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Volumn 40, Issue 1, 1999, Pages 1-16

Remnant lipoprotein metabolism: Key pathways involving cell-surface heparan sulfate proteoglycans and apolipoprotein E

Author keywords

Apolipoprotein E; Heparan sulfate proteoglycans; Hepatic lipase; Lipoprotein lipase; Remnants

Indexed keywords

APOLIPOPROTEIN E; CHYLOMICRON; HEPARAN SULFATE; LIPOPROTEIN; LIPOPROTEIN LIPASE; LOW DENSITY LIPOPROTEIN; LOW DENSITY LIPOPROTEIN RECEPTOR; PROTEOGLYCAN;

EID: 0032895028     PISSN: 00222275     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Review
Times cited : (580)

References (126)
  • 1
    • 0022413810 scopus 로고
    • Atherogenic lipoproteins and coronary artery disease: Concepts derived from recent advances in cellular and molecular biology
    • Mahley, R. W. 1985. Atherogenic lipoproteins and coronary artery disease: concepts derived from recent advances in cellular and molecular biology. Circulation. 72: 943-948.
    • (1985) Circulation , vol.72 , pp. 943-948
    • Mahley, R.W.1
  • 2
    • 0025964011 scopus 로고
    • Genetic defects in lipoprotein metabolism. Elevation of atherogenic lipoproteins caused by impaired catabolism
    • Mahley, R. W., K. H. Weisgraber, T. L. Innerarity, and S. C. Rall, Jr. 1991. Genetic defects in lipoprotein metabolism. Elevation of atherogenic lipoproteins caused by impaired catabolism. J. Am. Med. Assoc. 265: 78-83.
    • (1991) J. Am. Med. Assoc. , vol.265 , pp. 78-83
    • Mahley, R.W.1    Weisgraber, K.H.2    Innerarity, T.L.3    Rall S.C., Jr.4
  • 3
    • 0002235065 scopus 로고    scopus 로고
    • Disorders of lipid metabolism
    • J. D. Wilson, D. W. Foster, H. M. Kronenberg, and P. R. Larsen, editors. W.B. Saunders, Philadelphia
    • Mahley, R. W., K. H. Weisgraber, and R. V. Farese, Jr. 1998. Disorders of lipid metabolism. In Williams Textbook of Endocrinology. 9th edition. J. D. Wilson, D. W. Foster, H. M. Kronenberg, and P. R. Larsen, editors. W.B. Saunders, Philadelphia. 1099-1153.
    • (1998) Williams Textbook of Endocrinology. 9th Edition , pp. 1099-1153
    • Mahley, R.W.1    Weisgraber, K.H.2    Farese R.V., Jr.3
  • 4
    • 0022549920 scopus 로고
    • A receptor-mediated pathway for cholesterol homeostasis
    • Brown, M. S., and J. L. Goldstein. 1986. A receptor-mediated pathway for cholesterol homeostasis. Science. 232: 34-47.
    • (1986) Science , vol.232 , pp. 34-47
    • Brown, M.S.1    Goldstein, J.L.2
  • 5
    • 0024299370 scopus 로고
    • Apolipoprotein E: Cholesterol transport protein with expanding role in cell biology
    • Mahley, R. W. 1988. Apolipoprotein E: cholesterol transport protein with expanding role in cell biology. Science. 240: 622-630.
    • (1988) Science , vol.240 , pp. 622-630
    • Mahley, R.W.1
  • 6
    • 0019877031 scopus 로고
    • Lipoprotein binding to canine hepatic membranes. Metabolically distinct apoE and apoB,E receptors
    • Hui, D. Y., T. L. Innerarity, and R. W. Mahley. 1981. Lipoprotein binding to canine hepatic membranes. Metabolically distinct apoE and apoB,E receptors. J. Biol. Chem. 256: 5646-5655.
    • (1981) J. Biol. Chem. , vol.256 , pp. 5646-5655
    • Hui, D.Y.1    Innerarity, T.L.2    Mahley, R.W.3
  • 7
    • 0021685314 scopus 로고
    • Binding of chylomicron remnants and β-very low density lipoproteins to hepatic and extrahepatic lipoprotein receptors. A process independent of apolipoprotein B48
    • Hui, D. Y., T. L. Innerarity, R. W. Milne, Y. L. Marcel, and R. W. Mahley. 1984. Binding of chylomicron remnants and β-very low density lipoproteins to hepatic and extrahepatic lipoprotein receptors. A process independent of apolipoprotein B48. J. Biol. Chem. 259: 15060-15068.
    • (1984) J. Biol. Chem. , vol.259 , pp. 15060-15068
    • Hui, D.Y.1    Innerarity, T.L.2    Milne, R.W.3    Marcel, Y.L.4    Mahley, R.W.5
  • 8
    • 0001665337 scopus 로고
    • Surface location and high affinity for calcium of a 500-kd liver membrane protein closely related to the LDL-receptor suggest a physiological role as lipoprotein receptor
    • Herz, J., U. Hamann, S. Rogne, O. Myklebost, H. Gausepohl, and K. K. Stanley. 1988. Surface location and high affinity for calcium of a 500-kd liver membrane protein closely related to the LDL-receptor suggest a physiological role as lipoprotein receptor. EMBO J. 7: 4119-4127.
    • (1988) EMBO J. , vol.7 , pp. 4119-4127
    • Herz, J.1    Hamann, U.2    Rogne, S.3    Myklebost, O.4    Gausepohl, H.5    Stanley, K.K.6
  • 11
    • 0027532494 scopus 로고
    • The LDL-receptor-related protein - Portrait of a multifunctional receptor
    • Herz, J. 1993. The LDL-receptor-related protein - portrait of a multifunctional receptor. Curr. Opin. Lipidol. 4: 107-113.
    • (1993) Curr. Opin. Lipidol. , vol.4 , pp. 107-113
    • Herz, J.1
  • 12
    • 0028173897 scopus 로고
    • Structures and functions of multiligand lipoprotein receptors: Macrophage scavenger receptors and LDL receptor-related protein (LRP)
    • Krieger, M., and J. Herz. 1994. Structures and functions of multiligand lipoprotein receptors: macrophage scavenger receptors and LDL receptor-related protein (LRP). Annu. Rev. Biochem. 63: 601-637.
    • (1994) Annu. Rev. Biochem. , vol.63 , pp. 601-637
    • Krieger, M.1    Herz, J.2
  • 13
    • 0028917252 scopus 로고
    • Lipoprotein and receptor interactions in vivo
    • Herz, J., and T. E. Willnow. 1995. Lipoprotein and receptor interactions in vivo. Curr. Opin. Lipidol. 6: 97-103.
    • (1995) Curr. Opin. Lipidol. , vol.6 , pp. 97-103
    • Herz, J.1    Willnow, T.E.2
  • 14
    • 0030783740 scopus 로고    scopus 로고
    • Novel members of the low density lipoprotein receptor superfamily and their potential roles in lipid metabolism
    • Schneider, W. J., J. Nimpf, and H. Bujo. 1997. Novel members of the low density lipoprotein receptor superfamily and their potential roles in lipid metabolism. Curr. Opin. Lipidol. 8: 315-319.
    • (1997) Curr. Opin. Lipidol. , vol.8 , pp. 315-319
    • Schneider, W.J.1    Nimpf, J.2    Bujo, H.3
  • 15
    • 0025847767 scopus 로고
    • The human asialoglycoprotein receptor is a possible binding site for low-density lipoproteins and chylomicron remnants
    • Windler, E., J. Greeve, B. Levkau, V. Kolb-Bachofen, W. Daerr, and H. Greten. 1991. The human asialoglycoprotein receptor is a possible binding site for low-density lipoproteins and chylomicron remnants. Biochem. J. 276: 79-87.
    • (1991) Biochem. J. , vol.276 , pp. 79-87
    • Windler, E.1    Greeve, J.2    Levkau, B.3    Kolb-Bachofen, V.4    Daerr, W.5    Greten, H.6
  • 16
    • 0026751532 scopus 로고
    • Free fatty acids activate a high-affinity saturable pathway for degradation of low-density lipoproteins in fibroblasts from a subject homozygous for familial hypercholesterolemia
    • Bihain, B. E., and F. T. Yen. 1992. Free fatty acids activate a high-affinity saturable pathway for degradation of low-density lipoproteins in fibroblasts from a subject homozygous for familial hypercholesterolemia. Biochemistry. 31: 4628-4636.
