Direct evidence for cholesterol crystalline domains in biological membranes: Role in human pathobiology

Biochimica et Biophysica Acta - Biomembranes

Volumn 1610, Issue 2, 2003, Pages 198-207

  Mason, R Preston ^a,c   Tulenko, Thomas N ^b   Jacob, Robert F ^a  

^a BRIGHAM AND WOMEN S HOSPITAL   (United States)

^b LANKENAU INSTITUTE FOR MEDICAL RESEARCH   (United States)

^c ELUCIDA RESEARCH LLC   (United States)

Author keywords

Atherosclerosis; Cholesterol; Domain; Lens; Lipid; Membrane

Indexed keywords

CHOLESTEROL;

AORTA ATHEROSCLEROSIS; ARTERY MUSCLE; BILAYER MEMBRANE; CELL CULTURE; CELL DIVISION; CELL FUNCTION; CELL MATURATION; CELL MEMBRANE; CELL MEMBRANE PERMEABILITY; CELL TYPE; FOAM CELL; HUMAN; ION TRANSPORT; LENS FIBER; MACROPHAGE; MEMBRANE STRUCTURE; NONHUMAN; PRIORITY JOURNAL; REVIEW; SMOOTH MUSCLE FIBER; STRUCTURE ANALYSIS; X RAY DIFFRACTION;

ANIMALIA; MAMMALIA;

EID: 0347572922     PISSN: 00052736     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0005-2736(03)00018-X     Document Type: Review

References (69)

