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Volumn 40, Issue 12, 1999, Pages 2264-2270

Regulation of endoplasmic reticulum cholesterol by plasma membrane cholesterol

Author keywords

25 hydroxycholesterol; Homeostasis; Sensor; U18666A

Indexed keywords

25 HYDROXYCHOLESTEROL; AMPHOPHILE;

EID: 0033384957     PISSN: 00222275     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (213)

References (51)
  • 1
    • 0342348076 scopus 로고
    • Membrane-mediated control of reductase activity
    • B. Preiss, editor. Academic Press, Inc., New York
    • Mitropoulos, K. A., and S. Venkatesan. 1985. Membrane-mediated control of reductase activity. In Regulation of HMG-CoA Reductase. B. Preiss, editor. Academic Press, Inc., New York. 1-48.
    • (1985) Regulation of HMG-CoA Reductase , pp. 1-48
    • Mitropoulos, K.A.1    Venkatesan, S.2
  • 2
    • 0022310701 scopus 로고
    • The LDL receptor and HMG-CoA reductase - Two membrane molecules that regulate cholesterol homeostasis
    • Brown, M. S., and J. L. Goldstein. 1985. The LDL receptor and HMG-CoA reductase - two membrane molecules that regulate cholesterol homeostasis. Curr. Top. Cell. Regul. 26: 3-15.
    • (1985) Curr. Top. Cell. Regul. , vol.26 , pp. 3-15
    • Brown, M.S.1    Goldstein, J.L.2
  • 3
    • 0025120211 scopus 로고
    • Regulation of the mevalonate pathway
    • Goldstein, J., and M. Brown. 1990. Regulation of the mevalonate pathway. Nature. 343: 425-430.
    • (1990) Nature , vol.343 , pp. 425-430
    • Goldstein, J.1    Brown, M.2
  • 4
    • 0030941803 scopus 로고    scopus 로고
    • The SREBP pathway: Regulation of cholesterol metabolism by proteolysis of a membrane-bound transcription factor
    • Brown, M., and J. Goldstein. 1997. The SREBP pathway: regulation of cholesterol metabolism by proteolysis of a membrane-bound transcription factor. Cell. 89: 331-340.
    • (1997) Cell , vol.89 , pp. 331-340
    • Brown, M.1    Goldstein, J.2
  • 5
  • 6
    • 0030012975 scopus 로고    scopus 로고
    • The role of intracellular cholesterol transport in cholesterol homeostasis
    • Lange, Y., and T. L. Steck. 1996. The role of intracellular cholesterol transport in cholesterol homeostasis. Trends Cell Biol. 6: 205-208.
    • (1996) Trends Cell Biol , vol.6 , pp. 205-208
    • Lange, Y.1    Steck, T.L.2
  • 7
    • 0027972084 scopus 로고
    • Cholesterol homeostasis. Modulation by amphiphiles
    • Lange, Y., and T. L. Steck. 1994. Cholesterol homeostasis. Modulation by amphiphiles. J. Biol. Chem. 269: 29371-29374.
    • (1994) J. Biol. Chem. , vol.269 , pp. 29371-29374
    • Lange, Y.1    Steck, T.L.2
  • 8
    • 0026077761 scopus 로고
    • Lipoproteins activate acyl-coenzyme A:Cholesterol acyltransferase in macrophages only after cellular cholesterol pools are expanded to a critical threshold level
    • Xn, X-X., and I. Tabas. 1991. Lipoproteins activate acyl-coenzyme A:cholesterol acyltransferase in macrophages only after cellular cholesterol pools are expanded to a critical threshold level. J. Biol. Chem. 266: 17040-17048.
    • (1991) J. Biol. Chem. , vol.266 , pp. 17040-17048
    • Xn, X.-X.1    Tabas, I.2
  • 9
    • 0028812541 scopus 로고
    • Alteration of the myometrial plasma membrane cholesterol content with beta-cyclodextrin modulates the binding affinity of the oxytocin receptor
    • Klein, U., G. Gimpl, and F. Fahrenholz. 1995. Alteration of the myometrial plasma membrane cholesterol content with beta-cyclodextrin modulates the binding affinity of the oxytocin receptor. Biochemistry. 34: 13784-13793.