    • (1992) Biochemistry , vol.31 , pp. 4628-4636
    • Bihain, B.E.1    Yen, F.T.2
  • 18
    • 0029088393 scopus 로고
    • Mechanism of activation and functional significance of the lipolysis-stimulated receptor. Evidence for a role as chylomicron remnant receptor
    • Mann, C. J., J. Khallou, O. Chevreuil, A. A. Troussard, L. M. Guermani, K. Launay, B. Delplanque, F. T. Yen, and B. E. Bihain. 1995. Mechanism of activation and functional significance of the lipolysis-stimulated receptor. Evidence for a role as chylomicron remnant receptor. Biochemistry. 34: 10421-10431.
    • (1995) Biochemistry , vol.34 , pp. 10421-10431
    • Mann, C.J.1    Khallou, J.2    Chevreuil, O.3    Troussard, A.A.4    Guermani, L.M.5    Launay, K.6    Delplanque, B.7    Yen, F.T.8    Bihain, B.E.9
  • 19
  • 21
    • 0030044270 scopus 로고    scopus 로고
    • Recognition of lactoferrin and aminopeptidase M-modified lactoferrin by the liver: Involvement of proteoglycans and the remnant receptor
    • Ziere, G. J., J. K. Kruijt, M. K. Bijsterbosch, and T. J. C. van Berkel. 1996. Recognition of lactoferrin and aminopeptidase M-modified lactoferrin by the liver: involvement of proteoglycans and the remnant receptor. Biochem. J. 313: 289-295.
    • (1996) Biochem. J. , vol.313 , pp. 289-295
    • Ziere, G.J.1    Kruijt, J.K.2    Bijsterbosch, M.K.3    Van Berkel, T.J.C.4
  • 22
    • 0027989299 scopus 로고
    • Cellular binding site and membrane binding proteins for triglyceride-rich lipoproteins in human monocyte-macrophages and THP-1 monocytic cells
    • Gianturco, S. H., M. P. Ramprasad, A. H-Y. Lin, R. Song, and W. A. Bradley. 1994. Cellular binding site and membrane binding proteins for triglyceride-rich lipoproteins in human monocyte-macrophages and THP-1 monocytic cells. J. Lipid Res. 35: 1674-1687.
    • (1994) J. Lipid Res. , vol.35 , pp. 1674-1687
    • Gianturco, S.H.1    Ramprasad, M.P.2    Lin, A.H.-Y.3    Song, R.4    Bradley, W.A.5
  • 23
    • 0029089094 scopus 로고
    • Human THP-1 monocyte-macrophage membrane binding proteins: Distinct receptor(s) for triglyceride-rich lipoproteins
    • Ramprasad, M. P., R. Li, W. A. Bradley, and S. H. Gianturco. 1995. Human THP-1 monocyte-macrophage membrane binding proteins: distinct receptor(s) for triglyceride-rich lipoproteins. Biochemistry. 34: 9126-9135.
    • (1995) Biochemistry , vol.34 , pp. 9126-9135
    • Ramprasad, M.P.1    Li, R.2    Bradley, W.A.3    Gianturco, S.H.4
  • 24
    • 0001575895 scopus 로고
    • Type III hyperlipoproteinemia (dysbetalipoproteinemia): The role of apolipoprotein E in normal and abnormal lipoprotein metabolism
    • C. R. Scriver, A. L. Beaudet, W. S. Sly, and D. Valle, editors. McGraw-Hill, New York
    • Mahley, R. W., and S. C. Rall, Jr. 1995. Type III hyperlipoproteinemia (dysbetalipoproteinemia): the role of apolipoprotein E in normal and abnormal lipoprotein metabolism. In The Metabolic and Molecular Bases of Inherited Disease. 7th edition. C. R. Scriver, A. L. Beaudet, W. S. Sly, and D. Valle, editors. McGraw-Hill, New York. 1953-1980.
    • (1995) The Metabolic and Molecular Bases of Inherited Disease. 7th Edition , pp. 1953-1980
    • Mahley, R.W.1    Rall S.C., Jr.2
  • 25
    • 0030175843 scopus 로고    scopus 로고
    • Heparan sulfate proteoglycan/low density lipoprotein receptor-related protein pathway involved in type III hyperlipoproteinemia and Alzheimer's disease
    • Mahley, R. W. 1996. Heparan sulfate proteoglycan/low density lipoprotein receptor-related protein pathway involved in type III hyperlipoproteinemia and Alzheimer's disease. Isr. J. Med. Sci. 32: 414-429.
    • (1996) Isr. J. Med. Sci. , vol.32 , pp. 414-429
    • Mahley, R.W.1
  • 26
    • 0026725757 scopus 로고
    • Severe hypercholesterolemia and atherosclerosis in apolipoprotein E-deficient mice created by homologous recombination in ES cells
    • Plump, A. S., J. D. Smith, T. Hayek, K. Aalto-Setälä, A. Walsh, J. G. Verstuyft, E. M. Rubin, and J. L. Breslow. 1992. Severe hypercholesterolemia and atherosclerosis in apolipoprotein E-deficient mice created by homologous recombination in ES cells. Cell. 71: 343-353.
    • (1992) Cell , vol.71 , pp. 343-353
    • Plump, A.S.1    Smith, J.D.2    Hayek, T.3    Aalto-Setälä, K.4    Walsh, A.5    Verstuyft, J.G.6    Rubin, E.M.7    Breslow, J.L.8
  • 27
    • 0026592806 scopus 로고
    • Spontaneous hypercholesterolemia and arterial lesions in mice lacking apolipoprotein E
    • Zhang, S. H., R. L. Reddick, J. A. Piedrahita, and N. Maeda. 1992. Spontaneous hypercholesterolemia and arterial lesions in mice lacking apolipoprotein E. Science. 258: 468-471.
    • (1992) Science , vol.258 , pp. 468-471
    • Zhang, S.H.1    Reddick, R.L.2    Piedrahita, J.A.3    Maeda, N.4
  • 28
    • 0028149980 scopus 로고
    • Role of heparan sulfate proteoglycans and the LDL receptor-related protein in remnant lipoprotein metabolism
    • Mahley, R. W., Z-S. Ji, W. J. Brecht, R. D. Miranda, and D. He. 1994. Role of heparan sulfate proteoglycans and the LDL receptor-related protein in remnant lipoprotein metabolism. Ann. NY Acad. Sci. 737: 39-52.
    • (1994) Ann. NY Acad. Sci. , vol.737 , pp. 39-52
    • Mahley, R.W.1    Ji, Z.-S.2    Brecht, W.J.3    Miranda, R.D.4    He, D.5
  • 29
    • 0028263619 scopus 로고
    • Enhanced binding and uptake of remnant lipoproteins by hepatic lipase-secreting hepatoma cells in culture
    • Ji, Z-S., S. J. Lauer, S. Fazio, A. Bensadoun, J. M. Taylor, and R. W. Mahley. 1994. Enhanced binding and uptake of remnant lipoproteins by hepatic lipase-secreting hepatoma cells in culture. J. Biol. Chem. 269: 13429-13436.
    • (1994) J. Biol. Chem. , vol.269 , pp. 13429-13436
    • Ji, Z.-S.1    Lauer, S.J.2    Fazio, S.3    Bensadoun, A.4    Taylor, J.M.5    Mahley, R.W.6
  • 30
    • 0028273560 scopus 로고
    • Role of hepatic lipase in the uptake and processing of chylomicron remnants in rat liver
    • Shafi, S., S. E. Brady, A. Bensadoun, and R. J. Havel. 1994. Role of hepatic lipase in the uptake and processing of chylomicron remnants in rat liver. J. Lipid Res. 35: 709-720.
    • (1994) J. Lipid Res. , vol.35 , pp. 709-720
    • Shafi, S.1    Brady, S.E.2    Bensadoun, A.3    Havel, R.J.4
  • 31
    • 0025940314 scopus 로고
    • Lipoprotein lipase enhances the binding of chylomicrons to low density lipoprotein receptor-related protein
    • Beisiegel, U., W. Weber, and G. Bengtsson-Olivecrona. 1991. Lipoprotein lipase enhances the binding of chylomicrons to low density lipoprotein receptor-related protein. Proc. Natl. Acad. Sci. USA. 88: 8342-8346.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 8342-8346
    • Beisiegel, U.1    Weber, W.2    Bengtsson-Olivecrona, G.3
  • 32
    • 0027251885 scopus 로고
    • Low density lipoprotein receptor internalizes low density and very low density lipoproteins that are bound to heparan sulfate proteoglycans via lipoprotein lipase
    • Mulder, M., P. Lombardi, H. Jansen, T. J. C. van Berkel, R. R. Frants, and L. M. Havekes. 1993. Low density lipoprotein receptor internalizes low density and very low density lipoproteins that are bound to heparan sulfate proteoglycans via lipoprotein lipase. J. Biol. Chem. 268: 9369-9375.
