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Volumn 273, Issue 3 42-3, 1997, Pages

A role for retrosomes in intracellular cholesterol transport from endosomes to the plasma membrane

Author keywords

Cholesterol metabolism; Membranes; Receptor mediated endocytosis

Indexed keywords

APOLIPOPROTEIN B; APOLIPOPROTEIN E; CHOLESTEROL; CHOLESTEROL ESTER; CHOLESTEROL ESTERASE; VERY LOW DENSITY LIPOPROTEIN;

EID: 0030879972     PISSN: 03636143     EISSN: None     Source Type: Journal    
DOI: 10.1152/ajpcell.1997.273.3.c1075     Document Type: Article
Times cited : (33)

References (43)
  • 1
    • 0027745543 scopus 로고
    • Transport of lipids to the plasma membrane in animal cells
    • Allan, D., and K. Kallen. Transport of lipids to the plasma membrane in animal cells. Prog. Lipid Res. 32: 543-560, 1993.
    • (1993) Prog. Lipid Res. , vol.32 , pp. 543-560
    • Allan, D.1    Kallen, K.2
  • 2
    • 0028346520 scopus 로고
    • Receptor mediated transcytosis of IgA in MDCK cells is via apical recycling endosomes
    • Apodaca, G., L. A. Katz, and K. E. Mostov. Receptor mediated transcytosis of IgA in MDCK cells is via apical recycling endosomes. J. Cell Biol. 125: 67-86, 1994.
    • (1994) J. Cell Biol. , vol.125 , pp. 67-86
    • Apodaca, G.1    Katz, L.A.2    Mostov, K.E.3
  • 4
    • 33845261493 scopus 로고
    • A rapid method of total lipid extraction and purification
    • Bligh, E. G., and W. J. Dyer. A rapid method of total lipid extraction and purification. Can. J. Biochem. Physiol. 37: 911-920, 1959.
    • (1959) Can. J. Biochem. Physiol. , vol.37 , pp. 911-920
    • Bligh, E.G.1    Dyer, W.J.2
  • 5
    • 0022549920 scopus 로고
    • A receptor mediated pathway for cholesterol homeostasis
    • Brown, M. S., and J. L. Goldstein. A receptor mediated pathway for cholesterol homeostasis. Science 232: 34-47, 1986.
    • (1986) Science , vol.232 , pp. 34-47
    • Brown, M.S.1    Goldstein, J.L.2
  • 6
    • 0024384937 scopus 로고
    • Identity of a cytosolic neutral cholesterol esterase in rat liver with the bile salt stimulated cholesterol esterase in pancreas
    • Camulli, E. D., M. J. Linke, H. L. Brockman, and D. Y. Hui. Identity of a cytosolic neutral cholesterol esterase in rat liver with the bile salt stimulated cholesterol esterase in pancreas. Biochim. Biophys. Acta 1005: 177-182, 1989.
    • (1989) Biochim. Biophys. Acta , vol.1005 , pp. 177-182
    • Camulli, E.D.1    Linke, M.J.2    Brockman, H.L.3    Hui, D.Y.4
  • 7
    • 0021761843 scopus 로고
    • 125I-asialoorosomucoid by rat hepatocytes, a non-lysosomal pathway insensitive to inhibitors of ligand degradation
    • 125I-asialoorosomucoid by rat hepatocytes, a non-lysosomal pathway insensitive to inhibitors of ligand degradation. Biochim. Biophys. Acta 805: 268-276, 1984.
    • (1984) Biochim. Biophys. Acta , vol.805 , pp. 268-276
    • Chang, T.1    Kullberg, D.W.2
  • 8
    • 0026701622 scopus 로고
    • Sphingomyelin content of intestinal cell membranes regulates cholesterol absorption
    • Chen, H., E. Born, S. N. Mathur, F. C. Johlin, Jr., and F. J. Field. Sphingomyelin content of intestinal cell membranes regulates cholesterol absorption. Biochem. J. 286: 771-777, 1992.
    • (1992) Biochem. J. , vol.286 , pp. 771-777
    • Chen, H.1    Born, E.2    Mathur, S.N.3    Johlin Jr., F.C.4    Field, F.J.5
  • 9
    • 0015209679 scopus 로고
    • Enzymatic characterization and lipid composition of rat liver subcellular membranes
    • Colbeau, A., J. Nachbaur, and P. M. Vignais. Enzymatic characterization and lipid composition of rat liver subcellular membranes. Biochim. Biophys. Acta 249: 462-492, 1971.
