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Volumn 262, Issue 3, 1999, Pages 939-946

The effect of interleukin 1β on the biosynthesis of cholesterol, phosphatidylcholine, and sphingomyelin in fibroblasts, and on their efflux from cells to lipid-free apolipoprotein A-I

Author keywords

Cholesterol; Cholesterol efflux; Interleukin 1 ; Phosphatidylcholine; Sphingomyelin

Indexed keywords

APOLIPOPROTEIN A1; CHOLESTEROL; CHOLESTEROL ACYLTRANSFERASE; CHOLESTEROL ESTER; OLEIC ACID; PHOSPHATIDYLCHOLINE; RECOMBINANT INTERLEUKIN 1BETA; SPHINGOMYELIN; SPHINGOMYELIN PHOSPHODIESTERASE;

EID: 0033564375     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1432-1327.1999.00484.x     Document Type: Article
Times cited : (7)

References (51)
  • 2
    • 0028143674 scopus 로고
    • The IL-1 receptor signaling pathway
    • 2. Kuno, K. & Matsushima, K. (1994) The IL-1 receptor signaling pathway. J. Leukoc. Biol. 56, 542-547.
    • (1994) J. Leukoc. Biol. , vol.56 , pp. 542-547
    • Kuno, K.1    Matsushima, K.2
  • 3
    • 0027461121 scopus 로고
    • Activation of the sphingomyelin signaling pathway in intact EL4 cells and in a cell-free system by IL-1 beta
    • 3. Mathias, S., Younes, A., Kan, C.-C., Orlow, I., Joseph, C. & Kolesnick, R.N. (1993) Activation of the sphingomyelin signaling pathway in intact EL4 cells and in a cell-free system by IL-1 beta. Science 259, 519-522.
    • (1993) Science , vol.259 , pp. 519-522
    • Mathias, S.1    Younes, A.2    Kan, C.-C.3    Orlow, I.4    Joseph, C.5    Kolesnick, R.N.6
  • 4
    • 0031037134 scopus 로고    scopus 로고
    • Interleukin 1-beta-induced protein kinase C-zeta activation is mimicked by exogenous phospholipase D
    • 4. Limatola, C., Barabino, B., Nista, A. & Santoni, A. (1997) Interleukin 1-beta-induced protein kinase C-zeta activation is mimicked by exogenous phospholipase D. Biochem. J. 321, 497-501.
    • (1997) Biochem. J. , vol.321 , pp. 497-501
    • Limatola, C.1    Barabino, B.2    Nista, A.3    Santoni, A.4
  • 5
    • 0023809589 scopus 로고
    • Interleukin-1 stimulates diacylglycerol production in T lymphocytes by a novel mechanism
    • 5. Rosoff, P.M., Savage, N. & Dinarello, C.A. (1988) Interleukin-1 stimulates diacylglycerol production in T lymphocytes by a novel mechanism. Cell 54, 73-81.
    • (1988) Cell , vol.54 , pp. 73-81
    • Rosoff, P.M.1    Savage, N.2    Dinarello, C.A.3
  • 6
    • 0026726492 scopus 로고
    • Interleukin-1-mediated PGE2 production and sphingomyelin metabolism. Evidence for the regulation of cyclooxygenase gene expression by sphingosine and ceramide
    • 6. Ballou, L.R., Chao, C.P., Holness, M.A., Barker, S.C. & Raghovv, R. (1992) Interleukin-1-mediated PGE2 production and sphingomyelin metabolism. Evidence for the regulation of cyclooxygenase gene expression by sphingosine and ceramide. J. Biol. Chem. 267, 20044-20050.
    • (1992) J. Biol. Chem. , vol.267 , pp. 20044-20050
    • Ballou, L.R.1    Chao, C.P.2    Holness, M.A.3    Barker, S.C.4    Raghovv, R.5
  • 7
    • 0029913791 scopus 로고    scopus 로고
    • Interleukin 1 stimulates cholesterol esterification and cholesterol deposition in J774 monocytes-macrophages
    • 7. Mazière, C., Barbu, V., Auclair, M. & Mazière, J.-C. (1996) Interleukin 1 stimulates cholesterol esterification and cholesterol deposition in J774 monocytes-macrophages. Biochim. Biophys. Acta 1300, 30-34.
