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Volumn 37, Issue 4, 1996, Pages 693-707

Lipoprotein lipase and lipolysis: Central roles in lipoprotein metabolism and atherogenesis

Author keywords

apolipoprotein; atherosclerosis; cholesterol; e ndothelial cells; fatty acids; heparin; lipoproteins; proteoglycans; triglyceride

Indexed keywords

APOLIPOPROTEIN; APOLIPOPROTEIN C; APOLIPOPROTEIN E; CHYLOMICRON; GLYCOSAMINOGLYCAN; HIGH DENSITY LIPOPROTEIN; INTERMEDIATE DENSITY LIPOPROTEIN; LIPOPROTEIN; LIPOPROTEIN LIPASE; PROTEOHEPARAN SULFATE; TRIACYLGLYCEROL; VERY LOW DENSITY LIPOPROTEIN;

EID: 0029920693     PISSN: 00222275     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Review
Times cited : (856)

References (163)
  • 1
    • 0027177642 scopus 로고
    • Lipoprotein lipase gene expression: Physiological regulators at the transcriptional and post-translational level
    • Enerback, S., and J. M. Gimble. 1993. Lipoprotein lipase gene expression: physiological regulators at the transcriptional and post-translational level. Biochim. Biophys. Acta. 1169: 107-125.
    • (1993) Biochim. Biophys. Acta , vol.1169 , pp. 107-125
    • Enerback, S.1    Gimble, J.M.2
  • 3
    • 0028327343 scopus 로고
    • Structure, function and role of lipoprotein lipase in lipoprotein metabolism
    • Santamarina-Fojo, S., and K. A. Dugi. 1994. Structure, function and role of lipoprotein lipase in lipoprotein metabolism. Curr. Opin. Lipidol. 5: 117-125.
    • (1994) Curr. Opin. Lipidol. , vol.5 , pp. 117-125
    • Santamarina-Fojo, S.1    Dugi, K.A.2
  • 4
    • 0003024548 scopus 로고
    • Abolishment of alimentary lipemia following injection of heparin
    • Hahn, P. F. 1943. Abolishment of alimentary lipemia following injection of heparin. Science. 98: 19-20.
    • (1943) Science , vol.98 , pp. 19-20
    • Hahn, P.F.1
  • 5
    • 0000717112 scopus 로고
    • Idiopathic hyperlipemia: Metabolic studies in an affected family
    • Havel, R. J., and R. S. Gordon, Jr. 1960. Idiopathic hyperlipemia: metabolic studies in an affected family. J. Clin. Invest. 39: 1777-1790.
    • (1960) J. Clin. Invest. , vol.39 , pp. 1777-1790
    • Havel, R.J.1    Gordon Jr., R.S.2
  • 8
    • 0020672930 scopus 로고
    • Intestinal synthesis, secretion, and transport of lipoproteins
    • Bisgaier, C. L., and R. M. Glickman. 1983. Intestinal synthesis, secretion, and transport of lipoproteins. Annu. Rev. Physiol. 45: 625-636.
    • (1983) Annu. Rev. Physiol. , vol.45 , pp. 625-636
    • Bisgaier, C.L.1    Glickman, R.M.2
  • 9
    • 0343256402 scopus 로고
    • Interchange of apolipoproteins between chylomicrons and high density lipoproteins during alimentary lipemia in man
    • Havel, R. J., J. P. Kane, and M. L. Kashyap. 1973. Interchange of apolipoproteins between chylomicrons and high density lipoproteins during alimentary lipemia in man. J. Clin. Invest. 61: 1654-1665.
    • (1973) J. Clin. Invest. , vol.61 , pp. 1654-1665
    • Havel, R.J.1    Kane, J.P.2    Kashyap, M.L.3
  • 10
    • 0022621329 scopus 로고
    • Post-secretory acquisition of apolipoprotein E by nascent rat hepatic very-low-density lipoproteins in the absence of cholesteryl ester transfer
    • Dolphin, P. J., S. J. Forsyth, and E. S. Krul. 1986. Post-secretory acquisition of apolipoprotein E by nascent rat hepatic very-low-density lipoproteins in the absence of cholesteryl ester transfer. Biochim. Biophys. Acta. 875: 21-30.
