biol Chem 1994, 269:22547-22556.
11. Lange Y: Cholesterol movement from plasma membrane to rough endoplasmic reticulum. J Biol Chem 1994, 269:3411-3414.
12. Lange Y, Steck TL: Cholesterol homeostasis. Modulation by amphiphiles. J Biol Chem 1994, 269:29371-29374.
13. •] this study demonstrates that amphiphile steroids such as progesterone, estradiol, dehydroepiandrosterone sulphate and tamoxifen as well as some nonsteroidal amphiphiles inhibit cholesterol biosynthesis by inactivating multidrug resistance proteins. The authors suggest that multidrug resistance proteins regulate the transfer of UC and cholesterol precursor molecules to the ER for synthesis of CE and UC, respectively.
14. ••].
15. Brown MS, Ho YK, Goldstein JL: The cholesteryl ester cycle in macrophage foam cells. Continual hydrolysis and re-esterification of cytoplasmic cholesteryl esters. J Biol Chem 1980, 255:9344-9352.
16. Bernard D, Rodriguez A, Rothblat GH, Glick, JM: cAMP stimulates cholesteryl ester clearance to high density lipoproteins in J774 macrophages. J Biol Chem 1991, 266:710-716.
17. ••,15]).
18. Warner GJ, Stoudt G, Bamberger M, Jonson WJ, Rothblat GH: Cell toxicity induced by inhibition of acyl coenzyme A:cholesterol acyltransferase and accumulation of unesterified cholesterol. J Biol Chem 1995, 270:5772-5778. Inhibition of ACAT led to an increase of UC in PMΦs that was cytotoxic. Accumulation of UC and cytotoxicity by ACAT-inhibition were prevented by the presence of reconstituted HDL.
19. Johnson WJ, Mahlberg FH, Rothblat GH, Phillips MC: Cholesterol transport between cells and high density lipoproteins. Biochim Biophys Acta 1991, 1085:273-298.
20. Rothblat GH, Mahlberg FH, Johnson WJ, Phillips MC: Apolipoproteins, membrane cholesterol domains, and the regulation of cholesterol efflux. J Lipid Res 1992, 33:1091-1097.
21. Fielding C, Fielding PE: Molecular physiology of reverse cholesterol transport. J Lipid Res 1995, 36:211-228. An excellent review on the heterogeneity of HDL, mechanisms of cholesterol efflux, and processing of cell-derived cholesterol in the plasma compartment.
22. Assmann G, von Eckardstein A, Brewer HB Jr: Familial high density lipoprotein deficiency: Tangier disease. In The metabolic and molecular basis of inherited disease edn 7. Edited by Scriver C, Beaudet A, Sly W, Valle D. New York: McGraw-Hill; 1995: 2053-2072. This review summarizes the clinical, pathological, biochemical and genetic presentation of TD as well as the regulation of cellular cholesterol homeostasis by HDL.
23. ++ antagonists and ACAT-inhibitors promote cholesterol efflux from macrophages by different mechanisms. I. Characterization of cellular lipid metabolism. Arteriosclerosis 1988, 8:46-56.
24. Kruth HS, Skarlatos SI, Gaynor PM, Gamble W: Production of cholesterol-enriched nascent high density lipoproteins by human monocyte-derived macrophages is a mechanism that contributes to macrophage cholesterol efflux. J Biol Chem 1994, 269:24511-24518.
25. Kawano M, Miida T, Fielding CJ, Fielding PE: Quantitation of preβ-HDL-dependent and nonspecific components of the total efflux of cellular cholesterol and phospholipid. Biochemistry 1993, 32:5025-5028.
26. Huang Y, von Eckardstein A, Wu S, Maeda N, Assmann G: A solely apolipoprotein E containing plasma lipoprotein with electrophoretic gamma-mobility takes up cellular cholesterol. Proc Natl Acad Sci U S A 1994, 91:1834-1838.
27. 3H]UC was released into plasmas of apoE2/2 and apoE4/4 individuals as compared with plasmas of apoE3/3 individuals.
28. 1Lp(AI), also esterify cholesterol.
29. 1Lp(AI) and LDL accounted for this considerable residual cholesterol efflux capacity of HDL-deficient plasmas.