    • (1971) Biochim. Biophys. Acta , vol.249 , pp. 462-492
    • Colbeau, A.1    Nachbaur, J.2    Vignais, P.M.3
  • 11
    • 0018099957 scopus 로고
    • Reversal by Triton-1339 of ethinylestradiol-induced hepatic cholesterol esterification
    • Davis, R. A., R. Showalter, and F. Kern. Reversal by Triton-1339 of ethinylestradiol-induced hepatic cholesterol esterification. Biochem. J. 174: 45-51, 1978.
    • (1978) Biochem. J. , vol.174 , pp. 45-51
    • Davis, R.A.1    Showalter, R.2    Kern, F.3
  • 12
    • 0025981673 scopus 로고
    • Evidence for extralysosomal hydrolysis of high density lipoprotein cholesterol esters in rat hepatome cells (FU 5AH): A model for delivery of high density lipoprotein cholesterol
    • DeLamatre, J. G., R. M. Carter, and C. A. Hornick. Evidence for extralysosomal hydrolysis of high density lipoprotein cholesterol esters in rat hepatome cells (FU 5AH): a model for delivery of high density lipoprotein cholesterol. J. Cell. Physiol. 146: 18-24, 1991.
    • (1991) J. Cell. Physiol. , vol.146 , pp. 18-24
    • DeLamatre, J.G.1    Carter, R.M.2    Hornick, C.A.3
  • 13
    • 0027364908 scopus 로고
    • Evidence that a neutral cholesterol ester hydrolase is responsible for the extralysosomal hydrolysis of high density lipoprotein cholesterol ester in rat hepatoma cells
    • DeLamatre, J. G., R. M. Carter, and C. A. Hornick. Evidence that a neutral cholesterol ester hydrolase is responsible for the extralysosomal hydrolysis of high density lipoprotein cholesterol ester in rat hepatoma cells. J. Cell. Physiol. 157: 164-168, 1993.
    • (1993) J. Cell. Physiol. , vol.157 , pp. 164-168
    • DeLamatre, J.G.1    Carter, R.M.2    Hornick, C.A.3
  • 14
    • 0025275589 scopus 로고
    • Metabolism of apo E-free high density lipoproteins in rat hepatoma cells: Evidence for a retroendocytic pathway
    • DeLamatre, J. G., T. G. Sarphie, R. C. Archibold, and C. A. Hornick. Metabolism of apo E-free high density lipoproteins in rat hepatoma cells: evidence for a retroendocytic pathway. J. Lipid Res. 31: 191-202, 1990.
    • (1990) J. Lipid Res. , vol.31 , pp. 191-202
    • DeLamatre, J.G.1    Sarphie, T.G.2    Archibold, R.C.3    Hornick, C.A.4
  • 15
    • 0026850383 scopus 로고
    • Purification of pancreatic cholesterol esterase expressed in recombinant baculovirus-infected Sp9 cells
    • DiPersio, L. P., J. A. Kissel, and D. Y. Hui. Purification of pancreatic cholesterol esterase expressed in recombinant baculovirus-infected Sp9 cells. Protein Expr. Purif. 3: 114-120, 1992.
    • (1992) Protein Expr. Purif. , vol.3 , pp. 114-120
    • DiPersio, L.P.1    Kissel, J.A.2    Hui, D.Y.3
  • 16
    • 0028794049 scopus 로고
    • Plasma membrane caveolae mediate the efflux of cellular free cholesterol
    • Fielding, P. E., and C. J. Fielding. Plasma membrane caveolae mediate the efflux of cellular free cholesterol. Biochemistry 34: 14288-14292, 1995.
    • (1995) Biochemistry , vol.34 , pp. 14288-14292
    • Fielding, P.E.1    Fielding, C.J.2
  • 17
    • 0026728768 scopus 로고
    • Alterations in lipolytic activity at hepatic subcellular sites of fed and fasted rats
    • Cell Physiol. 31
    • Fu, D., and C. A. Hornick. Alterations in lipolytic activity at hepatic subcellular sites of fed and fasted rats. Am. J. Physiol. 262 (Cell Physiol. 31): C1102-C1108, 1992.
    • (1992) Am. J. Physiol. , vol.262
    • Fu, D.1    Hornick, C.A.2
  • 18
    • 0028798270 scopus 로고
    • Modulation of lipid metabolism at rat hepatic subcellular sites by female sex hormones
    • Fu, D., and C. A. Hornick. Modulation of lipid metabolism at rat hepatic subcellular sites by female sex hormones. Biochim. Biophys. Acta 1254: 267-273, 1995.