    • (1986) Biochim. Biophys. Acta , vol.875 , pp. 21-30
    • Dolphin, P.J.1    Forsyth, S.J.2    Krul, E.S.3
  • 11
    • 0018611740 scopus 로고
    • Removal of apoC-II and apoC-III from VLDL during lipolysis in vitro
    • Eisenberg, S. 1979. Removal of apoC-II and apoC-III from VLDL during lipolysis in vitro. J. Biol. Chem. 254: 12603-12608.
    • (1979) J. Biol. Chem. , vol.254 , pp. 12603-12608
    • Eisenberg, S.1
  • 12
    • 0025248437 scopus 로고
    • Lipoprotein apoC-II activation of lipoprotein lipase. Modulation by apolipoprotein A-IV
    • Goldberg, I. J., C. A. Scheraldi, L. K. Yacoub, U. Saxena, and C. L. Bisgaier. 1990. Lipoprotein apoC-II activation of lipoprotein lipase. Modulation by apolipoprotein A-IV. J. Biol. Chem. 265: 4266-4272.
    • (1990) J. Biol. Chem. , vol.265 , pp. 4266-4272
    • Goldberg, I.J.1    Scheraldi, C.A.2    Yacoub, L.K.3    Saxena, U.4    Bisgaier, C.L.5
  • 13
    • 0021999508 scopus 로고
    • Effect of heparin-induced lipolysis on the distribution of apolipoprotein E among lipoprotein subclasses. Studies with patients deficient in hepatic triglyceride lipase and lipoprotein lipase
    • Rubinstein, A., J. C. Gibson, J. R. J. Paterniti, G. Kakis, A. Little, H. N. Ginsberg, and W. V. Brown. 1985. Effect of heparin-induced lipolysis on the distribution of apolipoprotein E among lipoprotein subclasses. Studies with patients deficient in hepatic triglyceride lipase and lipoprotein lipase. J. Clin. Invest. 75: 710-721.
    • (1985) J. Clin. Invest. , vol.75 , pp. 710-721
    • Rubinstein, A.1    Gibson, J.C.2    Paterniti, J.R.J.3    Kakis, G.4    Little, A.5    Ginsberg, H.N.6    Brown, W.V.7
  • 14
    • 0001298717 scopus 로고
    • Familial HDL deficiency: Tangier disease
    • J. B. Stanbury, J. B. Wyngaarden, D. S. Fredrickson, J. L. Goldstein, and B. S. Brown, editors. McGraw-Hill, New York
    • Herbert, P., G. Assmann, A. Gotto, and D. S. Fredrickson. 1983. Familial HDL deficiency: Tangier disease. In The Metabolic Basis of Inherited Disease. J. B. Stanbury, J. B. Wyngaarden, D. S. Fredrickson, J. L. Goldstein, and B. S. Brown, editors. McGraw-Hill, New York. 589-621.
    • (1983) The Metabolic Basis of Inherited Disease , pp. 589-621
    • Herbert, P.1    Assmann, G.2    Gotto, A.3    Fredrickson, D.S.4
  • 16
    • 0020039856 scopus 로고
    • The C-II/C-III ratio of transferable apolipoprotein in primary and secondary hypertriglyceridemia
    • Erkelens, D. W., and J. A. Mocking. 1982. The C-II/C-III ratio of transferable apolipoprotein in primary and secondary hypertriglyceridemia. Clin. Chim. Acta. 6: 59-65.
    • (1982) Clin. Chim. Acta , vol.6 , pp. 59-65
    • Erkelens, D.W.1    Mocking, J.A.2
  • 17
    • 0027495159 scopus 로고
    • Abnormal activation of lipoprotein lipase by non-equilibrating apoC-II: Further evidence for the presence of non-equilibrating pools of apolipoproteins C-II and C-III in plasma lipoproteins
    • Tornoci, L., C. A. Schcraldi, X. Li, H. Ide, I. J. Goldberg, and N. A. Le. 1993. Abnormal activation of lipoprotein lipase by non-equilibrating apoC-II: further evidence for the presence of non-equilibrating pools of apolipoproteins C-II and C-III in plasma lipoproteins. J. Lipid Res. 34: 1793-1803.
    • (1993) J. Lipid Res. , vol.34 , pp. 1793-1803
    • Tornoci, L.1    Schcraldi, C.A.2    Li, X.3    Ide, H.4    Goldberg, I.J.5    Le, N.A.6
  • 18
    • 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
  • 19
    • 0024593478 scopus 로고
    • Release of endothelial cell lipoprotein lipase by plasma lipoproteins and free fatty acids
    • Saxena, U., L. D. Witte, and I. J. Goldberg. 1989. Release of endothelial cell lipoprotein lipase by plasma lipoproteins and free fatty acids. J. Biol. Chem. 264: 4349-4355.