    • (1995) Biochemistry , vol.34 , pp. 13784-13793
    • Klein, U.1    Gimpl, G.2    Fahrenholz, F.3
  • 10
    • 0025333987 scopus 로고
    • Zymosterol is located in the plasma membrane of cultured human fibroblasts
    • Echevarria, F., R. A. Norton, W. D. Nes, and Y. Lange. 1990. Zymosterol is located in the plasma membrane of cultured human fibroblasts. J. Biol. Chem. 265: 8484-8489.
    • (1990) J. Biol. Chem. , vol.265 , pp. 8484-8489
    • Echevarria, F.1    Norton, R.A.2    Nes, W.D.3    Lange, Y.4
  • 11
    • 0032563304 scopus 로고    scopus 로고
    • Circulation of cholesterol between lysosomes and the plasma membrane
    • Lange, Y, J. Ye, and T. L. Steck. 1998. Circulation of cholesterol between lysosomes and the plasma membrane. J. Biol. Chem. 273: 18915-18922.
    • (1998) J. Biol. Chem. , vol.273 , pp. 18915-18922
    • Lange, Y.1    Ye, J.2    Steck, T.L.3
  • 12
    • 0016206178 scopus 로고
    • Suppression of 3-hydroxy-3-methylglutaryl coenzyme A reductase activity and inhibition of growth of human fibroblasts by 7-ketocholesterol
    • Brown, M. S., and J. L. Goldstein. 1974. Suppression of 3-hydroxy-3-methylglutaryl coenzyme A reductase activity and inhibition of growth of human fibroblasts by 7-ketocholesterol. J. Biol. Chem. 249: 7306-7314.
    • (1974) J. Biol. Chem. , vol.249 , pp. 7306-7314
    • Brown, M.S.1    Goldstein, J.L.2
  • 13
    • 0030977396 scopus 로고    scopus 로고
    • Quantitation of the pool of cholesterol associated with acyl-CoA:Cholesterol acyltransferase in human fibroblasls
    • Lange, Y., and T. L. Steck. 1997. Quantitation of the pool of cholesterol associated with acyl-CoA:cholesterol acyltransferase in human fibroblasls. J. Biol. Chem. 272: 13103-13108.
    • (1997) J. Biol. Chem. , vol.272 , pp. 13103-13108
    • Lange, Y.1    Steck, T.L.2
  • 15
    • 0025975875 scopus 로고
    • Disposition of intracellular cholesterol in human fibroblasts
    • Lange, Y. 1991. Disposition of intracellular cholesterol in human fibroblasts. J. Lipid Res. 32: 329-339.
    • (1991) J. Lipid Res. , vol.32 , pp. 329-339
    • Lange, Y.1
  • 16
    • 0030943621 scopus 로고    scopus 로고
    • Acyl-coenzyme A:Cholesterol acyltransferase
    • Chang, T., C. C. Chang, and D. Cheng. 1997. Acyl-coenzyme A:cholesterol acyltransferase. Annu. Rev. Biochem. 66: 613-638.
    • (1997) Annu. Rev. Biochem. , vol.66 , pp. 613-638
    • Chang, T.1    Chang, C.C.2    Cheng, D.3
  • 17
    • 0032567506 scopus 로고    scopus 로고
    • Recombinant acyl-CoA:Cholesterol acyltransferase-1 (ACAT-1) purified to essential homogeneity utilizes cholesterol in mixed micelles or in vesicles in a highly cooperative manner
    • Chang, C. C. Y., C. Y. G. Lee, E. T. Chang, J. C. Cruz, M. C. Levesque, and T. Y. Chang. 1998. Recombinant acyl-CoA:cholesterol acyltransferase-1 (ACAT-1) purified to essential homogeneity utilizes cholesterol in mixed micelles or in vesicles in a highly cooperative manner. J. Biol. Chem. 273: 35132-35141.
    • (1998) J. Biol. Chem. , vol.273 , pp. 35132-35141
    • Chang, C.C.Y.1    Lee, C.Y.G.2    Chang, E.T.3    Cruz, J.C.4    Levesque, M.C.5    Chang, T.Y.6
  • 19
    • 0032486433 scopus 로고    scopus 로고
    • Teratogen-mediated inhibition of target tissue response to Shh signaling
    • Cooper, M. K., J. A. Porter, K. E. Young, and P. A. Beachy. 1998. Teratogen-mediated inhibition of target tissue response to Shh signaling. Science. 280: 1603-1607.
