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Volumn 1818, Issue 2, 2012, Pages 330-336

Side-chain oxysterols: From cells to membranes to molecules

Author keywords

Cholesterol; Homeostasis; Molecular dynamics; Oxysterol; Sterol

Indexed keywords

OXYSTEROL;

EID: 84855446282     PISSN: 00052736     EISSN: 18792642     Source Type: Journal    
DOI: 10.1016/j.bbamem.2011.06.014     Document Type: Review
Times cited : (46)

References (49)
  • 1
    • 7044241302 scopus 로고    scopus 로고
    • How lipids affect the activities of integral membrane proteins
    • DOI 10.1016/j.bbamem.2004.05.012, PII S0005273604001592, Lipid-Protein Interactions
    • A. Lee How lipids affect the activities of integral membrane proteins Biochim. Biophys. Acta 1666 2004 62 87 (Pubitemid 39425199)
    • (2004) Biochimica et Biophysica Acta - Biomembranes , vol.1666 , Issue.1-2 , pp. 62-87
    • Lee, A.G.1
  • 2
    • 0022087303 scopus 로고
    • Regulation of adenylate cyclase (EC 4.6.1.1) activity by its lipid environment
    • M. Houslay Regulation of adenylate cyclase (EC 4.6.1.1) activity by its lipid environment Proc. Nutr. Soc. 44 1985 157 165
    • (1985) Proc. Nutr. Soc. , vol.44 , pp. 157-165
    • Houslay, M.1
  • 3
    • 22344441881 scopus 로고    scopus 로고
    • Influence of the membrane lipid structure on signal processing via G protein-coupled receptors
    • DOI 10.1124/mol.105.011692
    • Q. Yang, R. Alemany, J. Casas, K. Kitajka, S. Lanier, and P. Escribá Influence of the membrane lipid structure on signal processing via G protein-coupled receptors Mol. Pharmacol. 68 2005 210 217 (Pubitemid 41002960)
    • (2005) Molecular Pharmacology , vol.68 , Issue.1 , pp. 210-217
    • Yang, Q.1    Alemany, R.2    Casas, J.3    Kitajka, K.4    Lanier, S.M.5    Escriba, P.V.6
  • 4
    • 33745041479 scopus 로고    scopus 로고
    • Roles of bilayer material properties in function and distribution of membrane proteins
    • DOI 10.1146/annurev.biophys.35.040405.102022
    • T. McIntosh, and S. Simon Roles of bilayer material properties in function and distribution of membrane proteins Annu. Rev. Biophys. Biomol. Struct. 35 2006 177 198 (Pubitemid 43877375)
    • (2006) Annual Review of Biophysics and Biomolecular Structure , vol.35 , pp. 177-198
    • McIntosh, T.J.1    Simon, S.A.2
  • 5
    • 0037339478 scopus 로고    scopus 로고
    • Cholesterol-induced protein sorting: An analysis of energetic feasibility
    • J.A. Lundbaek, O.S. Andersen, T. Werge, and C. Nielsen Cholesterol-induced protein sorting: an analysis of energetic feasibility Biophys. J. 84 2003 2080 2089 (Pubitemid 36322969)
    • (2003) Biophysical Journal , vol.84 , Issue.3 , pp. 2080-2089
    • Lundbaek, J.A.1    Andersen, O.S.2    Werge, T.3    Nielsen, C.4
  • 6
    • 0034677631 scopus 로고    scopus 로고
    • PIP2 and PIP3: Complex roles at the cell surface
    • M.P. Czech PIP2 and PIP3: complex roles at the cell surface Cell 100 2000 603 606
    • (2000) Cell , vol.100 , pp. 603-606
    • Czech, M.P.1
  • 7
    • 4444309565 scopus 로고    scopus 로고
    • The complex life of simple sphingolipids
    • DOI 10.1038/sj.embor.7400208
    • A. Futerman, and Y. Hannun The complex life of simple sphingolipids EMBO Rep. 5 2004 777 782 (Pubitemid 39199166)
    • (2004) EMBO Reports , vol.5 , Issue.8 , pp. 777-782
    • Futerman, A.H.1    Hannun, Y.A.2
  • 8
    • 38549152194 scopus 로고    scopus 로고