    • (1993) J. Biol. Chem. , vol.268 , pp. 9369-9375
    • Mulder, M.1    Lombardi, P.2    Jansen, H.3    Van Berkel, T.J.C.4    Frants, R.R.5    Havekes, L.M.6
  • 33
    • 0030661590 scopus 로고    scopus 로고
    • Hepatic uptake of chylomicron remnants
    • Cooper, A. D. 1997. Hepatic uptake of chylomicron remnants. J. Lipid Res. 38: 2173-2192.
    • (1997) J. Lipid Res. , vol.38 , pp. 2173-2192
    • Cooper, A.D.1
  • 34
    • 0030785846 scopus 로고    scopus 로고
    • Mechanisms of hepatic chylomicron remnant clearance
    • Willnow, T. E. 1997. Mechanisms of hepatic chylomicron remnant clearance. Diabet. Med. 14 (Suppl. 3): S75-S80.
    • (1997) Diabet. Med. , vol.14 , Issue.3 SUPPL.
    • Willnow, T.E.1
  • 35
    • 0027990682 scopus 로고
    • Secretion-capture role for apolipoprotein E in remnant lipoprotein metabolism involving cell surface heparan sulfate proteoglycans
    • Ji, Z-S., S. Fazio, Y-L. Lee, and R. W. Mahley. 1994. Secretion-capture role for apolipoprotein E in remnant lipoprotein metabolism involving cell surface heparan sulfate proteoglycans. J. Biol. Chem. 269: 2764-2772.
    • (1994) J. Biol. Chem. , vol.269 , pp. 2764-2772
    • Ji, Z.-S.1    Fazio, S.2    Lee, Y.-L.3    Mahley, R.W.4
  • 36
    • 0027246180 scopus 로고
    • Role of heparan sulfate proteoglycans in the binding and uptake of apolipoprotein E-enriched remnant lipoproteins by cultured cells
    • Ji, Z-S., W. J. Brecht, R. D. Miranda, M. M. Hussain, T. L. Innerarity, and R. W. Mahley. 1993. Role of heparan sulfate proteoglycans in the binding and uptake of apolipoprotein E-enriched remnant lipoproteins by cultured cells. J. Biol. Chem. 268: 10160-10167.
    • (1993) J. Biol. Chem. , vol.268 , pp. 10160-10167
    • Ji, Z.-S.1    Brecht, W.J.2    Miranda, R.D.3    Hussain, M.M.4    Innerarity, T.L.5    Mahley, R.W.6
  • 37
    • 0028913217 scopus 로고
    • Intravenous heparinase inhibits remnant lipoprotein clearance from the plasma and uptake by the liver: In vivo role of heparan sulfate proteoglycans
    • Ji, Z-S., D. A. Sanan, and R. W. Mahley. 1995. Intravenous heparinase inhibits remnant lipoprotein clearance from the plasma and uptake by the liver: in vivo role of heparan sulfate proteoglycans. J. Lipid Res. 36: 583-592.
    • (1995) J. Lipid Res. , vol.36 , pp. 583-592
    • Ji, Z.-S.1    Sanan, D.A.2    Mahley, R.W.3
  • 39
    • 0028936263 scopus 로고
    • Lipoproteins and the liver sieve: The role of the fenestrated sinusoidal endothelium in lipoprotein metabolism, atherosclerosis, and cirrhosis
    • Fraser, R., B. R. Dobbs, and G. W. T. Rogers. 1995. Lipoproteins and the liver sieve: the role of the fenestrated sinusoidal endothelium in lipoprotein metabolism, atherosclerosis, and cirrhosis. Hepatology. 21: 863-874.
    • (1995) Hepatology , vol.21 , pp. 863-874
    • Fraser, R.1    Dobbs, B.R.2    Rogers, G.W.T.3
  • 40
    • 0024989691 scopus 로고
    • Apolipoprotein E localization in rat hepatocytes by immunogold labeling of cryothin sections
    • Hamilton, R. L., J. S. Wong, L. S. S. Guo, S. Krisans, and R. J. Havel. 1990. Apolipoprotein E localization in rat hepatocytes by immunogold labeling of cryothin sections. J. Lipid Res. 31: 1589-1603.
    • (1990) J. Lipid Res. , vol.31 , pp. 1589-1603
    • Hamilton, R.L.1    Wong, J.S.2    Guo, L.S.S.3    Krisans, S.4    Havel, R.J.5
  • 41
    • 0021956622 scopus 로고
    • Heparan sulfate proteoglycans are concentrated on the sinusoidal plasmalemmal domain and in intracellular organelles of hepatocytes
    • Stow, J. L., L. Kjéllen, E. Unger, M. Höök, and M. G. Farquhar. 1985. Heparan sulfate proteoglycans are concentrated on the sinusoidal plasmalemmal domain and in intracellular organelles of hepatocytes. J. Cell Biol. 100: 975-980.
    • (1985) J. Cell Biol. , vol.100 , pp. 975-980
    • Stow, J.L.1    Kjéllen, L.2    Unger, E.3    Höök, M.4    Farquhar, M.G.5
  • 42
    • 0030950597 scopus 로고    scopus 로고
    • Hepatic lipase is abundant on both hepatocyte and endothelial cell surfaces in the liver
    • Sanan, D. A., J. Fan, A. Bensadoun, and J. M. Taylor. 1997. Hepatic lipase is abundant on both hepatocyte and endothelial cell surfaces in the liver. J. Lipid Res. 38: 1002-1013.
    • (1997) J. Lipid Res. , vol.38 , pp. 1002-1013
    • Sanan, D.A.1    Fan, J.2    Bensadoun, A.3    Taylor, J.M.4
  • 44
    • 0025991653 scopus 로고
    • Use of an anti-low density lipoprotein receptor antibody to quantify the role of the LDL receptor in the removal of chylomicron remnants in the mouse in vivo
    • Choi, S. Y., L. G. Fong, M. J. Kirven, and A. D. Cooper. 1991. Use of an anti-low density lipoprotein receptor antibody to quantify the role of the LDL receptor in the removal of chylomicron remnants in the mouse in vivo. J. Clin. Invest. 88: 1173-1181.
    • (1991) J. Clin. Invest. , vol.88 , pp. 1173-1181
    • Choi, S.Y.1    Fong, L.G.2    Kirven, M.J.3    Cooper, A.D.4
  • 45
    • 0027306114 scopus 로고
    • 2-macroglobulin receptor in chylomicron remnant removal in the mouse in vivo
    • 2-macroglobulin receptor in chylomicron remnant removal in the mouse in vivo. J. Biol. Chem. 268: 15804-15811.
    • (1993) J. Biol. Chem. , vol.268 , pp. 15804-15811
    • Choi, S.Y.1    Cooper, A.D.2
  • 46
    • 0028268018 scopus 로고
    • The two-receptor model of lipoprotein clearance: Tests of the hypothesis in "knockout" mice lacking the low density lipoprotein receptor, apolipoprotein E, or both proteins
    • Ishibashi, S., J. Herz, N. Maeda, J. L. Goldstein, and M. S. Brown. 1994. The two-receptor model of lipoprotein clearance: tests of the hypothesis in "knockout" mice lacking the low density lipoprotein receptor, apolipoprotein E, or both proteins. Proc. Natl. Acad. Sci. USA. 91: 4431-4435.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 4431-4435
    • Ishibashi, S.1    Herz, J.2    Maeda, N.3    Goldstein, J.L.4    Brown, M.S.5
  • 47
    • 0029076825 scopus 로고
    • Initial hepatic removal of chylomicron remnants is unaffected but endocytosis is delayed in mice lacking the low density lipoprotein receptor
    • Herz, J., S-Q. Qiu, A. Oesterle, H. V. de Silva, S. Shafi, and R. J. Havel. 1995. Initial hepatic removal of chylomicron remnants is unaffected but endocytosis is delayed in mice lacking the low density lipoprotein receptor. Proc. Natl. Acad. Sci. USA. 92: 4611-4615.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 4611-4615
    • Herz, J.1    Qiu, S.-Q.2    Oesterle, A.3    De Silva, H.V.4    Shafi, S.5    Havel, R.J.6
  • 48
    • 0032004972 scopus 로고    scopus 로고
    • Inducible inactivation of hepatic LRP gene by Cre-mediated recombination confirms role of LRP in clearance of chylomicron remnants
    • Rohlmann, A., M. Gotthardt, R. E. Hammer, and J. Herz. 1998. Inducible inactivation of hepatic LRP gene by Cre-mediated recombination confirms role of LRP in clearance of chylomicron remnants. J. Clin. Invest. 101: 689-695.