    • (1989) J. Biol. Chem. , vol.264 , pp. 4349-4355
    • Saxena, U.1    Witte, L.D.2    Goldberg, I.J.3
  • 20
    • 0027319705 scopus 로고
    • Analysis of techniques to obtain plasma for measurement of levels of free fatty acids
    • Zambon, A., S. I. Hashimoto, and J. D. Brunzell. 1993. Analysis of techniques to obtain plasma for measurement of levels of free fatty acids. J. Lipid Res. 34: 1021-1028.
    • (1993) J. Lipid Res. , vol.34 , pp. 1021-1028
    • Zambon, A.1    Hashimoto, S.I.2    Brunzell, J.D.3
  • 21
    • 0021815235 scopus 로고
    • Apolipoprotein effects on the lipolysis of perfused triglyceride by heparin-immobilized milk lipase
    • Clark, A., and S. Quarfordt. 1985. Apolipoprotein effects on the lipolysis of perfused triglyceride by heparin-immobilized milk lipase. J. Biol. Chem. 260: 4778-4783.
    • (1985) J. Biol. Chem. , vol.260 , pp. 4778-4783
    • Clark, A.1    Quarfordt, S.2
  • 22
    • 0024340678 scopus 로고
    • Apolipoprotein E mediates binding of normal very low density lipoprotein to heparin but is not required for high affinity receptor binding
    • Fielding, P. E., Y. Ishikawa, and C. J. Fielding. 1989. Apolipoprotein E mediates binding of normal very low density lipoprotein to heparin but is not required for high affinity receptor binding. J. Biol. Chem. 264: 12462-12466.
    • (1989) J. Biol. Chem. , vol.264 , pp. 12462-12466
    • Fielding, P.E.1    Ishikawa, Y.2    Fielding, C.J.3
  • 23
    • 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
  • 24
    • 0023869649 scopus 로고
    • A change in apolipoprotein B expression is required for the binding of apolipoprotein E to very low density lipoprotein
    • Ishikawa, Y., C. J. Fielding, and P. E. Fielding. 1988. A change in apolipoprotein B expression is required for the binding of apolipoprotein E to very low density lipoprotein. J. Biol. Chem. 263: 2744-2749.
    • (1988) J. Biol. Chem. , vol.263 , pp. 2744-2749
    • Ishikawa, Y.1    Fielding, C.J.2    Fielding, P.E.3
  • 26
    • 0023798732 scopus 로고
    • Heterogeneity of apolipoprotein E epitope expression on human lipoproteins: Importance for apolipoprotein E function
    • Krul, E. S., M. J. Tikkanen, and G. Schonfeld. 1988. Heterogeneity of apolipoprotein E epitope expression on human lipoproteins: importance for apolipoprotein E function. J. Lipid Res. 29: 1309-1325.
    • (1988) J. Lipid Res. , vol.29 , pp. 1309-1325
    • Krul, E.S.1    Tikkanen, M.J.2    Schonfeld, G.3
  • 27
    • 0025835486 scopus 로고
    • Lipolysis exposes unreactive endogenous apolipoprotein E-3 in human and rat plasma very low density lipoprotein
    • Sehayek, E., V. U. Lewin, S. T. Chajek, and S. Eisenberg. 1991. Lipolysis exposes unreactive endogenous apolipoprotein E-3 in human and rat plasma very low density lipoprotein. J. Clin. Invest. 88: 553-560.
    • (1991) J. Clin. Invest. , vol.88 , pp. 553-560
    • Sehayek, E.1    Lewin, V.U.2    Chajek, S.T.3    Eisenberg, S.4
  • 28
    • 0027534554 scopus 로고
    • Hepatic lipase treatment of chylomicron remnants increases exposure of apolipoprotein E
    • Brasaemle, D. L., K. Comely-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    Comely-Moss, K.2    Bensadoun, A.3
  • 29
    • 0025950963 scopus 로고
    • Mechanisms of inhibition by apolipoprotein C of apolipoprotein E-dependent cellular metabolism of human triglyceride-rich lipoproteins through the low density lipoprotein receptor pathway
    • Sehayek, E., and S. Eisenberg. 1991. Mechanisms of inhibition by apolipoprotein C of apolipoprotein E-dependent cellular metabolism of human triglyceride-rich lipoproteins through the low density lipoprotein receptor pathway. J. Biol. Chem. 266: 18259-18267.