    • Principles of bioactive lipid signalling: Lessons from sphingolipids
    • DOI 10.1038/nrm2329, PII NRM2329
    • Y. Hannun, and L. Obeid Principles of bioactive lipid signalling: lessons from sphingolipids. Nature reviews Mol. Cell Biol. 9 2008 139 150 (Pubitemid 351158911)
    • (2008) Nature Reviews Molecular Cell Biology , vol.9 , Issue.2 , pp. 139-150
    • Hannun, Y.A.1    Obeid, L.M.2
  • 9
    • 70349898677 scopus 로고    scopus 로고
    • The ins and outs of phospholipid asymmetry in the plasma membrane: Roles in health and disease
    • B. Fadeel, and D. Xue The ins and outs of phospholipid asymmetry in the plasma membrane: roles in health and disease Crit. Rev. Biochem. Mol. Biol. 44 2009 264 277
    • (2009) Crit. Rev. Biochem. Mol. Biol. , vol.44 , pp. 264-277
    • Fadeel, B.1    Xue, D.2
  • 10
    • 38549141572 scopus 로고    scopus 로고
    • Cellular cholesterol trafficking and compartmentalization
    • DOI 10.1038/nrm2336, PII NRM2336
    • E. Ikonen Cellular cholesterol trafficking and compartmentalization Nat. Rev. Mol. Cell Biol. 9 2008 125 138 (Pubitemid 351158918)
    • (2008) Nature Reviews Molecular Cell Biology , vol.9 , Issue.2 , pp. 125-138
    • Ikonen, E.1
  • 11
    • 33745400408 scopus 로고    scopus 로고
    • Cholesterol is required for efficient endoplasmic reticulum-to-Golgi transport of secretory membrane proteins
    • DOI 10.1091/mbc.E05-02-0100
    • A. Ridsdale, M. Denis, P.-Y. Gougeon, J. Ngsee, J. Presley, and X. Zha Cholesterol is required for efficient endoplasmic reticulum-to-Golgi transport of secretory membrane proteins Mol. Biol. Cell 17 2006 1593 1605 (Pubitemid 44011579)
    • (2006) Molecular Biology of the Cell , vol.17 , Issue.4 , pp. 1593-1605
    • Ridsdale, A.1    Denis, M.2    Gougeon, P.-Y.3    Ngsee, J.K.4    Presley, J.F.5    Zha, X.6
  • 12
    • 79951839943 scopus 로고    scopus 로고
    • 25-Hydroxycholesterol increases the availability of cholesterol in phospholipid membranes
    • B. Olsen, P. Schlesinger, D. Ory, and N. Baker 25-Hydroxycholesterol increases the availability of cholesterol in phospholipid membranes Biophys. J. 100 2011 948 956
    • (2011) Biophys. J. , vol.100 , pp. 948-956
    • Olsen, B.1    Schlesinger, P.2    Ory, D.3    Baker, N.4
  • 13
    • 0036027683 scopus 로고    scopus 로고
    • Cholesterol interactions with phospholipids in membranes
    • DOI 10.1016/S0163-7827(01)00020-0, PII S0163782701000200
    • H. Ohvo-Rekilä, B. Ramstedt, P. Leppimäki, and P. Slotte Cholesterol interactions with phospholipids in membranes Prog. Lipid Res. 41 2002 66 97 (Pubitemid 32998278)
    • (2002) Progress in Lipid Research , vol.41 , Issue.1 , pp. 66-97
    • Ohvo-Rekila, H.1    Ramstedt, B.2    Leppimaki, P.3    Peter Slotte, J.4
  • 17
    • 0036251153 scopus 로고    scopus 로고
    • SREBPs: Activators of the complete program of cholesterol and fatty acid synthesis in the liver
    • DOI 10.1172/JCI200215593
    • J. Horton, J. Goldstein, and M. Brown SREBPs: activators of the complete program of cholesterol and fatty acid synthesis in the liver J. Clin. Invest. 109 2002 1125 1131 (Pubitemid 34496588)
    • (2002) Journal of Clinical Investigation , vol.109 , Issue.9 , pp. 1125-1131
    • Horton, J.D.1    Goldstein, J.L.2    Brown, M.S.3
  • 18
    • 4944247161 scopus 로고    scopus 로고
    • Nuclear receptor signaling in the control of cholesterol homeostasis: Have the orphans found a home?