    • (1998) J. Clin. Invest. , vol.101 , pp. 689-695
    • Rohlmann, A.1    Gotthardt, M.2    Hammer, R.E.3    Herz, J.4
  • 49
    • 0028827449 scopus 로고
    • Intracellular localization and metabolism of chylomicron remnants in the livers of low density lipoprotein receptor-deficient mice and apoE-deficient mice. Evidence for slow metabolism via an alternative apoE-dependent pathway
    • Mortimer, B-C., D. J. Beveridge, I. J. Martins, and T. C. Redgrave. 1995. Intracellular localization and metabolism of chylomicron remnants in the livers of low density lipoprotein receptor-deficient mice and apoE-deficient mice. Evidence for slow metabolism via an alternative apoE-dependent pathway. J. Biol. Chem. 270: 28767-28776.
    • (1995) J. Biol. Chem. , vol.270 , pp. 28767-28776
    • Mortimer, B.-C.1    Beveridge, D.J.2    Martins, I.J.3    Redgrave, T.C.4
  • 52
    • 0032523950 scopus 로고    scopus 로고
    • Increased expression of apolipoprotein E in transgenic rabbits results in reduced levels of very low density lipoproteins and an accumulation of low density lipoproteins in plasma
    • Fan, J., Z.-S. Ji, Y. Huang, H. de Silva, D. Sanan, R. W. Mahley, T. L. Innerarity, and J. M. Taylor. 1998. Increased expression of apolipoprotein E in transgenic rabbits results in reduced levels of very low density lipoproteins and an accumulation of low density lipoproteins in plasma. J. Clin. Invest. 101: 2151-2164.
    • (1998) J. Clin. Invest. , vol.101 , pp. 2151-2164
    • Fan, J.1    Ji, Z.-S.2    Huang, Y.3    De Silva, H.4    Sanan, D.5    Mahley, R.W.6    Innerarity, T.L.7    Taylor, J.M.8
  • 53
    • 0027216450 scopus 로고
    • Type III hyperlipoproteinemic phenotype in transgenic mice expressing dysfunctional apolipoprotein E
    • Fazio, S., Y-L. Lee, Z-S. Ji, and S. C. Rall, Jr. 1993. Type III hyperlipoproteinemic phenotype in transgenic mice expressing dysfunctional apolipoprotein E. J. Clin. Invest. 92: 1497-1503.
    • (1993) J. Clin. Invest. , vol.92 , pp. 1497-1503
    • Fazio, S.1    Lee, Y.-L.2    Ji, Z.-S.3    Rall S.C., Jr.4
  • 54
    • 0024559621 scopus 로고
    • Type III hyperlipoproteinemia associated with apolipoprotein E phenotype E3/3. Structure and genetics of an apolipoprotein E3 variant
    • Rall, S. C., Jr., Y. M. Newhouse, H. R. G. Clarke, K. H. Weisgraber, B. J. McCarthy, R. W. Mahley, and T. P. Bersot. 1989. Type III hyperlipoproteinemia associated with apolipoprotein E phenotype E3/3. Structure and genetics of an apolipoprotein E3 variant. J. Clin. Invest. 83: 1095-1101.
    • (1989) J. Clin. Invest. , vol.83 , pp. 1095-1101
    • Rall S.C., Jr.1    Newhouse, Y.M.2    Clarke, H.R.G.3    Weisgraber, K.H.4    McCarthy, B.J.5    Mahley, R.W.6    Bersot, T.P.7
  • 55
    • 0026584011 scopus 로고
    • The functional characteristics of a human apolipoprotein E variant (cysteine at residue 142) may explain its association with dominant expression of type III hyperlipoproteinemia
    • Horie, Y., S. Fazio, J. R. Westerlund, K. H. Weisgraber, and S. C. Rall, Jr. 1992. The functional characteristics of a human apolipoprotein E variant (cysteine at residue 142) may explain its association with dominant expression of type III hyperlipoproteinemia. J. Biol. Chem. 267: 1962-1968.
    • (1992) J. Biol. Chem. , vol.267 , pp. 1962-1968
    • Horie, Y.1    Fazio, S.2    Westerlund, J.R.3    Weisgraber, K.H.4    Rall S.C., Jr.5
  • 56
    • 0021034630 scopus 로고
    • Resistance of a very low density lipoprotein subpopulation from familial dysbetalipoproteinemia to in vitro lipolytic conversion to the low density lipoprotein density fraction
    • Chung, B. H., and J. P. Segrest. 1983. Resistance of a very low density lipoprotein subpopulation from familial dysbetalipoproteinemia to in vitro lipolytic conversion to the low density lipoprotein density fraction. J. Lipid Res. 24: 1148-1159.
    • (1983) J. Lipid Res. , vol.24 , pp. 1148-1159
    • Chung, B.H.1    Segrest, J.P.2
  • 57
    • 0010430712 scopus 로고
    • Role of apolipoprotein E in the lipolytic conversion of β-very low density lipoproteins to low density lipoproteins in type III hyperlipoproteinemia
    • Ehnholm, C., R. W. Mahley, D. A. Chappell, K. H. Weisgraber, E. Ludwig, and J. L. Witztum. 1984. Role of apolipoprotein E in the lipolytic conversion of β-very low density lipoproteins to low density lipoproteins in type III hyperlipoproteinemia. Proc. Natl. Acad. Sci. USA. 81: 5566-5570.
    • (1984) Proc. Natl. Acad. Sci. USA , vol.81 , pp. 5566-5570
    • Ehnholm, C.1    Mahley, R.W.2    Chappell, D.A.3    Weisgraber, K.H.4    Ludwig, E.5    Witztum, J.L.6
  • 58
    • 0027934205 scopus 로고
    • Triglyceride-rich lipoproteins of subjects heterozygous for apolipoprotein E2(Lys146→Gln) are inefficiently converted to cholesterol-rich lipoproteins
    • Mulder, M., H. van der Boom, P. de Knijff, C. Braam, A. van den Maagdenberg, J. A. Gevers Leuven, and L. M. Havekes. 1994. Triglyceride-rich lipoproteins of subjects heterozygous for apolipoprotein E2(Lys146→Gln) are inefficiently converted to cholesterol-rich lipoproteins. Atherosclerosis. 108: 183-192.
    • (1994) Atherosclerosis , vol.108 , pp. 183-192
    • Mulder, M.1    Van Der Boom, H.2    De Knijff, P.3    Braam, C.4    Van Den Maagdenberg, A.5    Gevers Leuven, J.A.6    Havekes, L.M.7
  • 59
    • 0031471229 scopus 로고    scopus 로고
    • Genetic factors precipitating type III hyperlipoproteinemia in hypolipidemic transgenic mice expressing human apolipoprotein E2
    • Huang, Y., S. C. Rall, Jr., and R. W. Mahley. 1997. Genetic factors precipitating type III hyperlipoproteinemia in hypolipidemic transgenic mice expressing human apolipoprotein E2. Arterioscler. Thromb. Vasc. Biol. 17: 2817-2824.
    • (1997) Arterioscler. Thromb. Vasc. Biol. , vol.17 , pp. 2817-2824
    • Huang, Y.1    Rall S.C., Jr.2    Mahley, R.W.3
  • 60
    • 0032504182 scopus 로고    scopus 로고
    • Apolipoprotein E2 reduces the low density lipoprotein level in transgenic mice by impairing lipoprotein lipase-mediated lipolysis of triglyceride-rich lipoproteins
    • Huang, Y., X. Q. Liu, S. C. Rall, Jr., and R. W. Mahley. 1998. Apolipoprotein E2 reduces the low density lipoprotein level in transgenic mice by impairing lipoprotein lipase-mediated lipolysis of triglyceride-rich lipoproteins. J. Biol. Chem. 273: 17483-17490.
    • (1998) J. Biol. Chem. , vol.273 , pp. 17483-17490
    • Huang, Y.1    Liu, X.Q.2    Rall S.C., Jr.3    Mahley, R.W.4
  • 61
    • 0018366114 scopus 로고
    • Localization of the heparin-releasable lipase in situ in the rat liver
    • Kuusi, T., E. A. Nikkilä, I. Virtanen, and P. K. J. Kinnunen. 1979. Localization of the heparin-releasable lipase in situ in the rat liver. Biochem. J. 181: 245-246.