    • (1991) J. Biol. Chem. , vol.266 , pp. 18259-18267
    • Sehayek, E.1    Eisenberg, S.2
  • 30
    • 0027301838 scopus 로고
    • The alpha2-macroglobulin receptor/low density lipoprotein receptor-related protein binds lipoprotein lipase and beta-migrating very low density lipoprotein associated with the lipase
    • Nykj;aer, A., O. G. Bengtsson, A. Lookene, S. K. Moestrup, C. M. Petersen, W. Weber, U. Beisiegel, and J. Gliemann. 1993. The alpha2-macroglobulin receptor/low density lipoprotein receptor-related protein binds lipoprotein lipase and beta-migrating very low density lipoprotein associated with the lipase. J. Biol. Chem. 268: 15048-15055.
    • (1993) J. Biol. Chem. , vol.268 , pp. 15048-15055
    • Nykj1    aer, A.2    Bengtsson, O.G.3    Lookene, A.4    Moestrup, S.K.5    Petersen, C.M.6    Weber, W.7    Beisiegel, U.8    Gliemann, J.9
  • 31
    • 0028238889 scopus 로고
    • Cellular catabolism of normal very low density lipopro-teins via the low density lipoprotein receptor-related protein/alpha 2-macroglobulin receptor is induced by the C-terminal domain of lipoprotein lipase
    • Chappell, D. A., I. Inoue, G. L. Fry, M. W. Pladet, S. L. Bowen, P. H. Iverius, J. M. Lalouel, and D. K. Strickland. 1994. Cellular catabolism of normal very low density lipopro-teins via the low density lipoprotein receptor-related protein/alpha 2-macroglobulin receptor is induced by the C-terminal domain of lipoprotein lipase. J. Biol. Chem. 269: 18001-18006.
    • (1994) J. Biol. Chem. , vol.269 , pp. 18001-18006
    • Chappell, D.A.1    Inoue, I.2    Fry, G.L.3    Pladet, M.W.4    Bowen, S.L.5    Iverius, P.H.6    Lalouel, J.M.7    Strickland, D.K.8
  • 32
    • 0027216450 scopus 로고
    • Type III hyperlipoproteinemic phenotype in transgenic mice expressing dysfunctional apolipoprotein E
    • Fazio, S., Y. L. Lee, Z. S. Ji, and S. J. Rall. 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.J.4
  • 33
    • 0019820184 scopus 로고
    • Type III hyperlipoproteinemia associated with apolipoprotein E deficiency
    • Ghiselli, G. E., 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.E.1    Schaefer, E.J.2    Gascon, P.3    Brewer Jr., H.B.4
  • 34
    • 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. J. 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 III, H.B.2    Meng, M.S.3    Skarlatos, S.I.4    Larosa, J.C.5    Brewer Jr., H.J.6
  • 35
    • 0026725757 scopus 로고
    • Severe hypercholesterolemia and atherosclerosis in apolipoprotein E-deficient mice created by homologous recombination in ES cells
    • Plump, A., J. Smith, T. Hayek, K. Aalto-Setala, A. Walsh, J. Verstuyft, E. Rubin, and 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.1    Smith, J.2    Hayek, T.3    Aalto-Setala, K.4    Walsh, A.5    Verstuyft, J.6    Rubin, E.7    Breslow8
  • 36
    • 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
  • 37
    • 15844395514 scopus 로고
    • Overexpression of apolipoprotein C-I causes hypertriglyceridemia and decreased remnant clearance in transgenic mice
    • Shachter, N. S., T. Ebara, R. Ramakrishnan, and J. Smith. 1995. Overexpression of apolipoprotein C-I causes hypertriglyceridemia and decreased remnant clearance in transgenic mice. Circulation. 92: I-106.