    • DOI 10.1161/01.RES.0000143422.83209.be
    • D. Ory Nuclear receptor signaling in the control of cholesterol homeostasis: have the orphans found a home? Circ. Res. 95 2004 660 670 (Pubitemid 39331925)
    • (2004) Circulation Research , vol.95 , Issue.7 , pp. 660-670
    • Ory, D.S.1
  • 19
    • 1242269851 scopus 로고    scopus 로고
    • Regulation of bile acid synthesis: Pathways, nuclear receptors, and mechanisms
    • DOI 10.1016/j.jhep.2003.11.006
    • J. Chiang Regulation of bile acid synthesis: pathways, nuclear receptors, and mechanisms J. Hepatol. 40 2004 539 551 (Pubitemid 38230860)
    • (2004) Journal of Hepatology , vol.40 , Issue.3 , pp. 539-551
    • Chiang, J.Y.L.1
  • 20
    • 33947617210 scopus 로고    scopus 로고
    • Enzymes in the conversion of cholesterol into bile acids
    • DOI 10.2174/156652407780059168
    • M. Norlin, and K. Wikvall Enzymes in the conversion of cholesterol into bile acids Curr. Mol. Med. 7 2007 199 218 (Pubitemid 46488191)
    • (2007) Current Molecular Medicine , vol.7 , Issue.2 , pp. 199-218
    • Norlin, M.1    Wikvall, K.2
  • 21
    • 38349112601 scopus 로고    scopus 로고
    • Effectors of rapid homeostatic responses of endoplasmic reticulum cholesterol and 3-hydroxy-3-methylglutaryl-CoA reductase
    • Y. Lange, D. Ory, J. Ye, M. Lanier, F.-F. Hsu, and T. Steck Effectors of rapid homeostatic responses of endoplasmic reticulum cholesterol and 3-hydroxy-3-methylglutaryl-CoA reductase J. Biol. Chem. 283 2008 1445 1455
    • (2008) J. Biol. Chem. , vol.283 , pp. 1445-1455
    • Lange, Y.1    Ory, D.2    Ye, J.3    Lanier, M.4    Hsu, F.-F.5    Steck, T.6
  • 22
    • 0037815282 scopus 로고    scopus 로고
    • NPC1 and NPC2 regulate cellular cholesterol homeostasis through generation of low density lipoprotein cholesterol-derived oxysterols
    • DOI 10.1074/jbc.M302588200
    • A. Frolov, S. Zielinski, J. Crowley, N. Dudley-Rucker, J. Schaffer, and D. Ory NPC1 and NPC2 regulate cellular cholesterol homeostasis through generation of low density lipoprotein cholesterol-derived oxysterols J. Biol. Chem. 278 2003 25517 25525 (Pubitemid 36835303)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.28 , pp. 25517-25525
    • Frolov, A.1    Zielinski, S.E.2    Crowley, J.R.3    Dudley-Rucker, N.4    Schaffer, J.E.5    Ory, D.S.6
  • 24
    • 0029805887 scopus 로고    scopus 로고
    • An oxysterol signalling pathway mediated by the nuclear receptor LXRα
    • DOI 10.1038/383728a0
    • B.A. Janowski, P.J. Willy, T.R. Devi, J.R. Falck, and D.J. Mangelsdorf An oxysterol signalling pathway mediated by the nuclear receptor LXR alpha Nature 383 1996 728 731 (Pubitemid 26360651)
    • (1996) Nature , vol.383 , Issue.6602 , pp. 728-731
    • Janowski, B.A.1    Willy, P.J.2    Devi, T.R.3    Falck, J.R.4    Mangelsdorf, D.J.5
  • 25
    • 66349136255 scopus 로고    scopus 로고
    • Are side-chain oxidized oxysterols regulators also in vivo?