1. Leonard A., Dufourc E.J. Interactions of cholesterol with the membrane lipid matrix. A solid state NMR approach. Biochimie. 73:1991;1295-1302.
2. Yeagle P.L. Cholesterol and the cell membrane. Biochim. Biophys. Acta. 822:1985;267-287.
3. Chen M., Mason R.P., Tulenko T.N. Atherosclerosis alters the composition, structure and function of arterial smooth muscle cell plasma membranes. Biochim. Biophys. Acta. 1272:1995;101-112.
4. McIntosh T.J. The effect of cholesterol on the structure of phosphatidylcholine bilayers. Biochim. Biophys. Acta. 513:1978;43-58.
5. Franks N.P. Structural analysis of hydrated egg lecithin and cholesterol bilayers: I. X-ray diffraction. J. Mol. Biol. 100:1976;345-358.
6. Shinitzky M., Inbar M. Microviscosity parameters and protein mobility in biological membranes. Biochim. Biophys. Acta. 433:1976;133-149.
7. Small D.M. Progression and regression of atherosclerotic lesions. Insights from lipid physical biochemistry. Arteriosclerosis. 8:1988;103-129.
8. Kellner-Weibel G., Yancey P.G., Jerome W.G., Walser T., Mason R.P., Phillips M.C., Rothblat G.H. Crystallization of free cholesterol in model macrophage foam cells. Arterioscler. Thromb. Vasc. Biol. 19:1999;1891-1898.
9. Tulenko T.N., Chen M., Mason P.E., Mason R.P. Physical effects of cholesterol on arterial smooth muscle membranes: evidence of immiscible cholesterol domains and alterations in bilayer width during atherogenesis. J. Lipid Res. 39:1998;947-956.
10. Ruocco M.J., Shipley G.G. Interaction of cholesterol with galactocerebroside and galactocerebroside-phosphatidylcholine bilayer membranes. Biophys. J. 46:1984;695-707.
11. Bach D., Borochov N., Wachtel E. Phase separation of cholesterol in dimyristoyl phosphatidylserine cholesterol mixtures. Chem. Phys. Lipids. 92:1998;71-77.
12. Katz S.S., Small D.M., Smith F.R., Dell R.B., Goodman D.S. Cholesterol turnover in lipid phases of human atherosclerotic plaque. J. Lipid Res. 23:1982;733-737.
13. Rafferty N.S. Maisel H. The Ocular Lens. 1985;1-60 Marcel Dekker, New York, NY.
14. Li L.K., So L., Spector A. Membrane cholesterol and phospholipid in consecutive concentric sections of human lenses. J. Lipid Res. 26:1985;600-609.
15. Li L.K., So L., Spector A. Age-dependent changes in the distribution and concentration of human lens cholesterol and phospholipids. Biochim. Biophys. Acta. 917:1987;112-120.
16. Broekhuyse R.M., Soeting W.J. Lipids in tissues of the eye: XV. Essential fatty acids in lens lipids. Exp. Eye Res. 22:1976;653-657.
17. Byrdwell W.C., Borchman D., Porter R.A., Taylor K.G., Yappert M.C. Separation and characterization of the unknown phospholipid in human lens membranes. Investig. Ophthalmol. Vis. Sci. 35:1994;4333-4343.
18. Byrdwell W.C., Borchman D. Liquid chromatography/mass-spectrometric characterization of sphingomyelin and dihydrosphingomyelin of human lens membranes. Ophthalmic Res. 29:1997;191-206.
19. Franks N.P., Levine Y.K. Low-angle X-ray diffraction. Mol. Biol. Biochem. Biophys. 31:1981;437-487.
20. Blaurock A.E. Evidence of bilayer structure and of membrane interactions from X-ray diffraction analysis. Biochim. Biophys. Acta. 650:1982;167-207.
21. Blaurock A.E. Structure of the nerve myelin membrane: proof of the low-resolution profile. J. Mol. Biol. 56:1971;35-52.
22. Moody M.F. X-ray diffraction pattern of nerve myelin: a method for determining the phases. Science. 142:1963;1173-1174.
23. Blaurock A.E., Wilkins M.H. Structure of retinal photoreceptor membranes. Nature. 236:1972;313-314.
24. Corless J.M. Lamellar structure of bleached and unbleached rod photoreceptor membranes. Nature. 237:1972;229-231.
25. Knutton S., Finean J.B., Coleman R., Limbrick A.R. Low-angle X-ray diffraction and electronmicroscope studies of isolated erythrocyte membranes. J. Cell Sci. 7:1970;357-371.
26. Dupont Y., Hasselbach W. Structural changes in sarcoplasmic reticulum membrane induced by SH reagents. Nat., New Biol. 246:1973;41-44.
27. Worthington C.R., Liu S.C. Structure of sarcoplasmic reticulum membranes at low resolution (17 Å). Arch. Biochem. Biophys. 157:1973;573-579.
28. Gleason M.M., Medow M.S., Tulenko T.N. Excess membrane cholesterol alters calcium movements, cytosolic calcium levels, and membrane fluidity in arterial smooth muscle cells. Circ. Res. 69:1991;216-227.
29. Russell P., Robison W.G. Jr., Kinoshita J.H. A new method for rapid isolation of the intrinsic membrane proteins from lens. Exp. Eye Res. 32:1981;511-516.
30. Folch J., Lees M., Sloane Stanley G.H. A simple method for the isolation and purification of total lipids from animal tissues. J. Biol. Chem. 226:1957;497-509.
31. Cenedella R.J. Digitonide precipitable sterols: a reevaluation with special attention to lanosterol. Lipids. 17:1982;443-447.
32. Pollet S., Ermidou S., Le Saux F., Monge M., Baumann N. Microanalysis of brain lipids: multiple two-dimensional thin-layer chromatography. J. Lipid Res. 19:1978;916-921.
33. Mason R.P., Jacob R.F. Armstrong D. Methods in Molecular Biology: Ultrastructural and Molecular Biology Protocols. vol. 193:2002;71-80 Humana Press, Totowa, NJ.
34. Simons K., Toomre D. Lipid rafts and signal transduction. Nat. Rev., Mol. Cell Biol. 1:2000;31-39.