    • (1995) Circulation , vol.92
    • Shachter, N.S.1    Ebara, T.2    Ramakrishnan, R.3    Smith, J.4
  • 41
    • 0022971151 scopus 로고
    • Apolipoprotein B metabolism in subjects with deficiency of apolipoproteins C-III and A-I. Evidence that apolipoprotein C-III inhibits catabolism of triglyceride-rich lipoproteins by lipoprotein lipase in vivo
    • Ginsberg, H. N., N. A. Le, I. J. Goldberg, J. C. Gibson, A. Rubinstein, I. P. Wang, R. Norum, and W. V. Brown. 1986. Apolipoprotein B metabolism in subjects with deficiency of apolipoproteins C-III and A-I. Evidence that apolipoprotein C-III inhibits catabolism of triglyceride-rich lipoproteins by lipoprotein lipase in vivo. J. Clin. Invest. 78: 1287-1295.
    • (1986) J. Clin. Invest. , vol.78 , pp. 1287-1295
    • Ginsberg, H.N.1    Le, N.A.2    Goldberg, I.J.3    Gibson, J.C.4    Rubinstein, A.5    Wang, I.P.6    Norum, R.7    Brown, W.V.8
  • 42
    • 0025302165 scopus 로고
    • Opposing effects of apolipoproteins E and C on lipoprotein binding to low density lipoprotein receptor-related protein
    • Kowal, R. C., J. Herz, K. H. Weisgraber, R. W. Mahley, M. S. Brown, and J. L. Goldstein. 1990. Opposing effects of apolipoproteins E and C on lipoprotein binding to low density lipoprotein receptor-related protein. J. Biol. Chem. 265: 10771-10779.
    • (1990) J. Biol. Chem. , vol.265 , pp. 10771-10779
    • Kowal, R.C.1    Herz, J.2    Weisgraber, K.H.3    Mahley, R.W.4    Brown, M.S.5    Goldstein, J.L.6
  • 43
    • 0019138139 scopus 로고
    • Regulation of hepatic uptake of triglyceride-rich lipoproteins in the rat
    • Windler, E., Y. Chao, and R. J. Havel. 1980. Regulation of hepatic uptake of triglyceride-rich lipoproteins in the rat. J. Biol. Chem. 255: 8303-8306.
    • (1980) J. Biol. Chem. , vol.255 , pp. 8303-8306
    • Windler, E.1    Chao, Y.2    Havel, R.J.3
  • 44
    • 0018834489 scopus 로고
    • Effect of apolipoproteins on hepatic uptake of triglyceride emulsions in the rat
    • Shelburne, F., J. Hanks, W. Meyers, and S. Quarfordt. 1980. Effect of apolipoproteins on hepatic uptake of triglyceride emulsions in the rat. J. Clin. Invest. 65: 652-658.
    • (1980) J. Clin. Invest. , vol.65 , pp. 652-658
    • Shelburne, F.1    Hanks, J.2    Meyers, W.3    Quarfordt, S.4
  • 45
    • 0027509976 scopus 로고
    • Reduced lipolysis of large apoE-poor very-low-density lipoprotein subfractions from type IV hypertriglyceridemic subjects in vitro and in vivo
    • Evans, A. J., B. M. Wolfe, W. L. Strong, and M. W. Huff. 1993. Reduced lipolysis of large apoE-poor very-low-density lipoprotein subfractions from type IV hypertriglyceridemic subjects in vitro and in vivo. Metab. Clin. Exp. 42: 105-115.
    • (1993) Metab. Clin. Exp. , vol.42 , pp. 105-115
    • Evans, A.J.1    Wolfe, B.M.2    Strong, W.L.3    Huff, M.W.4
  • 46
    • 0015530365 scopus 로고
    • Inhibition of lipoprotein lipase by an apoprotein of human very low density lipoprotein
    • Brown, W. V., and M. L. Baginsky. 1972. Inhibition of lipoprotein lipase by an apoprotein of human very low density lipoprotein. Biochem. Biophys. Res. Commun. 46: 375-381.
    • (1972) Biochem. Biophys. Res. Commun. , vol.46 , pp. 375-381
    • Brown, W.V.1    Baginsky, M.L.2
  • 47
    • 0019453469 scopus 로고
    • Interaction of lipoprotein lipase with phospholipid vesicles: Role of apolipoprotein C-II and heparin
    • Shirari, K., N. Matsuoka, and R. L. Jackson. 1981. Interaction of lipoprotein lipase with phospholipid vesicles: role of apolipoprotein C-II and heparin. Biochim. Biophys. Acta. 665: 504-510.