    • (1996) Biochim. Biophys. Acta , vol.1300 , pp. 30-34
    • Mazière, C.1    Barbu, V.2    Auclair, M.3    Mazière, J.-C.4
  • 8
    • 0023839340 scopus 로고
    • Depletion of plasma-membrane sphingomyelin rapidly alters the distribution of cholesterol between plasma membranes and intracellular cholesterol pools in cultured fibroblasts
    • 8. Slotte, J.P. & Bierman, E.L. (1988) Depletion of plasma-membrane sphingomyelin rapidly alters the distribution of cholesterol between plasma membranes and intracellular cholesterol pools in cultured fibroblasts. Biochem. J. 250, 653-658.
    • (1988) Biochem. J. , vol.250 , pp. 653-658
    • Slotte, J.P.1    Bierman, E.L.2
  • 9
    • 0024419722 scopus 로고
    • Effects of sphingomyelin degradation on cell cholesterol oxidizability and steady-state distribution between the cell surface and the cell interior
    • 9. Slotte, J.P., Hedström, G., Rannström, S. & Ekman, S. (1989) Effects of sphingomyelin degradation on cell cholesterol oxidizability and steady-state distribution between the cell surface and the cell interior. Biochim. Biophys. Acta 985, 90-96.
    • (1989) Biochim. Biophys. Acta , vol.985 , pp. 90-96
    • Slotte, J.P.1    Hedström, G.2    Rannström, S.3    Ekman, S.4
  • 10
    • 0025187705 scopus 로고
    • Reversible effects of sphingomyelin degradation on cholesterol distribution and metabolism in fibroblasts and transformed neuroblastoma cells
    • 10. Pörn, M.I. & Slotte, J.P. (1990) Reversible effects of sphingomyelin degradation on cholesterol distribution and metabolism in fibroblasts and transformed neuroblastoma cells. Biochem. J. 271, 121-126.
    • (1990) Biochem. J. , vol.271 , pp. 121-126
    • Pörn, M.I.1    Slotte, J.P.2
  • 11
    • 0025757185 scopus 로고
    • Increased steroid hormone secretion in mouse Leydig tumor cells after induction of cholesterol translocation by sphingomyelin degradation
    • 11. Pörn, M.I., Tenhunen, J. & Slotte, J.P. (1991) Increased steroid hormone secretion in mouse Leydig tumor cells after induction of cholesterol translocation by sphingomyelin degradation. Biochim. Biophys. Acta 1093, 7-12.
    • (1991) Biochim. Biophys. Acta , vol.1093 , pp. 7-12
    • Pörn, M.I.1    Tenhunen, J.2    Slotte, J.P.3
  • 12
    • 0024509922 scopus 로고
    • Plasma membranes contain half the phospholipid and 90% of the cholesterol and sphingomyelin in cultured human fibroblasts
    • 12. Lange, Y., Swaisgood, M.H., Ramos, B.V. & Steck, T.L. (1989) Plasma membranes contain half the phospholipid and 90% of the cholesterol and sphingomyelin in cultured human fibroblasts. J. Biol. Chem. 264, 3786-3793.
    • (1989) J. Biol. Chem. , vol.264 , pp. 3786-3793
    • Lange, Y.1    Swaisgood, M.H.2    Ramos, B.V.3    Steck, T.L.4
  • 13
    • 0025975875 scopus 로고
    • Disposition of intracellular cholesterol in human fibroblasts
    • 13. 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
  • 15
    • 0020580252 scopus 로고
    • Sterol partitioning among intracellular membranes. Testing a model for cellular sterol distribution
    • 15. Wattenberg, B.W. & Silbert, D.F. (1983) Sterol partitioning among intracellular membranes. Testing a model for cellular sterol distribution. J. biol. Chem. 258, 2284-2289.
    • (1983) J. Biol. Chem. , vol.258 , pp. 2284-2289
    • Wattenberg, B.W.1    Silbert, D.F.2
  • 16
    • 0027250457 scopus 로고
    • Degradation of plasma membrane phosphatidylcholine appears not to affect the cellular cholesterol distribution
    • 16. Pörn, M.I., Ares, M.P.S. & Slotte, J.P. (1993) Degradation of plasma membrane phosphatidylcholine appears not to affect the cellular cholesterol distribution. J. Lipid Res. 34, 1385-1392.