    • (1995) Biochim. Biophys. Acta , vol.1254 , pp. 267-273
    • Fu, D.1    Hornick, C.A.2
  • 19
    • 0025323167 scopus 로고
    • Sphingomyelin synthesis in rat liver occurs predominantly at the cis and medial cisternae of the Golgi apparatus
    • Futerman, A. H., B. Stieger, A. L. Hubbard, and R. E. Pagano. Sphingomyelin synthesis in rat liver occurs predominantly at the cis and medial cisternae of the Golgi apparatus. J. Biol. Chem. 265: 8650-8657, 1990.
    • (1990) J. Biol. Chem. , vol.265 , pp. 8650-8657
    • Futerman, A.H.1    Stieger, B.2    Hubbard, A.L.3    Pagano, R.E.4
  • 20
    • 0021673438 scopus 로고
    • Progress in understanding the LDL receptor and HMG-CoA reductase, two membrane proteins that regulate the plasma cholesterol
    • Goldstein, J. L., and M. S. Brown. Progress in understanding the LDL receptor and HMG-CoA reductase, two membrane proteins that regulate the plasma cholesterol. J. Lipid Res. 25: 1450-1457, 1984.
    • (1984) J. Lipid Res. , vol.25 , pp. 1450-1457
    • Goldstein, J.L.1    Brown, M.S.2
  • 21
    • 0026528446 scopus 로고
    • Low density lipoprotein receptor and cation independent mannose 6 phosphate receptor are transported from the cell surface to the Golgi at equal rates in PC12 cells
    • Green, S. A., and K. B. Kelly. Low density lipoprotein receptor and cation independent mannose 6 phosphate receptor are transported from the cell surface to the Golgi at equal rates in PC12 cells. J. Cell Biol. 117: 47-55, 1992.
    • (1992) J. Cell Biol. , vol.117 , pp. 47-55
    • Green, S.A.1    Kelly, K.B.2
  • 22
    • 0023816688 scopus 로고
    • Bile salt-dependent, neutral cholesterol ester hydrolase of rat liver: Possible relationship with pancreatic ester hydrolase
    • Harrison, E. H. Bile salt-dependent, neutral cholesterol ester hydrolase of rat liver: possible relationship with pancreatic ester hydrolase. Biochim. Biophys. Acta 963: 28-34, 1988.
    • (1988) Biochim. Biophys. Acta , vol.963 , pp. 28-34
    • Harrison, E.H.1
  • 23
    • 0021949360 scopus 로고
    • Isolation and characterization of multivesicular bodies from rat hepatocytes: An organelle distinct from secretory vesicles of the Golgi apparatus
    • Hornick, C. A., R. L. Hamilton, E. Spaziani, G. H. Enders, and B. J. Havel. Isolation and characterization of multivesicular bodies from rat hepatocytes: an organelle distinct from secretory vesicles of the Golgi apparatus. J. Cell Biol. 100: 1558-1569, 1985.
    • (1985) J. Cell Biol. , vol.100 , pp. 1558-1569
    • Hornick, C.A.1    Hamilton, R.L.2    Spaziani, E.3    Enders, G.H.4    Havel, B.J.5
  • 24
    • 0026646737 scopus 로고
    • Triacylglycerol hydrolysis in isolated hepatic endosomes
    • Hornick, C. A., C. Thouron, J. G. DeLamatre, and J. Huang. Triacylglycerol hydrolysis in isolated hepatic endosomes. J. Biol. Chem. 267: 3396-3401, 1992.
    • (1992) J. Biol. Chem. , vol.267 , pp. 3396-3401
    • Hornick, C.A.1    Thouron, C.2    DeLamatre, J.G.3    Huang, J.4
  • 25
    • 0028158809 scopus 로고
    • Androgenic modulation of lipid metabolism at subcellular sites in cholestatic rats
    • Hossain, A., and C. A. Hornick. Androgenic modulation of lipid metabolism at subcellular sites in cholestatic rats. Horm. Metab. Res. 26: 19-25, 1994.
    • (1994) Horm. Metab. Res. , vol.26 , pp. 19-25
    • Hossain, A.1    Hornick, C.A.2
  • 26
    • 0027401875 scopus 로고
    • Dissection of compartments in rat hepatocytes involved in the intracellular trafficking of high density lipoprotein particles or their selectively internalized cholesterol esters
    • Jäckle, S., F. Rinninger, T. Lorenzen, H. Greten, and E. Windler. Dissection of compartments in rat hepatocytes involved in the intracellular trafficking of high density lipoprotein particles or their selectively internalized cholesterol esters. Hepatology 17: 455-465, 1993.