    • (1981) Biochim. Biophys. Acta , vol.665 , pp. 504-510
    • Shirari, K.1    Matsuoka, N.2    Jackson, R.L.3
  • 48
    • 0027984980 scopus 로고
    • Kinetics of Hpolysis of very low density lipoproteins by lipoprotein lipase. Importance of particle number and noncompetitive inhibition by particles with low triglyceride content
    • Connelly, P. W., G. F. Maguire, C. Vezina, R. A. Hegele, and A. Kuksis. 1994. Kinetics of Hpolysis of very low density lipoproteins by lipoprotein lipase. Importance of particle number and noncompetitive inhibition by particles with low triglyceride content. J. Biol. Chem. 269: 20554-20560.
    • (1994) J. Biol. Chem. , vol.269 , pp. 20554-20560
    • Connelly, P.W.1    Maguire, G.F.2    Vezina, C.3    Hegele, R.A.4    Kuksis, A.5
  • 49
    • 0025216496 scopus 로고
    • The effects of weight loss on the activity and expression of adipose-tissue lipoprotein lipase in very obese humans
    • Kern, P. A., J. M. Ong, B. Saffari, and J. Carty. 1990. The effects of weight loss on the activity and expression of adipose-tissue lipoprotein lipase in very obese humans. N. Engl. J. Med. 322: 1053-1059.
    • (1990) N. Engl. J. Med. , vol.322 , pp. 1053-1059
    • Kern, P.A.1    Ong, J.M.2    Saffari, B.3    Carty, J.4
  • 50
    • 0025264939 scopus 로고
    • The response of lipoprotein lipase to feeding and fasting. Evidence for posttranslational regulation
    • Doolittle, M. H., Z. O. Ben, J. Elovson, D. Martin, and T. G. Kirchgessner. 1990. The response of lipoprotein lipase to feeding and fasting. Evidence for posttranslational regulation. J. Biol. Chem. 265: 4570-4577.
    • (1990) J. Biol. Chem. , vol.265 , pp. 4570-4577
    • Doolittle, M.H.1    Ben, Z.O.2    Elovson, J.3    Martin, D.4    Kirchgessner, T.G.5
  • 51
    • 0019804407 scopus 로고
    • Binding of lipoprotein lipase to endothelial cells in culture
    • Cheng, C. F., A. OØsta, A. Bensadoun, and R. D. Rosenberg. 1981. Binding of lipoprotein lipase to endothelial cells in culture. J. Biol. Chem. 256: 12893-12896.
    • (1981) J. Biol. Chem. , vol.256 , pp. 12893-12896
    • Cheng, C.F.1    Oøsta, A.2    Bensadoun, A.3    Rosenberg, R.D.4
  • 52
    • 0026583305 scopus 로고
    • Patterns of sulphation in heparan sulphate: Polymorphism based on a common structural theme
    • Gallagher, J. T., J. E. Turnbull, and M. Lyon. 1992. Patterns of sulphation in heparan sulphate: polymorphism based on a common structural theme. Int. J. Biochem. 24: 553-560.
    • (1992) Int. J. Biochem. , vol.24 , pp. 553-560
    • Gallagher, J.T.1    Turnbull, J.E.2    Lyon, M.3
  • 53
    • 0026733347 scopus 로고
    • Cell surface heparan sulfate proteoglycans from human vascular endothelial cells. Core protein characterization and antithrombin III binding properties
    • Mertens, G., J. Cassiman, H. Van den Berghe, J. Vermylen, and G. David. 1992. Cell surface heparan sulfate proteoglycans from human vascular endothelial cells. Core protein characterization and antithrombin III binding properties. J. Biol. Chem. 267: 20435-20443.
    • (1992) J. Biol. Chem. , vol.267 , pp. 20435-20443
    • Mertens, G.1    Cassiman, J.2    Van Den Berghe, H.3    Vermylen, J.4    David, G.5
  • 54
    • 0025991749 scopus 로고
    • Identification and characterization of the endothelial cell surface lipoprotein lipase receptor
    • Saxena, U., M. G. Klein, and I. J. Goldberg. 1991. Identification and characterization of the endothelial cell surface lipoprotein lipase receptor. J. Biol. Chem. 266: 17516-17521.