    • (1993) J. Lipid Res. , vol.34 , pp. 1385-1392
    • Pörn, M.I.1    Ares, M.P.S.2    Slotte, J.P.3
  • 17
    • 0003029124 scopus 로고
    • A review of the kinetics of cholesterol movement between donor and acceptor bilayer membranes
    • Finegold, L.X., ed., CRC Press, Boca Raton, FL
    • 17. Bittman, R. (1993) A review of the kinetics of cholesterol movement between donor and acceptor bilayer membranes. In Cholesterol in Membrane Models. (Finegold, L.X., ed.), pp. 45-65. CRC Press, Boca Raton, FL.
    • (1993) Cholesterol in Membrane Models , pp. 45-65
    • Bittman, R.1
  • 19
    • 33745026603 scopus 로고
    • The distribution and chemical composition of ultracentrifugally separated lipoproleins in human serum
    • 19. Havel, R.J., Eder, H.A. & Bragdon, J.H. (1955) The distribution and chemical composition of ultracentrifugally separated lipoproleins in human serum. J. Clin. Invest. 34, 1345-1355.
    • (1955) J. Clin. Invest. , vol.34 , pp. 1345-1355
    • Havel, R.J.1    Eder, H.A.2    Bragdon, J.H.3
  • 20
    • 0022556074 scopus 로고
    • Sequential flotation ultracentrifugation
    • 20. Schumaker, V.N. & Puppione, D.L. (1986) Sequential flotation ultracentrifugation. Methods Enzymol. 128, 155-170.
    • (1986) Methods Enzymol. , vol.128 , pp. 155-170
    • Schumaker, V.N.1    Puppione, D.L.2
  • 22
    • 0022556160 scopus 로고
    • Receptor-mediated transport of cholesterol between cultured cells and HDLs
    • 22. Oram, J.F. (1986) Receptor-mediated transport of cholesterol between cultured cells and HDLs. Methods Enzymol. 129, 645-659.
    • (1986) Methods Enzymol. , vol.129 , pp. 645-659
    • Oram, J.F.1
  • 23
    • 0016691608 scopus 로고
    • Cholesterol ester formation in cultured human fibroblasts. Stimulation by oxygenated sterols
    • 23. Brown, M.S., Dana, S.E. & Goldstein, J.L. (1975) Cholesterol ester formation in cultured human fibroblasts. Stimulation by oxygenated sterols. J. Biol. Chem. 250, 4025-4027.
    • (1975) J. Biol. Chem. , vol.250 , pp. 4025-4027
    • Brown, M.S.1    Dana, S.E.2    Goldstein, J.L.3
  • 24
    • 0027422092 scopus 로고
    • Spingosine inhibits spingomyelinase-induced cholesteryl ester formation in cultured fibroblasts
    • 24. Härmälä, A.-S., Pörn, M.I. & Slotte, J.P. (1993) Spingosine inhibits spingomyelinase-induced cholesteryl ester formation in cultured fibroblasts. Biochim. Biophys. Acta 1210, 97-104.
    • (1993) Biochim. Biophys. Acta , vol.1210 , pp. 97-104
    • Härmälä, A.-S.1    Pörn, M.I.2    Slotte, J.P.3
  • 25
    • 75549109174 scopus 로고
    • Quantitative analysis of phospholipids by TLC
    • 25. Skipski, V.P., Peterson, R.F. & Barclay, M. (1964) Quantitative analysis of phospholipids by TLC. Biochem. J. 90, 374-378.
    • (1964) Biochem. J. , vol.90 , pp. 374-378
    • Skipski, V.P.1    Peterson, R.F.2    Barclay, M.3
  • 26
    • 70449246528 scopus 로고
    • Phosphorus assay in column chromatography
    • 26. Bartlett, G.R. (1958) Phosphorus assay in column chromatography. J. Biol. Chem. 234, 466-468.
    • (1958) J. Biol. Chem. , vol.234 , pp. 466-468
    • Bartlett, G.R.1
  • 27
    • 0028076002 scopus 로고
    • The role of diacylglycerol and ceramide in tumor necrosis factor and interleukin-1 signal transduction
    • 27. Schütze, S., Machleidt, T. & Krönke, M. (1994) The role of diacylglycerol and ceramide in tumor necrosis factor and interleukin-1 signal transduction, J. Leukoc. Biol. 56, 533-541.
    • (1994) J. Leukoc. Biol. , vol.56 , pp. 533-541
    • Schütze, S.1    Machleidt, T.2    Krönke, M.3
  • 28
    • 0028297068 scopus 로고
    • The sphingomyelin pathway in tumor necrosis factor and interleukin-1 signaling
    • 28. Kolesnick, R. & Golde, D.W. (1994) The sphingomyelin pathway in tumor necrosis factor and interleukin-1 signaling. Cell 77, 325-328.