    • (1993) Hepatology , vol.17 , pp. 455-465
    • Jäckle, S.1    Rinninger, F.2    Lorenzen, T.3    Greten, H.4    Windler, E.5
  • 27
    • 0028210170 scopus 로고
    • Synthesis of surface sphingomyelin in the plasma membrane recycling pathway of BHK cells
    • Kallen, K., D. Allan, J. Whatmore, and P. Quinn. Synthesis of surface sphingomyelin in the plasma membrane recycling pathway of BHK cells. Biochim. Biophys. Acta 1191: 52-58, 1994.
    • (1994) Biochim. Biophys. Acta , vol.1191 , pp. 52-58
    • Kallen, K.1    Allan, D.2    Whatmore, J.3    Quinn, P.4
  • 28
    • 0024829515 scopus 로고
    • Salvage of glucosylceramide by salvaging after internalization along the pathway of receptor mediated endocytosis
    • Kok, J. W., S. Eskelinen, K. Hoekstra, and D. Hoekstra. Salvage of glucosylceramide by salvaging after internalization along the pathway of receptor mediated endocytosis. Proc. Natl. Acad. Sci. USA 86: 9896-9900, 1989.
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 9896-9900
    • Kok, J.W.1    Eskelinen, S.2    Hoekstra, K.3    Hoekstra, D.4
  • 29
    • 0024383781 scopus 로고
    • Lipid recycling between the plasma membrane and intracellular compartments
    • Koval, M., and R. E. Pagano. Lipid recycling between the plasma membrane and intracellular compartments. J. Cell Biol. 108: 2169-2181, 1989.
    • (1989) J. Cell Biol. , vol.108 , pp. 2169-2181
    • Koval, M.1    Pagano, R.E.2
  • 30
    • 0020526090 scopus 로고
    • Internalization and subcellular localization of transferrin and transferrin receptors in HeLa cells
    • Lamb, J. E., F. Ray, J. H. Ward, J. P. Kushner, and J. Kaplan. Internalization and subcellular localization of transferrin and transferrin receptors in HeLa cells. J. Biol. Chem. 582: 8751-8758, 1983.
    • (1983) J. Biol. Chem. , vol.582 , pp. 8751-8758
    • Lamb, J.E.1    Ray, F.2    Ward, J.H.3    Kushner, J.P.4    Kaplan, J.5
  • 31
    • 0027322412 scopus 로고
    • Role of the plasma membrane in cholesterol esterification
    • Lange, Y., F. Strebel, and T. L. Steck. Role of the plasma membrane in cholesterol esterification. J. Biol. Chem. 268: 13838-13843, 1993.
    • (1993) J. Biol. Chem. , vol.268 , pp. 13838-13843
    • Lange, Y.1    Strebel, F.2    Steck, T.L.3
  • 32
    • 0024509922 scopus 로고
    • Plasma membranes contain half the phospholipid and 90% of the cholesterol and sphingomyelin in cultured human fibroblasts
    • Lange, Y., M. H. Swainsgood, B. Ramos, and T. L. Steck. Plasma membranes contain half the phospholipid and 90% of the cholesterol and sphingomyelin in cultured human fibroblasts. J. Biol. Chem. 264: 3786-3793, 1989.
    • (1989) J. Biol. Chem. , vol.264 , pp. 3786-3793
    • Lange, Y.1    Swainsgood, M.H.2    Ramos, B.3    Steck, T.L.4
  • 33
    • 0028245750 scopus 로고
    • Compartmentation of cholesterol within the cell
    • Liscum, L., and J. R. Faust. Compartmentation of cholesterol within the cell. Curr. Opin. Lipidol. 5: 221-226, 1994.
    • (1994) Curr. Opin. Lipidol. , vol.5 , pp. 221-226
    • Liscum, L.1    Faust, J.R.2
  • 34
    • 34548003946 scopus 로고
    • Efficient trace labelling of proteins with iodine
    • McFarlane, A. S. Efficient trace labelling of proteins with iodine. Nature 182: 53, 1958.
    • (1958) Nature , vol.182 , pp. 53
    • McFarlane, A.S.1
  • 35
    • 0020956251 scopus 로고
    • Filipin-cholesterol complexes form in uncoated vesicle membrane derived from coated vesicles during receptor mediated endocytosis of low density lipoprotein
    • McGookey, D. J., K. Fagerberg, and R. G. W. Anderson. Filipin-cholesterol complexes form in uncoated vesicle membrane derived from coated vesicles during receptor mediated endocytosis of low density lipoprotein. J. Cell Biol. 96: 1273-1278, 1983.