    • (1998) Science , vol.280 , pp. 1603-1607
    • Cooper, M.K.1    Porter, J.A.2    Young, K.E.3    Beachy, P.A.4
  • 20
    • 0022256566 scopus 로고
    • Role of acyl-CoA:Cholesterol acyltransferase in cellular cholesterol melabolism
    • Suckling, K. E., and E. F. Stange. 1985. Role of acyl-CoA:cholesterol acyltransferase in cellular cholesterol melabolism. J. Lipid Res. 26: 647-671.
    • (1985) J. Lipid Res. , vol.26 , pp. 647-671
    • Suckling, K.E.1    Stange, E.F.2
  • 21
    • 0029022909 scopus 로고
    • The stimulation of the cholesterol esterification pathway by atherogenic lipoproteins in macrophages
    • Tabas, I. 199.5. The stimulation of the cholesterol esterification pathway by atherogenic lipoproteins in macrophages. Curr. Opin. Lipidol. 6: 260-268.
    • (1995) Curr. Opin. Lipidol. , vol.6 , pp. 260-268
    • Tabas, I.1
  • 23
    • 0029945036 scopus 로고    scopus 로고
    • Review of progress in sterol oxidations: 1987-1995
    • Smith, L. L. 1996. Review of progress in sterol oxidations: 1987-1995. Lipids. 31: 453-487.
    • (1996) Lipids , vol.31 , pp. 453-487
    • Smith, L.L.1
  • 24
    • 0032572729 scopus 로고    scopus 로고
    • Cholesterol homoeostasis: A role for oxysterols
    • Accad, M., and R. V. Farese, Jr. 1998. Cholesterol homoeostasis: a role for oxysterols. Curr. Biol. 8: R601-604.
    • (1998) Curr. Biol. , vol.8
    • Accad, M.1    Farese R.V., Jr.2
  • 26
    • 0001934896 scopus 로고    scopus 로고
    • Intracellular cholesterol movement and homeostasis
    • T-Y. Chang, and D. A. Freeman, editors. Kluwer Academic Press, Boston, MA
    • Lange, Y. 1998. Intracellular cholesterol movement and homeostasis. In Intracellular Cholesterol Trafficking. T-Y. Chang, and D. A. Freeman, editors. Kluwer Academic Press, Boston, MA. 15-27.
    • (1998) Intracellular Cholesterol Trafficking , pp. 15-27
    • Lange, Y.1
  • 27
    • 0024312609 scopus 로고
    • The intracellular transport of low density lipoprotein-derived cholesterol is inhibited in Chinese hamster ovary cells cultured with 3-beta-[2-(diethylamino)ethoxy] androsten-5-ene-17-one
    • Liscum, L., and J. Faust, 1989. The intracellular transport of low density lipoprotein-derived cholesterol is inhibited in Chinese hamster ovary cells cultured with 3-beta-[2-(diethylamino)ethoxy] androsten-5-ene-17-one. J. Biol. Chem. 264: 11796-11806.
    • (1989) J. Biol. Chem. , vol.264 , pp. 11796-11806
    • Liscum, L.1    Faust, J.2
  • 28
    • 0031013536 scopus 로고    scopus 로고
    • Role of multidrug resistance P-glycoproteins in cholesterol esterification
    • Debry, P., E. A. Nash, D. W. Neklason, and J. E. Metherall. 1997. Role of multidrug resistance P-glycoproteins in cholesterol esterification. J. Biol. Chem. 272: 1026-1031.
    • (1997) J. Biol. Chem. , vol.272 , pp. 1026-1031
    • Debry, P.1    Nash, E.A.2    Neklason, D.W.3    Metherall, J.E.4
  • 29
    • 0033617320 scopus 로고    scopus 로고
    • A mammalian lysosomal membrane protein confers multidrug resistance upon expression in Saccharomyces cerevisiae
    • Hogue, D. L., L. Kitby, and V. Ling. 1999. A mammalian lysosomal membrane protein confers multidrug resistance upon expression in Saccharomyces cerevisiae. J. Biol. Chem. 274: 12877-12882.
    • (1999) J. Biol. Chem. , vol.274 , pp. 12877-12882
    • Hogue, D.L.1    Kitby, L.2    Ling, V.3
  • 31
    • 0027418774 scopus 로고
    • Characterization of lysosomes from Dictyostelium discoideum by magnetic fractionation
    • Rodriguez-Paris, J. M., K. N. Nolta, and T. L. Steck. 1993. Characterization of lysosomes from Dictyostelium discoideum by magnetic fractionation. J. Biol. Chem. 268: 9110-9116.