35. Brown D.A., London E. Structure and function of sphingolipid- and cholesterol-rich membrane rafts. J. Biol. Chem. 275:2000;17221-17224.
36. Ostermeyer A.G., Beckrich B.T., Ivarson K.A., Grove K.E., Brown D.A. Glycosphingolipids are not essential for formation of detergent-resistant membrane rafts in melanoma cells. Methyl-beta-cyclodextrin does not affect cell surface transport of a GPI-anchored protein. J. Biol. Chem. 274:1999;34459-34466.
37. Edidin M. Lipid microdomains in cell surface membranes. Curr. Opin. Struct. Biol. 7:1997;528-532.
38. Craven B.M. Crystal structure of cholesterol monohydrate. Nature. 260:1976;727-729.
39. Borchman D., Cenedella R.J., Lamba O.P. Role of cholesterol in the structural order of lens membrane lipids. Exp. Eye Res. 62:1996;191-197.
40. Chandrasekher G., Cenedella R.J. Protein associated with human lens 'native' membrane during aging and cataract formation. Exp. Eye Res. 60:1995;707-717.
41. Cenedella R.J., Bierkamper G.G. Mechanism of cataract production by 3-beta(2-diethylaminoethoxy) androst-5-en-17-one hydrochloride, U18666A: an inhibitor of cholesterol biosynthesis. Exp. Eye Res. 28:1979;673-688.
42. Jacob R.F., Cenedella R.J., Mason R.P. Direct evidence for immiscible cholesterol domains in human ocular lens fiber cell plasma membranes. J. Biol. Chem. 274:1999;31613-31618.
43. Phillips J.E., Geng Y.J., Mason R.P. 7-Ketocholesterol forms crystallin domains in model membranes and murine aortic smooth muscle cells. Atherosclerosis. 159:2001;125-135.
44. Bialecki R.A., Tulenko T.N. Excess membrane cholesterol alters calcium channels in arterial smooth muscle. Am. J. Physiol. 257:1989;C306-C314.
45. Broderick R., Bialecki R., Tulenko T.N. Cholesterol-induced changes in rabbit arterial smooth muscle sensitivity to adrenergic stimulation. Am. J. Physiol. 257:1989;H170-H178.
46. + pump in endothelial cells. Atherosclerosis. 110:1994;251-257.
47. +)-ATPase ATP hydrolyzing activity in bovine kidney. Biochemistry. 27:1988;6449-6452.
48. Chang H.M., Reitstetter R., Mason R.P., Gruener R. Attenuation of channel kinetics and conductance by cholesterol: an interpretation using structural stress as a unifying concept. J. Membr. Biol. 143:1995;51-63.
49. Schroeder F., Jefferson J.R., Kier A.B., Knittel J., Scallen T.J., Wood W.G., Hapala I. Membrane cholesterol dynamics: cholesterol domains and kinetic pools. Proc. Soc. Exp. Biol. Med. 196:1991;235-252.
50. Phillips M.C., Johnson W.C., Rothblat G.H. Mechanism and consequences of cellular cholesterol exchange and transfer. Biochim. Biophys. Acta. 906:1997;223-276.
51. Liscum L., Underwood K.W. Intracellular cholesterol transport and compartmentation. J. Biol. Chem. 270:1995;15443-15446.
52. Schroeder F., Woodford J.K., Kavecansky J., Wood W.G., Joiner C. Cholesterol domains in biological membranes. Mol. Membr. Biol. 12:1995;113-119.
53. Bretscher M.S., Munro S. Cholesterol and the Golgi apparatus. Science. 261:1993;1280-1281.
54. Mukherjee S., Chattopadhyay A. Membrane organization at low cholesterol concentrations: a study using 7-nitrobenz-2-oxa-1,3-diazol-4-yl-labeled cholesterol. Biochemistry. 35:1996;1311-1322.
55. Janes P.W., Ley S.C., Magee A.I., Kabouridis P.S. The role of lipid rafts in T cell antigen receptor (TCR) signalling. Semin. Immunol. 12:2000;23-34.
56. Langlet C., Bernard A.M., Drevot P., He H.T. Membrane rafts and signaling by the multichain immune recognition receptors. Curr. Opin. Immunol. 12:2000;250-255.
57. Simons K., Ikonen E. Functional rafts in cell membranes. Nature. 387:1997;569-572.
58. Simons K., Ikonen E. How cells handle cholesterol. Science. 290:2000;1721-1726.
59. Engelman D.M., Rothman J.E. The planar organization of lecithin-cholesterol bilayers. J. Biol. Chem. 247:1972;3694-3697.
60. Houslay M.D., Stanley K.K. Dynamics of Biological Membranes: Influence on Synthesis, Structure and Function. 1982;Wiley, New York, NY.
61. Rice P.A., McConnell H.M. Critical shape transitions of monolayer lipid domains. Proc. Natl. Acad. Sci. U. S. A. 86:1989;6445-6448.
62. Slotte J.P. Lateral domain formation in mixed monolayers containing cholesterol and dipalmitoylphosphatidylcholine or N-palmitoylsphingomyelin. Biochim. Biophys. Acta. 1235:1995;419-427.
63. Slotte J.P. Effect of sterol structure on molecular interactions and lateral domain formation in monolayers containing dipalmitoyl phosphatidylcholine. Biochim. Biophys. Acta. 1237:1995;127-134.
64. Bloom M., Thewalt J.L. Time and distance scales of membrane domain organization. Mol. Membr. Biol. 12:1995;9-13.
65. Hui S.W. Geometry of domains and domain boundaries in monolayers and bilayers. Mol. Membr. Biol. 12:1995;45-50.
66. Tocanne J.F. Detection of lipid domains in biological membranes. Comments Mol. Cell. Biophys. 8:1992;53-72.
67. Kirschner D.A., Caspar D.L. Comparative diffraction studies on myelin membranes. Ann. N.Y. Acad. Sci. 195:1972;309-320.
68. Maekawa S., Sato C., Kitajima K., Funatsu N., Kumanogoh H., Sokawa Y. Cholesterol-dependent localization of NAP-22 on a neuronal membrane microdomain (raft). J. Biol. Chem. 274:1999;21369-21374.
69. Epand R.M., Maekawa S., Yip C.M., Epand R.F. Protein-induced formation of cholesterol-rich domains. Biochemistry. 40:2001;10514-10521.