    • (1979) Biochem. J. , vol.181 , pp. 245-246
    • Kuusi, T.1    Nikkilä, E.A.2    Virtanen, I.3    Kinnunen, P.K.J.4
  • 62
    • 0019124890 scopus 로고
    • Uptake and degradation of rat and human very low density (remnant) apolipoprotein by parenchymal and non-parenchymal rat liver cells
    • van Tol, A., and T. J. C. van Berkel. 1980. Uptake and degradation of rat and human very low density (remnant) apolipoprotein by parenchymal and non-parenchymal rat liver cells. Biochim. Biophys. Acta. 619: 156-166.
    • (1980) Biochim. Biophys. Acta. , vol.619 , pp. 156-166
    • Van Tol, A.1    Van Berkel, T.J.C.2
  • 63
    • 0026646737 scopus 로고
    • Triacylglycerol hydrolysis in isolated hepatic endosomes
    • Hornick, C. A., C. Thouron, J. G. DeLamatre, and J. Huang. 1992. Triacylglycerol hydrolysis in isolated hepatic endosomes. J. Biol. Chem. 267: 3396-3401.
    • (1992) J. Biol. Chem. , vol.267 , pp. 3396-3401
    • Hornick, C.A.1    Thouron, C.2    DeLamatre, J.G.3    Huang, J.4
  • 64
    • 0028966426 scopus 로고
    • The cellular internalization and degradation of hepatic lipase is mediated by low density lipoprotein receptor-related protein and requires cell surface proteoglycans
    • Kounnas, M. Z., D. A. Chappell, H. Wong, W. S. Argraves, and D. K. Strickland. 1995. The cellular internalization and degradation of hepatic lipase is mediated by low density lipoprotein receptor-related protein and requires cell surface proteoglycans. J. Biol. Chem. 270: 9307-9312.
    • (1995) J. Biol. Chem. , vol.270 , pp. 9307-9312
    • Kounnas, M.Z.1    Chappell, D.A.2    Wong, H.3    Argraves, W.S.4    Strickland, D.K.5
  • 65
    • 0028988781 scopus 로고
    • Lipases and lecithin:Cholesterol acyltransferase in the control of lipoprotein metabolism
    • Applebaum-Bowden, D. 1995. Lipases and lecithin:cholesterol acyltransferase in the control of lipoprotein metabolism. Curr. Opin. Lipidol. 6: 130-135.
    • (1995) Curr. Opin. Lipidol. , vol.6 , pp. 130-135
    • Applebaum-Bowden, D.1
  • 66
    • 0029973767 scopus 로고    scopus 로고
    • Hepatic lipase mediates the uptake of chylomicrons and β-VLDL into cells via the LDL receptor-related protein (LRP)
    • Krapp, A., S. Ahle, S. Kersting, Y. Hua, K. Kneser, M. Nielsen, J. Gliemann, and U. Beisiegel. 1996. Hepatic lipase mediates the uptake of chylomicrons and β-VLDL into cells via the LDL receptor-related protein (LRP). J. Lipid Res. 37: 926-936.
    • (1996) J. Lipid Res. , vol.37 , pp. 926-936
    • Krapp, A.1    Ahle, S.2    Kersting, S.3    Hua, Y.4    Kneser, K.5    Nielsen, M.6    Gliemann, J.7    Beisiegel, U.8
  • 67
    • 0029895866 scopus 로고    scopus 로고
    • Chinese hamster ovary cells expressing a cell surface-anchored form of hepatic lipase. Characterization of low density lipoprotein and chylomicron remnant uptake and selective uptake of high density lipoprotein-cholesteryl ester
    • Komaromy, M., S. Azhar, and A. D. Cooper. 1996. Chinese hamster ovary cells expressing a cell surface-anchored form of hepatic lipase. Characterization of low density lipoprotein and chylomicron remnant uptake and selective uptake of high density lipoprotein-cholesteryl ester. J. Biol. Chem. 271: 16906-16914.
    • (1996) J. Biol. Chem. , vol.271 , pp. 16906-16914
    • Komaromy, M.1    Azhar, S.2    Cooper, A.D.3
  • 68
    • 0030878936 scopus 로고    scopus 로고
    • Uptake of hypertriglyceridemic very low density lipoproteins and their remnants by HepG2 cells: The role of lipoprotein lipase, hepatic triglyceride lipase, and cell surface proteoglycans
    • Huff, M. W., D. B. Miller, B. M. Wolfe, P. W. Connelly, and C. G. Sawyez. 1997. Uptake of hypertriglyceridemic very low density lipoproteins and their remnants by HepG2 cells: the role of lipoprotein lipase, hepatic triglyceride lipase, and cell surface proteoglycans. J. Lipid Res. 38: 1318-1333.
    • (1997) J. Lipid Res. , vol.38 , pp. 1318-1333
    • Huff, M.W.1    Miller, D.B.2    Wolfe, B.M.3    Connelly, P.W.4    Sawyez, C.G.5
  • 69
    • 0027534554 scopus 로고
    • Hepatic lipase treatment of chylomicron remnants increases exposure of apolipoprotein E
    • Brasaemle, D. L., K. Cornely-Moss, and A. Bensadoun. 1993. Hepatic lipase treatment of chylomicron remnants increases exposure of apolipoprotein E. J. Lipid Res. 34: 455-465.
    • (1993) J. Lipid Res. , vol.34 , pp. 455-465
    • Brasaemle, D.L.1    Cornely-Moss, K.2    Bensadoun, A.3
  • 70
    • 0027235976 scopus 로고
    • Hepatic lipase function and the accumulation of β-very-low-density lipoproteins in the plasma of cholesterol-fed rabbits
    • Chang, S., and J. Borensztajn. 1993. Hepatic lipase function and the accumulation of β-very-low-density lipoproteins in the plasma of cholesterol-fed rabbits. Biochem. J. 293: 745-750.
    • (1993) Biochem. J. , vol.293 , pp. 745-750
    • Chang, S.1    Borensztajn, J.2
  • 71
    • 0022460247 scopus 로고
    • Enrichment of apolipoprotein B-48 in the LDL density class following in vivo inhibition of hepatic lipase
    • Daggy, B. P., and A. Bensadoun. 1986. Enrichment of apolipoprotein B-48 in the LDL density class following in vivo inhibition of hepatic lipase. Biochim. Biophys. Acta. 877: 252-261.
    • (1986) Biochim. Biophys. Acta. , vol.877 , pp. 252-261
    • Daggy, B.P.1    Bensadoun, A.2
  • 72
    • 0018289132 scopus 로고
    • Hepatic endothelial lipase antiserum influences rat plasma low and high density lipoproteins in vivo
    • Kuusi, T., P. K. J. Kinnunen, and E. A. Nikkilä. 1979. Hepatic endothelial lipase antiserum influences rat plasma low and high density lipoproteins in vivo. FEBS Lett. 104: 384-388.
    • (1979) FEBS Lett. , vol.104 , pp. 384-388
    • Kuusi, T.1    Kinnunen, P.K.J.2    Nikkilä, E.A.3
  • 73
    • 0030069736 scopus 로고    scopus 로고
    • Relative roles of the LDL receptor, the LDL receptor-like protein, and hepatic lipase in chylomicron remnant removal by the liver
    • de Faria, E., L. G. Fong, M. Komaromy, and A. D. Cooper. 1996. Relative roles of the LDL receptor, the LDL receptor-like protein, and hepatic lipase in chylomicron remnant removal by the liver. J. Lipid Res. 37: 197-209.
    • (1996) J. Lipid Res. , vol.37 , pp. 197-209
    • De Faria, E.1    Fong, L.G.2    Komaromy, M.3    Cooper, A.D.4
  • 74
    • 0028144804 scopus 로고
    • Overexpression of hepatic lipase in transgenic rabbits leads to a marked reduction of plasma high density lipoproteins and intermediate density lipoproteins
    • Fan, J., J. Wang, A. Bensadoun, S. J. Lauer, Q. Dang, R. W. Mahley, and J. M. Taylor. 1994. Overexpression of hepatic lipase in transgenic rabbits leads to a marked reduction of plasma high density lipoproteins and intermediate density lipoproteins. Proc. Natl. Acad. Sci. USA. 91: 8724-8728.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 8724-8728
    • Fan, J.1    Wang, J.2    Bensadoun, A.3    Lauer, S.J.4    Dang, Q.5    Mahley, R.W.6    Taylor, J.M.7
  • 75
    • 0016816559 scopus 로고
    • The mechanism of assimilation of constituents of chylomicrons, very low density lipoproteins and remnants - A new theory
    • Felts, J. M., H. Itakura, and R. T. Crane. 1975. The mechanism of assimilation of constituents of chylomicrons, very low density lipoproteins and remnants - a new theory. Biochem. Biophys. Res. Commun. 66: 1467-1475.