30. Smart EJ, Ying Y-S, Conrad PA, Anderson RGW: Caveolin moves from caveolae to the Golgi apparatus in response to cholesterol oxidation. J Cell Biol 1994, 127:1185-1197
31. Fielding PE, Fielding C: Plasma membrane caveolae mediate the efflux of cellular free cholesterol. Biochemistry 1995, 34:14288-14292 Evidence is provided that caveolae represent plasma membrane domains that serve as both preferred acceptors of LDL-derived and biosynthetic UC and donors of UC to extracellular acceptors.
32. Davidson WS, Rodriguez WV, Lund-Katz S, Johnson WJ, Rothblat GH, Phillips MC: Effects of acceptor particle size on the efflux of cellular free cholesterol. J Biol Chem 1995, 270:17106-17113.
33. Kilsdonk EPC, Yancey PG, Stoudt GW, Bangerter FW, Johnson WJ, Phillips MC, Rothblat GH: Cellular cholesterol efflux mediated by cyclodextrins. J Biol Chem 1995, 270:17250-17256. Cyclodextrins very effectively but unselectively promoted cholesterol efflux from various cells. The authors suggest that cyclodextrins may serve as antiatherogenic pharmacological agents.
34. Davidson WS, Gillotte KL, Lund-Katz S, Johnson WJ, Rothblat GH, Phillips MC: Effects of acceptor particle size on the efflux of cellular free cholesterol. J Biol Chem 1995, 270:5882-5890. Desaturation and length of fatty acid chains in phospholipids influenced the fluidity of reconstituted HDL and thereby the conformation of apoA-I. Increasing the fluidity by decreasing length and saturation of fatty acid chains enhanced the cholesterol efflux capacity of reconstituted HDL.
35. 3. Arterioscler Thromb 1993, 13:958-966.
36. Bonnefont-Rousselot D, Motta C, Khalil AO, Sola R, La Ville AE, Delattre J, Gardès-Albert M: Physicochemical changes in human high density lipoproteins (HDL) oxidized by gamma radiolysis-generated oxyradicals. Effect on their cholesterol efflux capacity. Biochim Biophys Acta 1995, 1255:23-30.
37. Rifici VA, Khachadurian AK: Oxidation of high density lipoproteins. Characterization and effects of cholesterol efflux from J774 macrophages. Biochim Biophys Acta 1995, 1299:87-94.
38. LaVille AE, Sola R, Balanya J, Turner PR, Masana L: In vitro oxidized HDL is recognised by the scavenger receptor of macrophages: implications for its protective role in vivo. Atherosclerosis 1994, 105:179-189
39. Fruchart JC, Ailhaud G: Apolipoprotein A-containing particles: physiological role, quantification and clinical significance. Clin Chem 1992, 38:793-797.
40. Barbaras R, Puchois P, Fruchart JC, Ailhaud G: Cholesterol efflux from cultured adipose cells is mediated by LpAI particles but not by LpAI:AII particles. Biochem Biophys Res Commun 1987, 142:63-69.
41. Johnson WJ, Kilsdonk EPG, van Tol A, Phillips MC, Rothblat GH: Cholesterol efflux from cells to immunopurified subfractions of human high density lipoprotein: LpA-I and LpA-I:A-II. J Lipid Res 1991, 1992-2000.
42. Oikawa S, Mendez AJ, Oram JF, Bierman EL, Cheung MC: Effects of high density lipoprotein particles containing apoA-I, with or without apoA-II, on intracellular cholesterol efflux. Biochim Biophys Acta 1993, 1165: 327-334.
43. Stein O, Dabach Y, Hollander G, Bennaim M, Oette K, Stein Y: Effects of interactions of apolipoprotein A-II with apolipoproteins A-I and A-IV of (H-3)cholesterol efflux and uptake in cell culture. Biochim Biophys Acta 1992, 1257:174-180
44. Ohta T, Nakamura R, Ikeda Y, Shinohara M, Miyazaki A, Horiuchi S, Matsuda I: Differential effect of subspecies of lipoprotein containing apolipoprotein A-I on cholesterol efflux from cholesterol-loaded macrophages. Functional correlation with lecithin:cholesterol acyltransferase. Biochim Biophys Acta 1992, 1165:119-128.
45. von Hodenberg E, Heinen S, Howell KE, Luley C, Kübler W, Bond HM: Cholesterol efflux from macrophages mediated by high density lipoprotein subfractions which differ principally in apolipoprotein A-I and A-II ratios. Biochim Biophys Acta 1992, 1086:173-184.