    • (1991) J. Biol. Chem. , vol.266 , pp. 17516-17521
    • Saxena, U.1    Klein, M.G.2    Goldberg, I.J.3
  • 55
    • 0026317977 scopus 로고
    • The complete sequence of perlecan, a basement membrane heparan sulfate proteoglycan, reveals extensive similarity with laminin A chain, low density lipoprotein-receptor, and the neural cell adhesion molecule
    • Noonan, D. M., A. Fulle, P. Valente, S. Cai, E. Horigan, M. Sasaki, Y. Yamada, and J. R. Hassell. 1991. The complete sequence of perlecan, a basement membrane heparan sulfate proteoglycan, reveals extensive similarity with laminin A chain, low density lipoprotein-receptor, and the neural cell adhesion molecule. J. Biol. Chem. 266: 22939-22947.
    • (1991) J. Biol. Chem. , vol.266 , pp. 22939-22947
    • Noonan, D.M.1    Fulle, A.2    Valente, P.3    Cai, S.4    Horigan, E.5    Sasaki, M.6    Yamada, Y.7    Hassell, J.R.8
  • 56
    • 0026758187 scopus 로고
    • Primary structure of the human heparan sulfate proteoglycan from basement membrane (HSPG2/perlecan)
    • Murdoch, A. D., G. R. Dodge, I. Cohen, R. S. Tuan, and R. V. Iozzo. 1992. Primary structure of the human heparan sulfate proteoglycan from basement membrane (HSPG2/perlecan). J. Biol. Chem. 267: 8544-8557.
    • (1992) J. Biol. Chem. , vol.267 , pp. 8544-8557
    • Murdoch, A.D.1    Dodge, G.R.2    Cohen, I.3    Tuan, R.S.4    Iozzo, R.V.5
  • 57
    • 0027931863 scopus 로고
    • Purification and characterization of adipocyte heparan sulfate proteoglycans with affinity for lipoprotein lipase
    • Misa, K. B., K. C. Kim, S. Cho, M. G. Low, and A. Bensadoun. 1994. Purification and characterization of adipocyte heparan sulfate proteoglycans with affinity for lipoprotein lipase. J. Biol. Chem. 269: 23838-23844.
    • (1994) J. Biol. Chem. , vol.269 , pp. 23838-23844
    • Misa, K.B.1    Kim, K.C.2    Cho, S.3    Low, M.G.4    Bensadoun, A.5
  • 58
    • 0024454582 scopus 로고
    • Phosphatidylinositol-specific phospholipase C releases lipoprotein lipase from the heparin releasable pool in rat heart cell cultures
    • Chajek-Shaul, T., O. Halimi, M. Ben-Naim, O. Stein, and Y. Stein. 1989. Phosphatidylinositol-specific phospholipase C releases lipoprotein lipase from the heparin releasable pool in rat heart cell cultures. Biochim. Biophys. Acta. 1014: 178-183.
    • (1989) Biochim. Biophys. Acta , vol.1014 , pp. 178-183
    • Chajek-Shaul, T.1    Halimi, O.2    Ben-Naim, M.3    Stein, O.4    Stein, Y.5
  • 60
    • 0026012414 scopus 로고
    • Effect of chlorate on the sulfation of lipoprotein lipase and heparan sulfate proteoglycans. Sulfation of heparan sulfate proteoglycans affects lipoprotein lipase degradation
    • Hoogewerf, A. J., L. A. Cisar, D. C. Evans, and A. Bensadoun. 1991. Effect of chlorate on the sulfation of lipoprotein lipase and heparan sulfate proteoglycans. Sulfation of heparan sulfate proteoglycans affects lipoprotein lipase degradation. J. Biol. Chem. 266: 16564-16571.
    • (1991) J. Biol. Chem. , vol.266 , pp. 16564-16571
    • Hoogewerf, A.J.1    Cisar, L.A.2    Evans, D.C.3    Bensadoun, A.4
  • 61
    • 0028121995 scopus 로고
    • Oligosaccharide sequences of endothelial cell surface heparan sulfate proteoglycan with affinity for lipoprotein lipase
    • Parthasarathy, N., I. J. Goldberg, P. Sivaram, B. Mulloy, D. M. Flory, and W. D. Wagner. 1994. Oligosaccharide sequences of endothelial cell surface heparan sulfate proteoglycan with affinity for lipoprotein lipase. J. Biol. Chem. 269: 22391-22396.