    • (1983) J. Cell Biol. , vol.96 , pp. 1273-1278
    • McGookey, D.J.1    Fagerberg, K.2    Anderson, R.G.W.3
  • 36
    • 0026658579 scopus 로고
    • Apolipoproteins, membrane cholesterol domains and the regulation of cholesterol efflux
    • Rothblat, G. H., F. H. Mahlberg, W. J. Johnson, and M. C. Phillips. Apolipoproteins, membrane cholesterol domains and the regulation of cholesterol efflux. J. Lipid Res. 33: 1091-1097, 1992.
    • (1992) J. Lipid Res. , vol.33 , pp. 1091-1097
    • Rothblat, G.H.1    Mahlberg, F.H.2    Johnson, W.J.3    Phillips, M.C.4
  • 37
    • 0024425541 scopus 로고
    • Intracellular transport of cholesterol in type C Niemann-Pick fibroblasts
    • Slotte, J. P., G. Hedstrom, and E. L. Bierman. Intracellular transport of cholesterol in type C Niemann-Pick fibroblasts. Biochim. Biophys. Acta 1005: 303-309, 1989.
    • (1989) Biochim. Biophys. Acta , vol.1005 , pp. 303-309
    • Slotte, J.P.1    Hedstrom, G.2    Bierman, E.L.3
  • 38
    • 0021272476 scopus 로고
    • Detection of membrane cholesterol by filipin in isolated rat liver coated vesicles is dependent upon removal of clathrin coat
    • Steer, C. J., M. Bisher, R. Blumenthal, and A. C. Steven. Detection of membrane cholesterol by filipin in isolated rat liver coated vesicles is dependent upon removal of clathrin coat. J. Cell Biol. 99: 315-319, 1984.
    • (1984) J. Cell Biol. , vol.99 , pp. 315-319
    • Steer, C.J.1    Bisher, M.2    Blumenthal, R.3    Steven, A.C.4
  • 39
    • 0026338739 scopus 로고
    • The influence of particle size and multiple apoprotein E receptor interactions on the endocytic targetting of VLDL in mouse peritoneal macrophages
    • Tabas, I., J. N. Myers, T. L. Innerarity, X. Xiang-Xi, K. Arnold, J. Boyles, and F. R. Maxfield. The influence of particle size and multiple apoprotein E receptor interactions on the endocytic targetting of VLDL in mouse peritoneal macrophages. J. Cell Biol. 115: 1547-1560, 1992.
    • (1992) J. Cell Biol. , vol.115 , pp. 1547-1560
    • Tabas, I.1    Myers, J.N.2    Innerarity, T.L.3    Xiang-Xi, X.4    Arnold, K.5    Boyles, J.6    Maxfield, F.R.7
  • 40
    • 0023724514 scopus 로고
    • Receptor mediated endocytosis of high density lipoprotein by rat sinusoidal liver cells: Identification of a nonlysosomal endocytic pathway by fluorescence labeled ligand
    • Takata, K., S. Horiuchi, A. M. A. Rahim, and Y. Morino. Receptor mediated endocytosis of high density lipoprotein by rat sinusoidal liver cells: identification of a nonlysosomal endocytic pathway by fluorescence labeled ligand. J. Lipid Res. 29: 1117-1126, 1988.
    • (1988) J. Lipid Res. , vol.29 , pp. 1117-1126
    • Takata, K.1    Horiuchi, S.2    Rahim, A.M.A.3    Morino, Y.4
  • 41
    • 0024269716 scopus 로고
    • Endosomes differ from plasma membranes in phospholipid molecular species composition
    • Urade, R., Y. Hayashi, and M. Kito. Endosomes differ from plasma membranes in phospholipid molecular species composition. Biochim. Biophys. Acta 946: 151-163, 1988.
    • (1988) Biochim. Biophys. Acta , vol.946 , pp. 151-163
    • Urade, R.1    Hayashi, Y.2    Kito, M.3
  • 42
    • 0020580252 scopus 로고
    • Sterol partitioning among intracellular membranes
    • Wattenberg, B. W., and D. F. Silbert. Sterol partitioning among intracellular membranes. J. Biol. Chem. 258: 2284-2289, 1983.
    • (1983) J. Biol. Chem. , vol.258 , pp. 2284-2289
    • Wattenberg, B.W.1    Silbert, D.F.2
  • 43
    • 0026077761 scopus 로고
    • Lipoproteins activate acyl-coenzyme A:cholesterol acyltransferase in macrophages only after cellular cholesterol pools are expanded to a critical threshold level
    • Xiang-Xi, X., and I. Tabas. 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, 1994.
    • (1994) J. Biol. Chem. , vol.266 , pp. 17040-17048
    • Xiang-Xi, X.1    Tabas, I.2


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