    • (1975) Biochem. Biophys. Res. Commun. , vol.66 , pp. 1467-1475
    • Felts, J.M.1    Itakura, H.2    Crane, R.T.3
  • 76
    • 0026442201 scopus 로고
    • Lipoprotein lipase enhances binding of lipoproteins to heparan sulfate on cell surfaces and extracellular matrix
    • Eisenberg, S., E. Sehayek, T. Olivecrona, and I. Vlodavsky. 1992. Lipoprotein lipase enhances binding of lipoproteins to heparan sulfate on cell surfaces and extracellular matrix. J. Clin. Invest. 90: 2013-2021.
    • (1992) J. Clin. Invest. , vol.90 , pp. 2013-2021
    • Eisenberg, S.1    Sehayek, E.2    Olivecrona, T.3    Vlodavsky, I.4
  • 77
    • 0026717599 scopus 로고
    • Mechanisms by which lipoprotein lipase alters cellular metabolism of lipoprotein[a], low density lipoprotein, and nascent lipoproteins. Roles for low density lipoprotein receptors and heparan sulfate proteoglycans
    • Williams, K. J., G. M. Fless, K. A. Petrie, M. L. Snyder, R. W. Brocia, and T. L. Swenson. 1992. Mechanisms by which lipoprotein lipase alters cellular metabolism of lipoprotein[a], low density lipoprotein, and nascent lipoproteins. Roles for low density lipoprotein receptors and heparan sulfate proteoglycans. J. Biol. Chem. 267: 13284-13292.
    • (1992) J. Biol. Chem. , vol.267 , pp. 13284-13292
    • Williams, K.J.1    Fless, G.M.2    Petrie, K.A.3    Snyder, M.L.4    Brocia, R.W.5    Swenson, T.L.6
  • 81
    • 0029920693 scopus 로고    scopus 로고
    • Lipoprotein lipase and lipolysis: Central roles in lipoprotein metabolism and atherogenesis
    • Goldberg, I. J. 1996. Lipoprotein lipase and lipolysis: central roles in lipoprotein metabolism and atherogenesis. J. Lipid Res. 37: 693-707.
    • (1996) J. Lipid Res. , vol.37 , pp. 693-707
    • Goldberg, I.J.1
  • 82
    • 0019820184 scopus 로고
    • Type III hyperlipoproteinemia associated with apolipoprotein E deficiency
    • Ghiselli, G., E. J. Schaefer, P. Gascon, and H. B. Brewer, Jr. 1981. Type III hyperlipoproteinemia associated with apolipoprotein E deficiency. Science. 214: 1239-1241.
    • (1981) Science , vol.214 , pp. 1239-1241
    • Ghiselli, G.1    Schaefer, E.J.2    Gascon, P.3    Brewer H.B., Jr.4
  • 83
    • 0026498155 scopus 로고
    • Familial apolipoprotein e deficiency and type III hyperlipoproteinemia due to a premature stop codon in the apolipoprotein E gene
    • Lohse, P., H. B. Brewer III, M. S. Meng, S. I. Skarlatos, J. C. LaRosa, and H. B. Brewer, Jr. 1992. Familial apolipoprotein E deficiency and type III hyperlipoproteinemia due to a premature stop codon in the apolipoprotein E gene. J. Lipid Res. 33: 1583-1590.
    • (1992) J. Lipid Res. , vol.33 , pp. 1583-1590
    • Lohse, P.1    Brewer H.B. III2    Meng, M.S.3    Skarlatos, S.I.4    Larosa, J.C.5    Brewer H.B., Jr.6
  • 84
    • 0028225873 scopus 로고
    • Transgenic mice expressing human lipoprotein lipase driven by the mouse metallothionein promoter. A phenotype associated with increased perinatal mortality and reduced plasma very low density lipoprotein of normal size
    • Zsigmond, E., E. Scheffler, T. M. Forte, R. Potenz, W. Wu, and L. Chan. 1994. Transgenic mice expressing human lipoprotein lipase driven by the mouse metallothionein promoter. A phenotype associated with increased perinatal mortality and reduced plasma very low density lipoprotein of normal size. J. Biol. Chem. 269: 18757-18766.
    • (1994) J. Biol. Chem. , vol.269 , pp. 18757-18766
    • Zsigmond, E.1    Scheffler, E.2    Forte, T.M.3    Potenz, R.4    Wu, W.5    Chan, L.6
  • 85
    • 0030666462 scopus 로고    scopus 로고
    • Adenovirus-mediated gene transfer of human lipoprotein lipase ameliorates the hyperlipidemias associated with apolipoprotein E and LDL receptor deficiencies in mice
    • Zsigmond, E., K. Kobayashi, K-W. Tzung, L. Li, Y. Fuke, and L. Chan. 1997. Adenovirus-mediated gene transfer of human lipoprotein lipase ameliorates the hyperlipidemias associated with apolipoprotein E and LDL receptor deficiencies in mice. Hum. Gene Ther. 8: 1921-1933.
    • (1997) Hum. Gene Ther. , vol.8 , pp. 1921-1933
    • Zsigmond, E.1    Kobayashi, K.2    Tzung, K.-W.3    Li, L.4    Fuke, Y.5    Chan, L.6
  • 86
    • 0029075830 scopus 로고
    • Triglyceride lipases and atherosclerosis
    • Olivecrona, G., and T. Olivecrona. 1995. Triglyceride lipases and atherosclerosis. Curr. Opin. Lipidol. 6: 291-305.
    • (1995) Curr. Opin. Lipidol. , vol.6 , pp. 291-305
    • Olivecrona, G.1    Olivecrona, T.2
  • 87
    • 0030775796 scopus 로고    scopus 로고
    • Cell-surface heparan sulfate proteoglycans: Dynamic molecules mediating ligand catabolism
    • Williams, K. J., and I. V. Fuki. 1997. Cell-surface heparan sulfate proteoglycans: dynamic molecules mediating ligand catabolism. Curr. Opin. Lipidol. 8: 253-262.
    • (1997) Curr. Opin. Lipidol. , vol.8 , pp. 253-262
    • Williams, K.J.1    Fuki, I.V.2
  • 89
    • 0029961653 scopus 로고    scopus 로고
    • Lipoprotein lipase-mediated uptake of lipoprotein in human fibroblasts: Evidence for an LDL receptor-independent internalization pathway
    • Fernández-Borja, M., D. Bellido, E. Vilella, G. Olivecrona, and S. Vilaró. 1996. Lipoprotein lipase-mediated uptake of lipoprotein in human fibroblasts: evidence for an LDL receptor-independent internalization pathway. J. Lipid Res. 37: 464-481.
    • (1996) J. Lipid Res. , vol.37 , pp. 464-481
    • Fernández-Borja, M.1    Bellido, D.2    Vilella, E.3    Olivecrona, G.4    Vilaró, S.5
  • 90
    • 0029767012 scopus 로고    scopus 로고
    • Differences in the mechanisms of uptake and endocytosis of small and large chylomicron remnants by rat liver
    • Windler, E., J. Greeve, H. Robenek, F. Rinninger, H. Greten, and S. Jäckle. 1996. Differences in the mechanisms of uptake and endocytosis of small and large chylomicron remnants by rat liver. Hepatology. 24: 344-351.
    • (1996) Hepatology , vol.24 , pp. 344-351
    • Windler, E.1    Greeve, J.2    Robenek, H.3    Rinninger, F.4    Greten, H.5    Jäckle, S.6
  • 91
    • 0028988551 scopus 로고
    • 39 kDa receptor-associated protein is an ER resident protein and molecular chaperone for LDL receptor-related protein
    • Bu, G., H. J. Geuze, G. J. Strous, and A. L. Schwartz. 1995. 39 kDa receptor-associated protein is an ER resident protein and molecular chaperone for LDL receptor-related protein. EMBO J. 14: 2269-2280.
    • (1995) EMBO J. , vol.14 , pp. 2269-2280
    • Bu, G.1    Geuze, H.J.2    Strous, G.J.3    Schwartz, A.L.4
  • 92
    • 0029079403 scopus 로고
    • Functional expression of low density lipoprotein receptor-related protein is controlled by receptor-associated protein in vivo
    • Willnow, T. E., S. A. Armstrong, R. E. Hammer, and J. Herz. 1995. Functional expression of low density lipoprotein receptor-related protein is controlled by receptor-associated protein in vivo. Proc. Natl. Acad. Sci. USA. 92: 4537-4541.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 4537-4541
    • Willnow, T.E.1    Armstrong, S.A.2    Hammer, R.E.3    Herz, J.4
  • 93
    • 0029887302 scopus 로고    scopus 로고
    • RAP, a specialized chaperone, prevents ligand-induceri ER retention and degradation of LDL receptor-related endocytic receptors
    • Willnow, T. E., A. Rohlmann, J. Horton, H. Otani, J. R. Braun, R. E. Hammer, and J. Herz. 1996. RAP, a specialized chaperone, prevents ligand-induceri ER retention and degradation of LDL receptor-related endocytic receptors. EMBO J. 15: 2632-2639.