    • (1994) Cell , vol.77 , pp. 325-328
    • Kolesnick, R.1    Golde, D.W.2
  • 29
    • 0028031699 scopus 로고
    • Neutral sphingomyelinase action stimulates signal transduction of tumor necrosis factor-alpha in the synthesis of cholesteryl esters in human fibroblasts
    • 29. Chatterjee, S. (1994) Neutral sphingomyelinase action stimulates signal transduction of tumor necrosis factor-alpha in the synthesis of cholesteryl esters in human fibroblasts. J. Biol Chem. 269, 879-882.
    • (1994) J. Biol Chem. , vol.269 , pp. 879-882
    • Chatterjee, S.1
  • 30
    • 0027322412 scopus 로고
    • Role of the plasma membrane in cholesterol esterification in rat hepatoma cells
    • 30. Lange, Y., Strebel, F. & Steck, T.L. (1993) Role of the plasma membrane in cholesterol esterification in rat hepatoma cells. J. Biol. Chem. 268, 13838-13843.
    • (1993) J. Biol. Chem. , vol.268 , pp. 13838-13843
    • Lange, Y.1    Strebel, F.2    Steck, T.L.3
  • 31
    • 0031912029 scopus 로고    scopus 로고
    • Interleukin-1 beta stimulates mitogen-activated protein kinase in U373 astrocytoma cells without the production of lipid second messengers
    • 31. Utal, A.K., Stopka, A.L. & Coleman, P.D. (1997) Interleukin-1 beta stimulates mitogen-activated protein kinase in U373 astrocytoma cells without the production of lipid second messengers. Neurochem. Res. 23, 235-242.
    • (1997) Neurochem. Res. , vol.23 , pp. 235-242
    • Utal, A.K.1    Stopka, A.L.2    Coleman, P.D.3
  • 32
    • 0029932759 scopus 로고    scopus 로고
    • Interleukin-1 beta-induced ceramide and diacylglycerol generation may lead to activation of the c-Jun NH2-terminal kinase and the transcription factor ATF2 in the insulin-producing cell line RINm5F
    • 32. Welsh, N. (1996) Interleukin-1 beta-induced ceramide and diacylglycerol generation may lead to activation of the c-Jun NH2-terminal kinase and the transcription factor ATF2 in the insulin-producing cell line RINm5F. J. Biol. Chem. 271, 8307-8312.
    • (1996) J. Biol. Chem. , vol.271 , pp. 8307-8312
    • Welsh, N.1
  • 33
    • 0029943654 scopus 로고    scopus 로고
    • Cyclodextrin-mediated removal of sterols from monolayers: Effects of sterol structure and phospholipids on desorption rate
    • 33. Ohvo, H. & Slotle, J.P. ( 1996) Cyclodextrin-mediated removal of sterols from monolayers: effects of sterol structure and phospholipids on desorption rate. Biochemistry 35, 8018-8024.
    • (1996) Biochemistry , vol.35 , pp. 8018-8024
    • Ohvo, H.1    Slotle, J.P.2
  • 34
    • 0031573424 scopus 로고    scopus 로고
    • Effects of sphingomyelin and phosphatidylcholine degradation on cyclodextrin-mediated cholesterol efflux in cultured fibroblasts
    • 34. Ohvo, H., Olsio, C. & Slotte, J.P. (1997) Effects of sphingomyelin and phosphatidylcholine degradation on cyclodextrin-mediated cholesterol efflux in cultured fibroblasts. Biochim. Biophys. Acta 1349, 131-141.
    • (1997) Biochim. Biophys. Acta , vol.1349 , pp. 131-141
    • Ohvo, H.1    Olsio, C.2    Slotte, J.P.3
  • 35
    • 0019728872 scopus 로고
    • The effects of subfractions of high density lipoprotein on cholesterol efflux from cultured fibroblasts. Regulation of low density lipoprotein receptor activity
    • 35. Oram, J.F., Albers, J.J., Cheung, M.C. & Bierman, E.L. (1981) The effects of subfractions of high density lipoprotein on cholesterol efflux from cultured fibroblasts. Regulation of low density lipoprotein receptor activity. J. Biol. Chem. 256, 8348-8356.