    • Suppl
    • I. Björkhem Are side-chain oxidized oxysterols regulators also in vivo? J. Lipid Res. 50 2009 S213 S218 Suppl
    • (2009) J. Lipid Res. , vol.50
    • Björkhem, I.1
  • 26
    • 38849114338 scopus 로고    scopus 로고
    • Cholesterol efflux pathways and other potential mechanisms involved in the athero-protective effect of high density lipoproteins
    • DOI 10.1111/j.1365-2796.2007.01898.x
    • A.R. Tall Cholesterol efflux pathways and other potential mechanisms involved in the athero-protective effect of high density lipoproteins J. Intern. Med. 263 2008 256 273 (Pubitemid 351207349)
    • (2008) Journal of Internal Medicine , vol.263 , Issue.3 , pp. 256-273
    • Tall, A.R.1
  • 27
    • 0037082099 scopus 로고    scopus 로고
    • Mutant mammalian cells as tools to delineate the sterol regulatory element-binding protein pathway for feedback regulation of lipid synthesis
    • DOI 10.1006/abbi.2001.2615
    • J. Goldstein, R. Rawson, and M. Brown Mutant mammalian cells as tools to delineate the sterol regulatory element-binding protein pathway for feedback regulation of lipid synthesis Arch. Biochem. Biophys. 397 2002 139 148 (Pubitemid 34852273)
    • (2002) Archives of Biochemistry and Biophysics , vol.397 , Issue.2 , pp. 139-148
    • Goldstein, J.L.1    Rawson, R.B.2    Brown, M.S.3
  • 28
    • 0018647344 scopus 로고
    • Potent immunosuppression by oxidized cholesterol
    • G.M. Humphries, and H.M. McConnell Potent immunosuppression by oxidized cholesterol J. Immunol. 122 1979 121 126 (Pubitemid 9078528)
    • (1979) Journal of Immunology , vol.122 , Issue.1 , pp. 121-126
    • Humphries, G.M.K.1    McConnell, H.M.2
  • 29
    • 0030941803 scopus 로고    scopus 로고
    • The SREBP pathway: Regulation of cholesterol metabolism by proteolysis of a membrane-bound transcription factor
    • DOI 10.1016/S0092-8674(00)80213-5
    • M.S. Brown, and J.L. Goldstein The SREBP pathway: regulation of cholesterol metabolism by proteolysis of a membrane-bound transcription factor Cell 89 1997 331 340 (Pubitemid 27220877)
    • (1997) Cell , vol.89 , Issue.3 , pp. 331-340
    • Brown, M.S.1    Goldstein, J.L.2
  • 30
    • 0025120211 scopus 로고
    • Regulation of the mevalonate pathway
    • J.L. Goldstein, and M.S. Brown Regulation of the mevalonate pathway Nature 343 1990 425 430
    • (1990) Nature , vol.343 , pp. 425-430
    • Goldstein, J.L.1    Brown, M.S.2
  • 31
    • 0029797604 scopus 로고    scopus 로고
    • Overproduction of cholesterol and fatty acids causes massive liver enlargement in transgenic mice expressing truncated SREBP-1a
    • H. Shimano, J.D. Horton, R.E. Hammer, I. Shimomura, M.S. Brown, and J.L. Goldstein Overproduction of cholesterol and fatty acids causes massive liver enlargement in transgenic mice expressing truncated SREBP-1a J. Clin. Invest. 98 1996 1575 1584 (Pubitemid 26327867)
    • (1996) Journal of Clinical Investigation , vol.98 , Issue.7 , pp. 1575-1584
    • Shimano, H.1    Horton, J.D.2    Hammer, R.E.3    Shimomura, I.4    Brown, M.S.5    Goldstein, J.L.6
  • 32
    • 0036792050 scopus 로고    scopus 로고
    • Insig-2, a second endoplasmic reticulum protein that binds SCAP and blocks export of sterol regulatory element-binding proteins