46. Skarlatos SI, Duverger N, Rader D, Kruth HS: Cholesterol efflux from human monocyte-derived macrophages in the presence of LpA-I:A-II. Biochim Biophys Acta 1995, 1270:19-25.
47. Ohta T, Saku K, Takata K, Nakamura R, Ikeda Y, Matsuda I: Different effects of subclasses of HDL containg apo A-I but not apoA-II (LpA-I) on cholesterol esterifcation in plasma and cholesterol efflux from foam cells. Arterioscler Thromb Vasc Biol 1995, 15:956-962. Only small and intermediate size Lp(AI) were found effective in promoting net cholesterol efflux from rat MΦ foam cells.
48. Huang Y, von Eckardstein A, Wu S, Assmann G: Role of LpA-I and LpA-I/ A-II for cholesterol efflux and esterification as analysed by immunosubtracting nondenaturing two-dimensional electrophoresis. Arterioscler Thromb Vasc Biol 1995, 15:1412-1418. This study demonstrated in native plasma that Lp(AI) takes up and esterifies cell-derived UC more effectively than does Lp(AI-AII).
49. de la Llera Moya M, Atger V, Paul JL, Fournier N, Moatti N, Giral P, Friday KE, Rothblat GH: A cell culture system for screening human serum for ability to promote cellular cholesterol efflux. Arterioscler Thromb 1994, 14: 1056-1065.
50. Lagrost L, Dengremont C, Athias A, de Geitere C, Fruchart JC, Lallemant C, Gambert C, Castro G: Modulation of cholesterol efflux from Fu5AH hepatoma cells by the apolipoprotein content of high density lipoprotein particles. J Biol Chem 1995, 270:13004-13009. Stepwise substitution of apoA-I with apoA-II decreased the ability of HDL to remove radiolabeled UC from rat hepatocytes. Since this procedure did not change particle size, the authors conclude that the ratio apoA-I:apoA-II is one determinant of the ability of HDL to promote cholesterol efflux.
51. Bernini F, Calabresi L, Bonfadini G, Franceschini G: The molecular structure of apolipoprotein A-II modulates the capacity of HDL to promote cholesterol efflux. Biochim Biophys Acta 1996, 1299:19-25.
52. Hara H, Yokoyama S: Interaction of free apolipoproteins with macrophages: formation of high density lipoprotein-like lipoproteins and reduction of cellular cholesterol. J Biol Chem 1991, 266:3080-3086
53. Bielicki JK, Johnson WJ, Weinberg RB, Glick JM, Rothblat GM: Efflux of lipid from fibroblasts to apolipoproteins: dependence on elevated levels of cellular unesterified cholesterol. J Lipid Res 1992, 33:1699-1709.
54. Mendez AJ, Anantharamaiah GM, Segrest JP, Oram JF: Synthetic amphipathic helical peptides that mimic apolipoprotein A-I in clearing cellular cholesterol. J Clin Invest 1994, 94:1698-1705.
55. Yancey PG, Bielicki JK, Johnson WJ, Lund-Katz S, Palgunachari MN, Anantharamaiah GM, Segrest JP, Phillips MC, Rothblat GH: Efflux of cellular cholesterol and phospholipid to lipid-free apolipoproteins and class A amphipathic peptides. Biochemistry 1995, 34:7955-7965. Enrichment of MΦs with cholesterol increased efflux of cholesterol and phospholipids to lipid-free apoA-I. At equivalent protein concentrations apoA-I was more effective than HDL. Efflux of both phospholipid and cholesterol was also achieved with amphipathic peptides which had no sequence homology to apoA-I.
56. Li Q, Komaba A, Yokoyama S: Cholesterol is poorly available for apolipoprotein-mediated cellular lipid efflux from smooth muscle cells. Biochemistry 1993, 32:4597-4603.
57. Czarnecka H, Yokoyama S: Regulation of cellular cholesterol efflux by lecithin:cholesterol acyltransferase reaction through nonspecific lipid exchange. J Biol Chem 1996, 266:2023-2028. HDL but not lipid-free apoA-I promotes cholesterol efflux from erythrocytes. However, in the absence of LCAT no net transfer of cholesterol took place between HDL and cells. In the presence of LCAT this equilibrium was changed to efflux.