    • (1981) J. Biol. Chem. , vol.256 , pp. 8348-8356
    • Oram, J.F.1    Albers, J.J.2    Cheung, M.C.3    Bierman, E.L.4
  • 36
    • 0025728398 scopus 로고
    • Interaction of free apolipoproteins with macrophages. Formation of high density lipoprotein-like lipoproteins and reduction of cellular cholesterol
    • 36. Hara, H. & Yokoyama, S. (1991) Interaction of free apolipoproteins with macrophages. Formation of high density lipoprotein-like lipoproteins and reduction of cellular cholesterol. J. Biol. Chem. 266, 3080-3086.
    • (1991) J. Biol. Chem. , vol.266 , pp. 3080-3086
    • Hara, H.1    Yokoyama, S.2
  • 37
    • 0023663531 scopus 로고
    • Mechanisms and consequences of cellular cholesterol exchange and transfer
    • 37. Phillips, M.C., Johnson, W.J. & Rothblat, G.H. (1987) Mechanisms and consequences of cellular cholesterol exchange and transfer. Biochim. Biophys. Acta 906, 223-276.
    • (1987) Biochim. Biophys. Acta , vol.906 , pp. 223-276
    • Phillips, M.C.1    Johnson, W.J.2    Rothblat, G.H.3
  • 38
    • 0026465419 scopus 로고
    • Efflux of lipid from fibroblasts to apolipoproteins: Dependence on elevated levels of cellular unesterified cholesterol
    • 38. Biclicki, J.K., Johnson, W.J., Weinberg, R.B., Click, J.M. & Rothblat, G.H. (1992) Efflux of lipid from fibroblasts to apolipoproteins: dependence on elevated levels of cellular unesterified cholesterol. J. Lipid Res. 33, 1699-1709.
    • (1992) J. Lipid Res. , vol.33 , pp. 1699-1709
    • Biclicki, J.K.1    Johnson, W.J.2    Weinberg, R.B.3    Click, J.M.4    Rothblat, G.H.5
  • 39
    • 0026623112 scopus 로고
    • Role of apolipoproteins in cholesterol efflux from macrophages to lipid microemulsion: Proposal of a putative model for the pre-beta high-density lipoprotein pathway
    • 39. Hara, H. & Yokoyama, S. (1992) Role of apolipoproteins in cholesterol efflux from macrophages to lipid microemulsion: proposal of a putative model for the pre-beta high-density lipoprotein pathway. Biochemistry 31, 2040-2046.
    • (1992) Biochemistry , vol.31 , pp. 2040-2046
    • Hara, H.1    Yokoyama, S.2
  • 40
    • 0027254395 scopus 로고
    • Cholesterol is poorly available for free apolipoprotein-mediated cellular lipid efflux from smooth muscle cells
    • 40. Li, Q., Komaba, A. & Yokoyama, S. (1993) Cholesterol is poorly available for free apolipoprotein-mediated cellular lipid efflux from smooth muscle cells. Biochemistry 32, 4597-1603.
    • (1993) Biochemistry , vol.32 , pp. 4597-11603
    • Li, Q.1    Komaba, A.2    Yokoyama, S.3
  • 41
    • 0027499052 scopus 로고
    • Apolipoprotein A-I-cell membrane interaction: Extracellular assembly of heterogeneous nascent HDL particles
    • 41. Forte, T.M., Goth-Goldstein, R., Nordhausen, R.W. & McCall, M.R. (1993) Apolipoprotein A-I-cell membrane interaction: extracellular assembly of heterogeneous nascent HDL particles. J. Lipid Res. 34, 317-324.
    • (1993) J. Lipid Res. , vol.34 , pp. 317-324
    • Forte, T.M.1    Goth-Goldstein, R.2    Nordhausen, R.W.3    McCall, M.R.4
  • 42
    • 0023503102 scopus 로고
    • Binding of high density lipoproteins to cell receptors promotes translocation of cholesterol from intracellular membranes to the cell surface
    • 42. Slotte, J.P., Oram, J.F. & Bierman, E.L. (1987) Binding of high density lipoproteins to cell receptors promotes translocation of cholesterol from intracellular membranes to the cell surface. J. Biol. Chem. 262, 12904-12907.