    • D. Yabe, M. Brown, and J. Goldstein Insig-2, a second endoplasmic reticulum protein that binds SCAP and blocks export of sterol regulatory element-binding proteins Proc. Natl. Acad. Sci. U. S. A. 99 2002 12753 12758
    • (2002) Proc. Natl. Acad. Sci. U. S. A. , vol.99 , pp. 12753-12758
    • Yabe, D.1    Brown, M.2    Goldstein, J.3
  • 33
    • 0037162719 scopus 로고    scopus 로고
    • Crucial step in cholesterol homeostasis: Sterols promote binding of SCAP to INSIG-1, a membrane protein that facilitates retention of SREBPs in ER
    • DOI 10.1016/S0092-8674(02)00872-3
    • T. Yang, P. Espenshade, M. Wright, D. Yabe, Y. Gong, R. Aebersold, J. Goldstein, and M. Brown Crucial step in cholesterol homeostasis: sterols promote binding of SCAP to INSIG-1, a membrane protein that facilitates retention of SREBPs in ER Cell 110 2002 489 500 (Pubitemid 35232292)
    • (2002) Cell , vol.110 , Issue.4 , pp. 489-500
    • Yang, T.1    Espenshade, P.J.2    Wright, M.E.3    Yabe, D.4    Gong, Y.5    Aebersold, R.6    Goldstein, J.L.7    Brown, M.S.8
  • 34
    • 0021856440 scopus 로고
    • Membrane-bound domain of HMG CoA reductase is required for sterol-enhanced degradation of the enzyme
    • G. Gil, J.R. Faust, D.J. Chin, J.L. Goldstein, and M.S. Brown Membrane-bound domain of HMG CoA reductase is required for sterol-enhanced degradation of the enzyme Cell 41 1985 249 258 (Pubitemid 15068442)
    • (1985) Cell , vol.41 , Issue.1 , pp. 249-258
    • Gil, G.1    Faust, J.R.2    Chin, D.J.3
  • 35
    • 0036534286 scopus 로고    scopus 로고
    • The sterol-sensing domain: Multiple families, a unique role?
    • DOI 10.1016/S0168-9525(02)02640-9, PII S0168952502026409
    • P. Kuwabara, and M. Labouesse The sterol-sensing domain: multiple families, a unique role? Trends Genet. 18 2002 193 201 (Pubitemid 34273740)
    • (2002) Trends in Genetics , vol.18 , Issue.4 , pp. 193-201
    • Kuwabara, P.E.1    Labouesse, M.2
  • 36
    • 0033384957 scopus 로고    scopus 로고
    • Regulation of endoplasmic reticulum cholesterol by plasma membrane cholesterol
    • Y. Lange, J. Ye, M. Rigney, and T. Steck Regulation of endoplasmic reticulum cholesterol by plasma membrane cholesterol J. Lipid Res. 40 1999 2264 2270 (Pubitemid 30017528)
    • (1999) Journal of Lipid Research , vol.40 , Issue.12 , pp. 2264-2270
    • Lange, Y.1    Ye, J.2    Rigney, M.3    Steck, T.L.4
  • 40
    • 0037245750 scopus 로고    scopus 로고
    • Accelerated degradation of HMG CoA reductase mediated by binding of insig-1 to its sterol-sensing domain
    • DOI 10.1016/S1097-2765(02)00822-5
    • N. Sever, T. Yang, M. Brown, J. Goldstein, and R. DeBose-Boyd Accelerated degradation of HMG CoA reductase mediated by binding of insig-1 to its sterol-sensing domain Mol. Cell 11 2003 25 33 (Pubitemid 36126588)
    • (2003) Molecular Cell , vol.11 , Issue.1 , pp. 25-33
    • Sever, N.1    Yang, T.2    Brown, M.S.3    Goldstein, J.L.4    DeBose-Boyd, R.A.5
  • 41
    • 44949133956 scopus 로고    scopus 로고
    • Cholesterol homeostasis and the escape tendency (activity) of plasma membrane cholesterol
    • Y. Lange, and T. Steck Cholesterol homeostasis and the escape tendency (activity) of plasma membrane cholesterol Prog. Lipid Res. 47 2008 319 332