    • (1993) J. Biol. Chem. , vol.268 , pp. 9110-9116
    • Rodriguez-Paris, J.M.1    Nolta, K.N.2    Steck, T.L.3
  • 32
    • 0028150776 scopus 로고
    • Analysis of successive endocytic compartments isolated from Dictyostelium discoideum by magnetic fractionation
    • Nolta, K. N., J. M. Rodriguez-Paris, and T. L. Steck. 1994. Analysis of successive endocytic compartments isolated from Dictyostelium discoideum by magnetic fractionation. Biochem. Biophys. Acta. 1224: 237-246.
    • (1994) Biochem. Biophys. Acta , vol.1224 , pp. 237-246
    • Nolta, K.N.1    Rodriguez-Paris, J.M.2    Steck, T.L.3
  • 35
    • 0021288057 scopus 로고
    • Pulmonary and generalized lysosomal storage induced by amphiphilic drugs
    • Hruban, Z. 1984. Pulmonary and generalized lysosomal storage induced by amphiphilic drugs. Environ. Health Perspect. 55: 53-76.
    • (1984) Environ. Health Perspect. , vol.55 , pp. 53-76
    • Hruban, Z.1
  • 36
    • 0028171319 scopus 로고
    • Lamellar bodies of rat alveolar type 2 cells have late cndosomal marker proteins on their limiting membranes
    • Wasano, K., and Y. Hirakawa. 1994. Lamellar bodies of rat alveolar type 2 cells have late cndosomal marker proteins on their limiting membranes. Histochemistry. 102: 329-335.
    • (1994) Histochemistry , vol.102 , pp. 329-335
    • Wasano, K.1    Hirakawa, Y.2
  • 37
    • 0033583562 scopus 로고    scopus 로고
    • Intracellular cholesterol transport
    • Liscum, L., and N. J. Munn. 1999. Intracellular cholesterol transport. Biochim. Biophys. Acta. 1438: 19-37.
    • (1999) Biochim. Biophys. Acta , vol.1438 , pp. 19-37
    • Liscum, L.1    Munn, N.J.2
  • 38
    • 0032512758 scopus 로고    scopus 로고
    • Evidence for a cholesterol transport pathway from lysosomes to endoplasmic reticulum that is independent of the plasma membrane
    • Underwood, K., N. Jacobs, A. Howley, and L. Liscum. 1998. Evidence for a cholesterol transport pathway from lysosomes to endoplasmic reticulum that is independent of the plasma membrane. J. Biol. Chem. 273: 4266-4274.
    • (1998) J. Biol. Chem. , vol.273 , pp. 4266-4274
    • Underwood, K.1    Jacobs, N.2    Howley, A.3    Liscum, L.4
  • 39
    • 0032527642 scopus 로고    scopus 로고
    • Structure and origin of ordered lipid domains in biological membranes
    • Brown, D. A., and E. London. 1998. Structure and origin of ordered lipid domains in biological membranes. J. Membr. Biol. 164: 103-114.
    • (1998) J. Membr. Biol. , vol.164 , pp. 103-114
    • Brown, D.A.1    London, E.2
  • 40
    • 0019139222 scopus 로고
    • The effect of cholesterol and other intercalated amphipaths on the contour and stability of the isolated red cell membrane
    • Lange, Y., H. B. Cutler, and T. L. Steck. 1980. The effect of cholesterol and other intercalated amphipaths on the contour and stability of the isolated red cell membrane. J. Biol. Chem. 255: 9331-9337.
    • (1980) J. Biol. Chem. , vol.255 , pp. 9331-9337
    • Lange, Y.1    Cutler, H.B.2    Steck, T.L.3
  • 41
    • 0019332679 scopus 로고
    • Effect of cholesterol concentration on organization of viral and vesicle membranes. Probed by accessibility to cholesterol oxidase
    • Pal, R., Y. Barenholz, and R. R. Wagner. 1980. Effect of cholesterol concentration on organization of viral and vesicle membranes. Probed by accessibility to cholesterol oxidase. J. Biol. Chem. 255: 5802-5806.
    • (1980) J. Biol. Chem. , vol.255 , pp. 5802-5806
    • Pal, R.1    Barenholz, Y.2    Wagner, R.R.3
  • 42
    • 0021341798 scopus 로고
    • Cholesterol oxidase susceptibility of the red cell membrane
    • Lange, Y, H. Matthies, and T. L. Steck. 1984. Cholesterol oxidase susceptibility of the red cell membrane. Biochim. Biophys. Acta. 769: 551-562.