    • (1996) EMBO J. , vol.15 , pp. 2632-2639
    • Willnow, T.E.1    Rohlmann, A.2    Horton, J.3    Otani, H.4    Braun, J.R.5    Hammer, R.E.6    Herz, J.7
  • 95
    • 0027985101 scopus 로고
    • Lactoferrin binding to heparan sulfate proteoglycans and the LDL receptor-related protein. Further evidence supporting the importance of direct binding of remnant lipoproteins to HSPG
    • Ji, Z-S., and R. W. Mahley. 1994. Lactoferrin binding to heparan sulfate proteoglycans and the LDL receptor-related protein. Further evidence supporting the importance of direct binding of remnant lipoproteins to HSPG. Arterioscler. Thromb. 14: 2025-2032.
    • (1994) Arterioscler. Thromb. , vol.14 , pp. 2025-2032
    • Ji, Z.-S.1    Mahley, R.W.2
  • 96
    • 0028243645 scopus 로고
    • Exogenous receptor-associated protein binds to two distinct sites on human fibroblasts but does not bind to the glycosaminoglycan residues of heparan sulfate proteoglycans
    • Vassiliou, G., and K. K. Stanley. 1994. Exogenous receptor-associated protein binds to two distinct sites on human fibroblasts but does not bind to the glycosaminoglycan residues of heparan sulfate proteoglycans. J. Biol. Chem. 269: 15172-15178.
    • (1994) J. Biol. Chem. , vol.269 , pp. 15172-15178
    • Vassiliou, G.1    Stanley, K.K.2
  • 98
    • 0025875756 scopus 로고
    • Proteoglycans: Structures and interactions
    • Kjellén, L., and U. Lindahl. 1991. Proteoglycans: structures and interactions. Annu. Rev. Biochem. 60: 443-475.
    • (1991) Annu. Rev. Biochem. , vol.60 , pp. 443-475
    • Kjellén, L.1    Lindahl, U.2
  • 101
    • 0029851509 scopus 로고    scopus 로고
    • In the absence of the low density lipoprotein receptor, human apolipoprotein CI overexpression in transgenic mice inhibits the hepatic uptake of very low density lipoproteins via a receptor-associated protein-sensitive pathway
    • Jong, M. C., V. E. H. Dahlmans, P. J. J. van Gorp, K. W. van Dijk, M. L. Breuer, and M. H. Hofker. 1996. In the absence of the low density lipoprotein receptor, human apolipoprotein CI overexpression in transgenic mice inhibits the hepatic uptake of very low density lipoproteins via a receptor-associated protein-sensitive pathway. J. Clin. Invest. 98: 2259-2267.
    • (1996) J. Clin. Invest. , vol.98 , pp. 2259-2267
    • Jong, M.C.1    Dahlmans, V.E.H.2    Van Gorp, P.J.J.3    Van Dijk, K.W.4    Breuer, M.L.5    Hofker, M.H.6
  • 102
    • 0028284556 scopus 로고
    • Inhibition of hepatic chylomicron remnant uptake by gene transfer of a receptor antagonist
    • Willnow, T. E., Z. Sheng, S. Ishibashi, and J. Herz. 1994. Inhibition of hepatic chylomicron remnant uptake by gene transfer of a receptor antagonist. Science. 264: 1471-1474.
    • (1994) Science , vol.264 , pp. 1471-1474
    • Willnow, T.E.1    Sheng, Z.2    Ishibashi, S.3    Herz, J.4
  • 103
    • 0032523099 scopus 로고    scopus 로고
    • Hepatic apoE, expression is required for remnant lipoprotein clearance in the absence of the low density lipoprotein receptor
    • Linton, M. F., A. H. Hasty, V. R. Babaev, and S. Fazio. 1998. Hepatic apoE, expression is required for remnant lipoprotein clearance in the absence of the low density lipoprotein receptor. J. Clin. Invest. 101: 1726-1736.
    • (1998) J. Clin. Invest. , vol.101 , pp. 1726-1736
    • Linton, M.F.1    Hasty, A.H.2    Babaev, V.R.3    Fazio, S.4
  • 104
    • 0031967097 scopus 로고    scopus 로고
    • Chylomicron remnant uptake is regulated by the expression and function of heparan sulfate proteoglycan in hepatocytes
    • Zeng, B-J., B-C. Mortimer, I. J. Martins, U. Seydel, and T. G. Redgrave. 1998. Chylomicron remnant uptake is regulated by the expression and function of heparan sulfate proteoglycan in hepatocytes. J. Lipid Res. 39: 845-860.
    • (1998) J. Lipid Res. , vol.39 , pp. 845-860
    • Zeng, B.-J.1    Mortimer, B.-C.2    Martins, I.J.3    Seydel, U.4    Redgrave, T.G.5
  • 105
    • 0026439778 scopus 로고
    • LDL receptor-related protein internalizes and degrades uPA-PAI-1 complexes and is essential for embryo implantation
    • Herz, J., D. E. Clouthier, and R. E. Hammer. 1992. LDL receptor-related protein internalizes and degrades uPA-PAI-1 complexes and is essential for embryo implantation. Cell. 71: 411-421.
    • (1992) Cell , vol.71 , pp. 411-421
    • Herz, J.1    Clouthier, D.E.2    Hammer, R.E.3
  • 106
    • 0032520147 scopus 로고    scopus 로고
    • Increased sphingomyelin content of plasma lipoproteins in apolipoprotein E knockout mice reflects combined production and catabolic defects and enhances reactivity with mammalian sphingomyelinase
    • Jeong, T-S., S. L. Schissel, I. Tabas, H. J. Pownall, A. R. Tall, and X-C. Jiang. 1998. Increased sphingomyelin content of plasma lipoproteins in apolipoprotein E knockout mice reflects combined production and catabolic defects and enhances reactivity with mammalian sphingomyelinase. J. Clin. Invest. 101: 905-912.
    • (1998) J. Clin. Invest. , vol.101 , pp. 905-912
    • Jeong, T.-S.1    Schissel, S.L.2    Tabas, I.3    Pownall, H.J.4    Tall, A.R.5    Jiang, X.-C.6
  • 108
    • 0031452443 scopus 로고    scopus 로고
    • Heparan sulfate proteoglycans participate in hepatic lipase- And apolipoprotein E-mediated binding and uptake of plasma lipoproteins, including high density lipoproteins
    • Ji, Z-S., H. L. Dichek, R. D. Miranda, and R. W. Mahley. 1997. Heparan sulfate proteoglycans participate in hepatic lipase- and apolipoprotein E-mediated binding and uptake of plasma lipoproteins, including high density lipoproteins. J. Biol. Chem. 272: 31285-31292.
    • (1997) J. Biol. Chem. , vol.272 , pp. 31285-31292
    • Ji, Z.-S.1    Dichek, H.L.2    Miranda, R.D.3    Mahley, R.W.4
  • 109
    • 0025835670 scopus 로고
    • Requirement of heparan sulfate for bFGF-mediated fibroblast growth and myoblast differentiation
    • Rapraeger, A. C., A. Krufka, and B. B. Olwin. 1991. Requirement of heparan sulfate for bFGF-mediated fibroblast growth and myoblast differentiation. Science, 252: 1705-1708.
    • (1991) Science , vol.252 , pp. 1705-1708
    • Rapraeger, A.C.1    Krufka, A.2    Olwin, B.B.3
  • 110
    • 0028579734 scopus 로고
    • Perlecan, basal lamina proteoglycan, promotes basic fibroblast growth factor-receptor binding, mitogenesis, and angiogenesis
    • Aviezer, D., D. Hecht, M. Safran, M. Eisinger, G. David, and A. Yayon. 1994. Perlecan, basal lamina proteoglycan, promotes basic fibroblast growth factor-receptor binding, mitogenesis, and angiogenesis. Cell. 79: 1005-1013.
    • (1994) Cell , vol.79 , pp. 1005-1013
    • Aviezer, D.1    Hecht, D.2    Safran, M.3    Eisinger, M.4    David, G.5    Yayon, A.6
  • 111
    • 0025950158 scopus 로고
    • A dual receptor system is required for basic fibroblast growth factor activity
    • Klagsbrun, M., and A. Baird. 1991. A dual receptor system is required for basic fibroblast growth factor activity. Cell. 67: 229-231.