58. Li Q, Yokoyama S: Independent regulation of cholesterol incorporation into free apolipoprotein-mediated cellular lipid efflux in rat vascular smooth muscle cells. J Biol Chem 1995, 269:26216-26223. Lipid-free apoA-I did not promote cholesterol efflux from native SMCs but from SMC-derived foam cells that were pretreated with cytokines and growth factors. Efflux could be inhibited with protein kinase C inhibitors. The authors conclude that interaction of apoA-I activates intracellular cholesterol translocation in some cells.
59. Forte TM, Goth-Goldstein R, Nordhausen RW, McCall MR: Apolipoprotein A-I-cell membrane interaction: extracellular assembly of heterogeneous nascent HDL particles J Lipid Res 1993, 34:317-324
60. 1Lp(AI) which was converted into αLp(AI) by normal plasma but not by plasma of TD patients.
61. •]). The authors concluded that unidirectional cholesterol efflux takes place in the presence of lipid-free apoA-I but bidirectional flux in the presence of HDL The latter is changed to net efflux by LCAT.
62. Asztalos BF, Sloop CH, Wong L, Roheim PS: Comparison of apoA-I containing subpopulations of dog plasma and perinodal lymph: evidence for alteration in subpopulations in the interstitial space. Biochim Biophys Acta 1993, 1169:301-304.
63. Liang H-Q, Rye K-A, Barter PJ: Dissociation of lipid-free apolipoprotein A-I from high density lipoproteins. J Lipid Res 1994, 35:1187-1194.
64. Hennessy LK, Kunitake ST, Kane JP: Apolipoprotein A-I-containing lipoproteins, with or without apolipoprotein A-II, as progenitors of preβ-high density lipoprotein particles. Biochemistry 1993, 32:5759-5765.
65. 3. This conversion was associated with increased plasma activity to promote cholesterol efflux from fibroblasts.
66. Johnson WJ, Chacko GK, Phillips MC, Rothblat GH: The efflux of lysosomal cholesterol from cells. J Biol Chem 1990, 265:5546-5553.
67. Johnson WJ, Fischer RT, Phillips MC, Rothblat GH: Efflux of newly synthesized cholesterol and biosynthetic sterol intermediates from cells. Dependence on acceptor type and enrichment of cells with cholesterol. J Biol Chem 1995, 270:25037-25046. HDL and phospholipid vesicles mediated efflux of biosynthetic cholesterol precursors and cholesterol from various cells. Desmosterol was the major sterol released by the cells. HDL-mediated efflux was specific for biosynthetic cholesterol but not for desmosterol and lysosomal cholesterol. The authors conclude a minor contribution of HDL-specific effects on sterol efflux.
68. Oram JF, Mendez AJ, Slotte JP, Johnson TF: High density lipoproteins mediate removal of sterol from intracellular pools but not from plasma membranes of cholesterol loaded fibroblasts. Arterioscler Thromb 1991, 11:403-414.
69. Mendez AJ, Oram JF, Bierman EL: Protein kinase C as a mediator of high density lipoprotein dependent efflux of intracellular cholesterol. J Biol Chem 1991, 266:10104-10111.
70. 3 stimulates multiple signaling pathways in human skin fibroblasts. Arterioscler Thromb Vasc Biol 1995, 15:1975-1986. This study demonstrates that HDL mediates breakdown of PC and PI by multiple phospholipases. Since PC-specific phospholipase D but not PC-specific phospholipase C was activated by apoA-I and apoA-II and induced by loading with cholesterol, it was concluded that more than one agonist is involved in HDL-induced signal transduction.
71. Mendez AJ: Monensin and brefeldin A inhibit high density lipoprotein mediated cholesterol efflux from cholesterol-enriched cells. Implications for intracellular cholesterol trafficking. J Biol Chem 1995, 270:5891-5900. HDL-mediated cholesterol efflux from fibroblasts and SMC was inhibited by monensin and brefeldin A, suggesting that the Golgi apparatus is involved in the transfer of UC between intracellular pools and plasma membrane.
72. Walter M, Gerdes U, Seedorf U, Assmann G: The high density lipoprotein- and apolipoprotein A-I-induced mobilization of cellular cholesterol is impaired in fibroblasts from Tangier disease subjects. Biochem Biophys Res Commun 1994, 205:850-856.
73. ••]).
74. •]).
75. 3- and LDL-mediated generation of inositol phosphates and DAG from PI phosphate was found to be disturbed in TD fibroblasts. The authors assume that lipoproteins fail to activate PI-specific phospholipase C properly in TD cells.