    • (1984) Biochim. Biophys. Acta , vol.769 , pp. 551-562
    • Lange, Y.1    Matthies, H.2    Steck, T.L.3
  • 43
    • 0017664541 scopus 로고
    • Membrane cholesterol and cell fusion of hen and guinea-pig erythrocytes
    • Hope, M. J., K. R. Bruckdorfer, C. A. Hart, and J. A. Lucy. 1977. Membrane cholesterol and cell fusion of hen and guinea-pig erythrocytes. Biochem. J. 166: 255-263.
    • (1977) Biochem. J. , vol.166 , pp. 255-263
    • Hope, M.J.1    Bruckdorfer, K.R.2    Hart, C.A.3    Lucy, J.A.4
  • 44
    • 0031692336 scopus 로고    scopus 로고
    • The caveolae membrane system
    • Anderson, R. G. 1998. The caveolae membrane system. Annu. Rev. Biochem. 67: 199-225.
    • (1998) Annu. Rev. Biochem. , vol.67 , pp. 199-225
    • Anderson, R.G.1
  • 45
    • 0031740079 scopus 로고    scopus 로고
    • The differential miscibility of lipids as the basis for the formation of functional membrane rafts
    • Rietveld, A., and K. Simons. 1998. The differential miscibility of lipids as the basis for the formation of functional membrane rafts. Biochim. Biophys. Acta. 1376: 467-479.
    • (1998) Biochim. Biophys. Acta , vol.1376 , pp. 467-479
    • Rietveld, A.1    Simons, K.2
  • 47
    • 0030997431 scopus 로고    scopus 로고
    • Murine SR-BI, a high density lipoprotein receptor that mediates selective lipid uptake, is N-glycosylated and fatty acylated and colocalizes with plasma membrane caveolae
    • Babitt, J., B. Trigatti, A. Rigotti, E. J. Smart, R. G. Anderson, S. Xu, and M. Krieger. 1997. Murine SR-BI, a high density lipoprotein receptor that mediates selective lipid uptake, is N-glycosylated and fatty acylated and colocalizes with plasma membrane caveolae. J. Biol. Chem. 272: 13242-13249.
    • (1997) J. Biol. Chem. , vol.272 , pp. 13242-13249
    • Babitt, J.1    Trigatti, B.2    Rigotti, A.3    Smart, E.J.4    Anderson, R.G.5    Xu, S.6    Krieger, M.7
  • 48
    • 0030809601 scopus 로고    scopus 로고
    • Intracellular cholesterol transport
    • Fielding, C. J., and P. E. Fielding. 1997. Intracellular cholesterol transport. J. Lipid Res. 38: 1503-1521.
    • (1997) J. Lipid Res. , vol.38 , pp. 1503-1521
    • Fielding, C.J.1    Fielding, P.E.2
  • 49
    • 0030970279 scopus 로고    scopus 로고
    • Caveolin mRNA levels are up-regulated by free cholesterol and down regulated by oxysterols in fibroblast monolayers
    • Fielding, C. J., A. Bist, and P. E. Fielding. 1997. Caveolin mRNA levels are up-regulated by free cholesterol and down regulated by oxysterols in fibroblast monolayers. Proc. Natl. Acad. Sci. USA. 94: 3753-3758.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 3753-3758
    • Fielding, C.J.1    Bist, A.2    Fielding, P.E.3
  • 50
    • 0031888035 scopus 로고    scopus 로고
    • Regulation of caveolin and caveolae by cholesterol in MDCK cells
    • Hailstones, D., L. Sleer, R. Parton, and K. Stanley. 1998. Regulation of caveolin and caveolae by cholesterol in MDCK cells. J. Lipid Res. 39: 369-379.
    • (1998) J. Lipid Res. , vol.39 , pp. 369-379
    • Hailstones, D.1    Sleer, L.2    Parton, R.3    Stanley, K.4
  • 51
    • 0032513038 scopus 로고    scopus 로고
    • Characterization of a cytosolic heat-shock protein-caveolin chaperone complex. Involvement in cholesterol trafficking
    • Uittenbogaard, A., Y-S. Ying, and E. J. Smart. 1998. Characterization of a cytosolic heat-shock protein-caveolin chaperone complex. Involvement in cholesterol trafficking. J. Biol. Chem. 273: 6525-6532.
    • (1998) J. Biol. Chem. , vol.273 , pp. 6525-6532
    • Uittenbogaard, A.1    Ying, Y.-S.2    Smart, E.J.3


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