    • (1991) Cell , vol.67 , pp. 229-231
    • Klagsbrun, M.1    Baird, A.2
  • 112
    • 0027323554 scopus 로고
    • Heparan sulfate proteoglycan and FGF receptor target basic FGF to different intracellular destinations
    • Reiland, J., and A. C. Rapraeger. 1993. Heparan sulfate proteoglycan and FGF receptor target basic FGF to different intracellular destinations. J. Cell Sci. 105: 1085-1093.
    • (1993) J. Cell Sci. , vol.105 , pp. 1085-1093
    • Reiland, J.1    Rapraeger, A.C.2
  • 113
    • 0028859082 scopus 로고
    • Basic fibroblast growth factor (FGF-2) internalization through the heparan sulfate proteoglycans-mediated pathway: An ultrastructural approach
    • Gleizes, P-E., J. Noaillac-Depeyre, F. Amalric, and N. Gas. 1995. Basic fibroblast growth factor (FGF-2) internalization through the heparan sulfate proteoglycans-mediated pathway: an ultrastructural approach. Eur. J. Cell Biol. 66: 47-59.
    • (1995) Eur. J. Cell Biol. , vol.66 , pp. 47-59
    • Gleizes, P.-E.1    Noaillac-Depeyre, J.2    Amalric, F.3    Gas, N.4
  • 114
    • 0028339789 scopus 로고
    • Variable heparan sulfate proteoglycan binding of apolipoprotein E variants may modulate the expression of type IIII hyperlipoproteinemia
    • Ji, Z-S., S. Fazio, and R. W. Mahley. 1994. Variable heparan sulfate proteoglycan binding of apolipoprotein E variants may modulate the expression of type IIII hyperlipoproteinemia. J. Biol. Chem. 269: 13421-13428.
    • (1994) J. Biol. Chem. , vol.269 , pp. 13421-13428
    • Ji, Z.-S.1    Fazio, S.2    Mahley, R.W.3
  • 115
    • 0029844205 scopus 로고    scopus 로고
    • Human apolipoprotein E: The Alzheimer's disease connection
    • Weisgraber, K. H., and R. W. Mahley. 1996. Human apolipoprotein E: the Alzheimer's disease connection. FASEB J. 10: 1485-1494.
    • (1996) FASEB J. , vol.10 , pp. 1485-1494
    • Weisgraber, K.H.1    Mahley, R.W.2
  • 116
    • 0002311452 scopus 로고    scopus 로고
    • Apolipoprotein E: Structure and function in lipid metabolism and neurobiology
    • R. N. Rosenberg, S. B. Prusiner, S. DiMauro, and R. L. Barchi, editors. Butterworth-Heinemann, Boston
    • Mahley, R. W. 1997. Apolipoprotein E: structure and function in lipid metabolism and neurobiology. In The Molecular and Genetic Basis of Neurological Disease. 2nd edition. R. N. Rosenberg, S. B. Prusiner, S. DiMauro, and R. L. Barchi, editors. Butterworth-Heinemann, Boston, 1037-1049.
    • (1997) The Molecular and Genetic Basis of Neurological Disease. 2nd Edition , pp. 1037-1049
    • Mahley, R.W.1
  • 119
  • 120
    • 0028850374 scopus 로고
    • Stable expression and secretion of apolipoproteins E3 and E4 in mouse neuroblastoma cells produces differential effects on neurite outgrowth
    • Bellosta, S., B. P. Nathan, M. Orth, L-M. Dong, R. W. Mahley, and R. E. Pitas. 1995. Stable expression and secretion of apolipoproteins E3 and E4 in mouse neuroblastoma cells produces differential effects on neurite outgrowth. J. Biol. Chem. 270: 27063-27071.
    • (1995) J. Biol. Chem. , vol.270 , pp. 27063-27071
    • Bellosta, S.1    Nathan, B.P.2    Orth, M.3    Dong, L.-M.4    Mahley, R.W.5    Pitas, R.E.6
  • 121
    • 0028822219 scopus 로고
    • Low density lipoprotein receptor-related protein mediates apolipoprotein E-dependent neurite outgrowth in a central nervous system-derived neuronal cell line
    • Holtzman, D. M., R. E. Pitas, J. Kilbridge, B. Nathan, R. W. Mahley, G. Bu, and A. L. Schwartz. 1995. Low density lipoprotein receptor-related protein mediates apolipoprotein E-dependent neurite outgrowth in a central nervous system-derived neuronal cell line. Proc. Natl. Acad. Sci. USA. 92: 9480-9484.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 9480-9484
    • Holtzman, D.M.1    Pitas, R.E.2    Kilbridge, J.3    Nathan, B.4    Mahley, R.W.5    Bu, G.6    Schwartz, A.L.7
  • 122
    • 0029958248 scopus 로고    scopus 로고
    • Apolipoprotein E-containing high density lipoprotein promotes neurite outgrowth and is a ligand for the low density lipoprotein receptor-related protein
    • Fagan, A. M., G. Bu, Y. Sun, A. Daugherty, and D. M. Holtzman. 1996. Apolipoprotein E-containing high density lipoprotein promotes neurite outgrowth and is a ligand for the low density lipoprotein receptor-related protein. J. Biol. Chem. 271: 30121-30125.
    • (1996) J. Biol. Chem. , vol.271 , pp. 30121-30125
    • Fagan, A.M.1    Bu, G.2    Sun, Y.3    Daugherty, A.4    Holtzman, D.M.5
  • 123
    • 0029157112 scopus 로고
    • The inhibitory effect of apolipoprotein E4 on neurite outgrowth is associated with microtubule depolymerization
    • Nathan, B. P., K-C. Chang, S. Bellosta, E. Brisch, N. Ge, R. W. Mahley, and R. E. Pitas. 1995. The inhibitory effect of apolipoprotein E4 on neurite outgrowth is associated with microtubule depolymerization. J. Biol. Chem. 270: 19791-19799.
    • (1995) J. Biol. Chem. , vol.270 , pp. 19791-19799
    • Nathan, B.P.1    Chang, K.-C.2    Bellosta, S.3    Brisch, E.4    Ge, N.5    Mahley, R.W.6    Pitas, R.E.7
  • 124
    • 0032577695 scopus 로고    scopus 로고
    • Differential cellular accumulation/retention of apolipoprotein E mediated by cell surface heparan sulfate proteoglycans. Apolipoproteins E3 and E2 greater than E4
    • Ji, Z-S., R. E. Pitas, and R. W. Mahley. 1998. Differential cellular accumulation/retention of apolipoprotein E mediated by cell surface heparan sulfate proteoglycans. Apolipoproteins E3 and E2 greater than E4. J. Biol. Chem. 273: 13452-13460.
    • (1998) J. Biol. Chem. , vol.273 , pp. 13452-13460
    • Ji, Z.-S.1    Pitas, R.E.2    Mahley, R.W.3
  • 125
    • 0031892172 scopus 로고    scopus 로고
    • Overexpression of hepatic lipase in transgenic mice decreases apolipoprotein B-containing and high density lipoproteins. Evidence that hepatic lipase acts as a ligand for lipoprotein uptake
    • Dichek, H. L., W. Brecht, J. Fan, Z-S. Ji, S. P. A. McCormick, H. Akeefe, L. Conzo, D. A. Sanan, K. H. Weisgraber, S. G. Young, J. M. Taylor, and R. W. Mahley. 1998. Overexpression of hepatic lipase in transgenic mice decreases apolipoprotein B-containing and high density lipoproteins. Evidence that hepatic lipase acts as a ligand for lipoprotein uptake. J. Biol. Chem. 273: 1896-1903.
    • (1998) J. Biol. Chem. , vol.273 , pp. 1896-1903
    • Dichek, H.L.1    Brecht, W.2    Fan, J.3    Ji, Z.-S.4    McCormick, S.P.A.5    Akeefe, H.6    Conzo, L.7    Sanan, D.A.8    Weisgraber, K.H.9    Young, S.G.10    Taylor, J.M.11    Mahley, R.W.12
  • 126
    • 0028213695 scopus 로고
    • Hepatic lipase may act as a ligand in the uptake of artificial chylomicron remnant-like particles by isolated rat hepatocytes
    • Diard, P., M-I. Malewiak, D. Lagrange, and S. Griglio. 1994. Hepatic lipase may act as a ligand in the uptake of artificial chylomicron remnant-like particles by isolated rat hepatocytes. Biochem. J. 299: 889-894.
    • (1994) Biochem. J. , vol.299 , pp. 889-894
    • Diard, P.1    Malewiak, M.-I.2    Lagrange, D.3    Griglio, S.4


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