76. McKnight GL, Reasoner J, Gilbert T, Sundquist KO, Hokland BM, McKernan PA, Champagne J, Johnson CJ, Bailey MC, Holly R, Oram J: Cloning and expression of a cellular high density lipoprotein binding protein that is upregulated by cholesterol loading of cells. J Biol Chem 1992, 267: 12131-12141.
77. Acton S, Rigotti A, Landschulz KT, Xu S, Hobbs HH, Krieger M: Identification of scavenger receptor SR-B1 as a high density lipoprotein receptor. Science 1996, 271:518-520 The scavenger receptor SR-B1 was identified as an HDL-binding protein on hepatic and steroidogenic cells that mediates selective uptake of CE without internalization of the entire particle.
78. Koller E, Koller FM, Binder BR: Purification and identification of the lipoprotein binding proteins from human blood platelet membrane. J Biol Chem 1989, 264:12414-12418.
79. 3 activates phospholipase D in normal but not in glycoprotein IIb/IIIa-deficient platelets. Biochem Biophys Res Commun 1995, 207:148-154. HDL did not activate phospholipase D in glycoprotein IIb/IIIa deficient platelets of patients with Glanzmann thrombasthenia, suggesting that glycoprotein IIb/IIIa serves as a signal-transducing HDL-binding protein on platelets.
80. 3 modulates platelet aggregation by activation of protein kinase C [Abstract]. Circulation 1993, 88:457.
81. Luchoomun J, Theret N, Clavey V, Duchateau P, Rosseneu M, Brasseur R, Denefle P, Fruchart JC, Castro GR: Structural domain of apolipoprotein A-I involved in its interaction with cells. Biochim Biophys Acta 1994, 1212:319-326.
82. Fielding PE, Kawano M, Catapano AL, Zoppo A, Marcovina S, Fielding CJ: Unique epitope of apolipoprotein A-I expressed in preβ1-high density lipoprotein and its role in the catalyzed efflux of cellular cholesterol. Biochemistry 1994, 33:6981-6985.
83. Sviridov D, Pyle L, Fidge N: Identification of a sequence in apolipoprotein A-I associated with the efflux of intracellular cholesterol to human species and apolipoprotein A-I containing particles. Biochemistry 1996, 35:189-196. Two monoclonal anti-apoA-I antibodies are described that inhibit efflux of intracellular cholesterol from hepatocytes mediated by serum, native and reconstituted HDL, and lipid-free apoA-I.
84. 165→Arg). J Biol Chem 1993, 268:2616-2622.
85. Banka CL, Black AS, Curtiss LK: Localization of an apolipoprotein A-I epitope critical for lipoprotein-mediated cholesterol efflux from monocytic cells. J Biol Chem 1994, 269:10288-10297.
86. Brouilette CG, Anantharamaiah GM: Structural models of human apolipoprotein A-I. Biochim Biophys Acta 1995, 1256:103-129. An extensive review on the structure of apoA-I.
87. Holvoet P, Zhao Z, Vanloo B, Vos R, Deridder E, Dhoest A, Taveirne J, Brouwers E, Demarsin E, Engelborghs Y et al. Phospholipid binding and lecithin:cholesterol acyltransferase activation properties of apolipoprotein A-I variants. Biochemistry 1995, 34:13334-13342.
88. Jonas A, von Eckardstein A, Kezdy KE, Steinmetz A, Assmann G: Structural and functional properties of reconstituted high density lipoprotein discs prepared with six apolipoprotein A-I variants. J Lipid Res 1991, 32:97-106.
89. Hakamata H, Miyazaki A, Sakai M, Suginohara Y, Sakamato Y-I, Horiuchi S: Species difference in cholesteryl ester cycle and HDL-induced cholesterol efflux from macrophage foam cells. Arterioscler Thromb 1994, 14:1860-1865
90. Mathur SN, Field FJ, Megan MB, Armstrong ML: A defect in mobilization of cholesteryl esters in rabbit macrophages. Biochim Biophys Acta 1985, 834:48-57
91. Pitas RE, Innerarity TL, Mahley RW: Foam cells in explants of atherosclerotic rabbit aortas have receptors for β-VLDL and modified LDL. Arteriosclerosis 1983, 3:2-12
92. Yancey PG, St Clair RW: Cholesterol efflux is defective in macrophages from atherosclerosis susceptible White Carneau pigeons relative to resistant Show Racer pigeons. Arterioscler Thromb 1992, 12:1291-1304
93. Miyazaki A, Rahim ATMA, Ohta T, Morino Y, Horiuchi S: High density lipoproteins mediates selective reduction in cholesteryl esters from macrophage foam cells. Biochim Biophys Acta 1992, 1126:73-80.