    • (2008) Prog. Lipid Res. , vol.47 , pp. 319-332
    • Lange, Y.1    Steck, T.2
  • 43
    • 77956511868 scopus 로고    scopus 로고
    • Accessibility of cholesterol in endoplasmic reticulum membranes and activation of SREBP-2 switch abruptly at a common cholesterol threshold
    • A. Sokolov, and A. Radhakrishnan Accessibility of cholesterol in endoplasmic reticulum membranes and activation of SREBP-2 switch abruptly at a common cholesterol threshold J. Biol. Chem. 285 2010 29480 29490
    • (2010) J. Biol. Chem. , vol.285 , pp. 29480-29490
    • Sokolov, A.1    Radhakrishnan, A.2
  • 45
    • 0023044208 scopus 로고
    • Membrane properties of oxysterols. Interfacial orientation, influence on membrane permeability and redistribution between membranes, interfacial orientation, influence on membrane permeability and redistribution between membranes
    • J.J. Theunissen, R.L. Jackson, H.J. Kempen, and R.A. Demel Membrane properties of oxysterols. Interfacial orientation, influence on membrane permeability and redistribution between membranes, interfacial orientation, influence on membrane permeability and redistribution between membranes Biochim. Biophys. Acta 860 1986 66 74
    • (1986) Biochim. Biophys. Acta , vol.860 , pp. 66-74
    • Theunissen, J.J.1    Jackson, R.L.2    Kempen, H.J.3    Demel, R.A.4
  • 46
    • 77954217091 scopus 로고    scopus 로고
    • Interaction of two oxysterols, 7-ketocholesterol and 25- hydroxycholesterol, with phosphatidylcholine and sphingomyelin in model membranes
    • E. Mintzer, G. Charles, and S. Gordon Interaction of two oxysterols, 7-ketocholesterol and 25-hydroxycholesterol, with phosphatidylcholine and sphingomyelin in model membranes Chem. Phys. Lipids 163 2010 586 593
    • (2010) Chem. Phys. Lipids , vol.163 , pp. 586-593
    • Mintzer, E.1    Charles, G.2    Gordon, S.3
  • 47
    • 33646147145 scopus 로고    scopus 로고
    • Phase behavior of lipid monolayers containing DPPC and cholesterol analogs
    • B. Stottrup, and S. Keller Phase behavior of lipid monolayers containing DPPC and cholesterol analogs Biophys. J. 90 2006 3176 3183
    • (2006) Biophys. J. , vol.90 , pp. 3176-3183
    • Stottrup, B.1    Keller, S.2
  • 48
    • 67949098831 scopus 로고    scopus 로고
    • Perturbations of membrane structure by cholesterol and cholesterol derivatives are determined by sterol orientation
    • B. Olsen, P. Schlesinger, and N. Baker Perturbations of membrane structure by cholesterol and cholesterol derivatives are determined by sterol orientation J. Am. Chem. Soc. 131 2009 4854 4865
    • (2009) J. Am. Chem. Soc. , vol.131 , pp. 4854-4865
    • Olsen, B.1    Schlesinger, P.2    Baker, N.3
  • 49
    • 0037959071 scopus 로고    scopus 로고
    • The state of lipid rafts: From model membranes to cells
    • DOI 10.1146/annurev.biophys.32.110601.142439
    • M. Edidin The state of lipid rafts: from model membranes to cells Annu. Rev. Biophys. Biomol. Struct. 32 2003 257 283 (Pubitemid 37056230)
    • (2003) Annual Review of Biophysics and Biomolecular Structure , vol.32 , pp. 257-283
    • Edidin, M.1


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