    • (1987) J. Biol. Chem. , vol.262 , pp. 12904-12907
    • Slotte, J.P.1    Oram, J.F.2    Bierman, E.L.3
  • 43
    • 0024494693 scopus 로고
    • High density lipoprotein stimulates sterol translocation between intracellular and plasma membrane pools in human monocyte-derived macrophages
    • 43. Aviram, M., Bierman, E.L. & Oram, J.F. (1989) High density lipoprotein stimulates sterol translocation between intracellular and plasma membrane pools in human monocyte-derived macrophages. J. Lipid Res. 30, 65-76.
    • (1989) J. Lipid Res. , vol.30 , pp. 65-76
    • Aviram, M.1    Bierman, E.L.2    Oram, J.F.3
  • 44
    • 0026644329 scopus 로고
    • Cellular cholesterol efflux. Role of cell membrane kinetic pools and interaction with apolipoproteins AI, AII, and Cs
    • 44. Mahlberg, F.H. & Rothblat, G.H. (1991) Cellular cholesterol efflux. Role of cell membrane kinetic pools and interaction with apolipoproteins AI, AII, and Cs. J. Biol. Chem. 267, 4541-4550.
    • (1991) J. Biol. Chem. , vol.267 , pp. 4541-4550
    • Mahlberg, F.H.1    Rothblat, G.H.2
  • 45
    • 0026658579 scopus 로고
    • Apolipoproteins, membrane cholesterol domains, and the regulation of cholesterol efflux
    • 45. Rothblat, G.H., Mahlberg, F.H., Johnson, W.J. & Phillips, M.C. (1992) Apolipoproteins, membrane cholesterol domains, and the regulation of cholesterol efflux. J. Lipid Res. 33, 1091-1097.
    • (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
  • 47
    • 0026512314 scopus 로고
    • Sorting of GPI-anchored proteins to glycolipid enriched membrane subdomains during transport to the apical cell surface
    • 47. Brown, D.A. & Rose, J.K. (1992) Sorting of GPI-anchored proteins to glycolipid enriched membrane subdomains during transport to the apical cell surface. Cell 68, 533-544.
    • (1992) Cell , vol.68 , pp. 533-544
    • Brown, D.A.1    Rose, J.K.2
  • 48
    • 0025695634 scopus 로고
    • Cholesterol controls the clustering of the glycophospholipid-anchored membrane receptor for 5-methyltetrahydrofolate
    • 48. Rothberg, K.G., Ying, Y., Kamen, B.A. & Andersson, R.W. (1990) Cholesterol controls the clustering of the glycophospholipid-anchored membrane receptor for 5-methyltetrahydrofolate. J. Cell Biol. 111, 2931-2938.
    • (1990) J. Cell Biol. , vol.111 , pp. 2931-2938
    • Rothberg, K.G.1    Ying, Y.2    Kamen, B.A.3    Andersson, R.W.4
  • 49
    • 0025303751 scopus 로고
    • The glycophospholipid-linked folate receptor internalizes folate without entering the clathrin-coated pit endocytic pathway
    • 49. Rothberg, K.G., Ying, Y., Kolhouse, J.F., Kamen, B.A. & Andersson, R.G.W. (1990) The glycophospholipid-linked folate receptor internalizes folate without entering the clathrin-coated pit endocytic pathway. J. Cell Biol. 110, 637-649.
    • (1990) J. Cell Biol. , vol.110 , pp. 637-649
    • Rothberg, K.G.1    Ying, Y.2    Kolhouse, J.F.3    Kamen, B.A.4    Andersson, R.G.W.5
  • 50
    • 0027275642 scopus 로고
    • Signal transducing molecules and glycosyl-phosphatidylinositol-linked proteins form a caveolin-rich insoluble complex in MDCK cells
    • 50. Sargiacomo, M., Sudol, M., Tang, Z.-L. & Lisanti, M.P. (1993) Signal transducing molecules and glycosyl-phosphatidylinositol-linked proteins form a caveolin-rich insoluble complex in MDCK cells. J. Cell Biol. 122, 789-807.
    • (1993) J. Cell Biol. , vol.122 , pp. 789-807
    • Sargiacomo, M.1    Sudol, M.2    Tang, Z.-L.3    Lisanti, M.P.4
  • 51
    • 0028794049 scopus 로고
    • Plasma membrane caveolae mediate the efflux of cellular free cholesterol
    • 51. Fielding, P.E. & Fielding, C.J. (1995) Plasma membrane caveolae mediate the efflux of cellular free cholesterol. Biochemistry 34, 14288-14292.
    • (1995) Biochemistry , vol.34 , pp. 14288-14292
    • Fielding, P.E.1    Fielding, C.J.2


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