94. Ho YK, Brown MS, Goldstein JL: Hydrolysis and excretion of cytoplasmic cholesteryl esters by macrophages: stimulation by high sensity lipoproteins and other agents. J Lipid Res 1980, 21:391-398
95. Hakamata H, Miyazaki A, Sakai M, Sakamato Y-I, Matsuda H, Kihara K, Horiuchi S: Differential effects of an acyl-coenzyme A:acyltransferase inhibitor on HDL-induced cholesterol efflux from rat macrophage foam cells. FEBS Lett 1995, 363:29-32
96. Yancey PG, St Clair RW: Mechanism of the defect in cholesteryl ester clearance from macrophages of atherosclerosis susceptible White Carneau pigeons. J Lipid Res 1994, 35:2114-2129.
97. Ishii I, Ito Y, Morisaki N, Saito Y, Hirose S: Genetic differences of lipid metabolism in macrophages from C57BL/6J and C3H/HeN mice. Arterioscler Thromb Vasc Biol 1995, 15:1189-1194 MΦs of C57BL/6J mice had lower NCEH activity and higher ACAT activity than did MΦs of C3H/HeN mice. Moreover, cholesterol feeding increased ACAT activity in MΦs of C57BL/6J mice but not in MΦs of C3H/HeN mice. These differences were suggested to explain the higher susceptibility to atherosclerosis of C57BL/6J mice.
98. Rosenfeld ME, Butler S, Ord VA, Lipton A, Dyer CA, Curtiss LA, Palinski W, Witztum JL: Abundant expression of apoprotein E by macrophages in human and rabbit atherosclerotic lesions. Arterioscler Thromb 1993, 13:1382-1389.
99. Basu S, Brown MS, Ho K, Havel RJ, Goldstein JL: Mouse macrophages synthesize and secrete a protein resembling apolipoprotein E. Proc Natl Acad Sci U S A 1981, 78:11657-11662.
100. Mazzone TL, Gump H, Diller P, Getz GS: Macrophage free cholesterol content regulates apolipoprotein E synthesis. J Biol Chem 1987, 262:11657-11662.
101. Mazzone T, Bassheerudin K, Poulos C: Regulation of macrophage apolipoprotein E gene expression by cholesterol. J Lipid Res 1989, 30: 1055-1064.
102. Mazzone T, Bassheerudin K: Dissociated regulation of macrophage low density receptor and apolipoprotein E gene expression by sterol. J Lipid Res 1991, 32:507-514.
103. Zuckerman SH, Evans GF, O'Neal J: Cytokine regulation of macrophage apoE secretion: opposin effects of GM-CSF and TGF-β. Atherosclerosis 1992, 96:203-214.
104. Clinton SK, Underwood R, Hayes L, Shermann ML, Kufe DW, Libby P: Macrophage colony stimulating factor gene expression in vascular cells and in experimental human atherosclerosis. Am J Pathol 1992, 140:301-316
105. Menju M, Tajima S, Yamammoto A: Expression of the apolipoprotein E gene in a human macrophage-like cell line. J Biochem 1989, 106:505-510.
106. Duan H, Li Z, Mazzone T: Tumor necrosis factor-a modulates monocyte/ macrophage apoprotein E gene expression. J Clin Invest 1995, 96: 915-922. Tumor necrosis factor alpha stimulated apoE mRNA expression and protein synthesis in human monocytes and THP-1 cells but not in fully differentiated human monocyte-derived MΦs. This effect could be inhibited by protein kinase C antagonists.
107. Basu SK, Ho Y, Brown MS, Bilheimer DW, Anderson RGW, Goldstein JL: Biochemical and genetic studies of the apoprotein E secreted by mouse macrophages and human monocytes. J Biol Chem 1982, 257:9788-9795.
108. Dory L: Synthesis and secretion of apo E in thioglycolate-elicited mouse peritoneal macrophages: effect of cholesterol efflux. J Lipid Res 1989, 30:809-816
109. Herscovitz H, Gantz D, Terycak AM, Zannis VI, Small DM: Expression of human apolipoprotein E but not apolipoprotein A-I by mouse C127 cells is associated with increased secretion of lipids in the form of vesicles and discs. J Lipid Res 1992, 33:791-803
110. Hayek T, Oiknine J, Brook JG, Aviram M: Role of HDL apolipoprotein E in cellular cholesterol efflux: studies in apoE knockout transgenic mice. Biochem Biophys Res Commun 1994, 205:1072-1078.
111. 3. J Lipid Res 1994, 35:1345-1353.
112. Basu S, Goldstein JL, Brown MS: Independent pathways for secretion of free cholesterol and apolipoprotein E by macrophages. Science 1983, 219:871-873.
113. 3 to promote cholesterol efflux from (apoE-deficient) J-774 MΦs. The authors conclude that endogenous apoE regulates cholesterol efflux from MΦs.
114. ++ Antagonists and ACAT-inhibitors promote cholesterol efflux from macrophages by different mechanisms. II. Characterization of intracellular morphologic changes. Arteriosclerosis 1988, 8:57-67
115. Yamada N, Inoue I, Kawamura M, Harada M, Watanabe Y, Shimano H, Gotoda T, Shimada M, Kohzaki M, Tsukada T et al.: Apolipoprotein E prevents the progression of atherosclerosis in Watanabe heritable hyperlipidemic rabbits. J Clin Invest 1992, 89:706-711.
116. Shimano H, Ohsuga J, Shimada M, Namba Y, Gotoda T, Harada Y, Katsuki M, Yazaki Y, Yamada N: Inhibition of diet-induced atheroma formation in transgenic mice expressing apolipoprotein E in the arterial wall. J Clin Invest 1995, 95:469-476. ApoE was overexpressed selectively in arterial wall cells of atherosclerosis-susceptible mice. After feeding of an atherogenic cholesterol-rich diet these mice developed signifcantly less fatty streaks than did control mice, although plasma lipid levels did not differ.
117. Bellosta S, Mahley RW, Sanan DA, Newland DL, Taylor JM, Pitas RE: Macrophage-specific expression of human apolipoprotein E reduces atherosclerosis in hypercholesterolemic apolipoprotein E-null mice. J Clin Invest 1995, 96:2170-2179. Human apoE was selectively expressed in MΦs of mice. These mice were bred with apoE-deficient mice to obtain mice that are hemizygous for apoE-expression in MΦs. These mice had hyperlipidemia indistinguishable from apoE-deficient mice, which did not produce apoE in MΦs. Nevertheless, mice hemizygous for apoE-expression in MΦs developed less severe atherosclerotic lesions.
118. Kritharides L, Jessup W, Mander EL, Dean RT: Apolipoprotein A-I-mediated efflux of sterols from oxidized LDL loaded macrophages. Arterioscler Thromb Vasc Biol 1995, 15:276-289. Loading of mouse PMΦs with oxidized LDL led to less pronounced accumulation of sterols than loading with acetyl-LDL. However, cholesterol and oxyslerols in MΦs loaded with oxidized LDL were more resistant towards apoA-I-induced efflux.
119. Kilsdonk EPC, Morel DW, Johnson WJ, Rothblat GH: Inhibition of cellular cholesterol efflux by 25-hydroxycholesterol. J Lipid Res 1995, 36: 505-516. 25-Hydroxycholesterol and other oxysterols inhibited cholesterol efflux from various cells. Since inhibition of efflux was observed in the presence of different acceptor particles and also from isolated plasma membranes, disturbed efflux is partially explained by disturbed efflux of membrane cholesterol.
120. Björkhem I, Andersson O, Diczfalusy U, Sevastik B, Xiu R-J, Duan C, Lund E: Atherosclerosis and sterol 27-hydroxylase: evidence for a role of this enzyme in elimination of cholesterol from human macrophages. Proc Natl Acad Sci U S A 1994, 91:8592-8596.
121. Björkhem I, Boberg KM: Inborn errors in bile acid biosynthesis and storage of sterols other than cholesterol. In The metabolic and molecular basis of inherited disease edn 7. Edited by Scriver C, Beaudet A, Sly W, Valle D. New York: McGraw-Hill; 1995, 2073-2099. An excellent review on normal and disturbed metabolism of bile acids and phytosterols.
122. Small DA, Goodacre JA, Yeaman SJ: Hormone sensitive lipase is responsible for the neutral cholesteryl ester hydrolase activity in macrophages. FEBS Lett 1989, 247:205-210.