    • (1994) J. Biol. Chem. , vol.269 , pp. 22391-22396
    • Parthasarathy, N.1    Goldberg, I.J.2    Sivaram, P.3    Mulloy, B.4    Flory, D.M.5    Wagner, W.D.6
  • 62
    • 0028902050 scopus 로고
    • Structure of heparin fragments with high affinity for lipoprotein lipase and inhibition of lipoprotein lipase binding to alpha 2-macroglobulin-receptor/low density lipoprotein receptor-related protein by heparin fragments
    • Larnkjaer, A., A. Nykjaer, G. Olivecrona, H. Thogersen, and P. Ostergaard. 1995. Structure of heparin fragments with high affinity for lipoprotein lipase and inhibition of lipoprotein lipase binding to alpha 2-macroglobulin-receptor/low density lipoprotein receptor-related protein by heparin fragments. Biochem. J. 307: 205-214.
    • (1995) Biochem. J. , vol.307 , pp. 205-214
    • Larnkjaer, A.1    Nykjaer, A.2    Olivecrona, G.3    Thogersen, H.4    Ostergaard, P.5
  • 63
    • 0026727774 scopus 로고
    • Identification of the basic fibroblast growth factor binding sequence in fibroblast heparan sulfate
    • Turnbull, J. E., D. G. Fernig, Y. Ke, M. C. Wilkinson, and J. T. Gallagher. 1992. Identification of the basic fibroblast growth factor binding sequence in fibroblast heparan sulfate. J. Biol. Chem. 267: 10337-10341.
    • (1992) J. Biol. Chem. , vol.267 , pp. 10337-10341
    • Turnbull, J.E.1    Fernig, D.G.2    Ke, Y.3    Wilkinson, M.C.4    Gallagher, J.T.5
  • 64
    • 0026699160 scopus 로고
    • Identification of a heparin-releasable lipoprotein lipase binding protein from endothelial cells
    • Sivaram, P., M. G. Klein, and I. J. Goldberg. 1992. Identification of a heparin-releasable lipoprotein lipase binding protein from endothelial cells. J. Biol. Chem. 267: 16517-16552.
    • (1992) J. Biol. Chem. , vol.267 , pp. 16517-16552
    • Sivaram, P.1    Klein, M.G.2    Goldberg, I.J.3
  • 65
    • 0028341102 scopus 로고
    • An amino-terminal fragment of apolipoprotein-B binds to lipoprotein lipase and may facilitate its binding to endothelial cells
    • Sivaram, P., S. Y. Choi, L. K. Curtiss, and I.J. Goldberg. 1994. An amino-terminal fragment of apolipoprotein-B binds to lipoprotein lipase and may facilitate its binding to endothelial cells. J. Biol. Chem. 269: 9409-9412.
    • (1994) J. Biol. Chem. , vol.269 , pp. 9409-9412
    • Sivaram, P.1    Choi, S.Y.2    Curtiss, L.K.3    Goldberg, I.J.4
  • 66
    • 0025308491 scopus 로고
    • Metabolism of endothelial cell-bound lipoprotein lipase: Evidence for heparan sulfate proteoglycan-mediated internalization and recycling
    • Saxena, U., M. G. Klein, and I. J. Goldberg. 1990. Metabolism of endothelial cell-bound lipoprotein lipase: evidence for heparan sulfate proteoglycan-mediated internalization and recycling. J. Biol. Chem. 265: 12880-12886.
    • (1990) J. Biol. Chem. , vol.265 , pp. 12880-12886
    • Saxena, U.1    Klein, M.G.2    Goldberg, I.J.3
  • 68
    • 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
  • 69
    • 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
  • 70
    • 0028007160 scopus 로고
    • A carboxyl-terminal fragment of lipoprotein lipase binds to the low density lipoprotein receptor-related protein and inhibits lipase-mediated uptake of lipoprotein in cells
    • Nykjaer, A., M. Nielsen, A. Lookene, N. Meyer, H. Roigaard, M. Etzerodt, U. Beisiegel, G. Olivecrona, and J. Gliemann. 1994. A carboxyl-terminal fragment of lipoprotein lipase binds to the low density lipoprotein receptor-related protein and inhibits lipase-mediated uptake of lipoprotein in cells. J. Biol. Chem. 269: 31747-31755.
    • (1994) J. Biol. Chem. , vol.269 , pp. 31747-31755
    • Nykjaer, A.1    Nielsen, M.2    Lookene, A.3    Meyer, N.4    Roigaard, H.5    Etzerodt, M.6    Beisiegel, U.7    Olivecrona, G.8    Gliemann, J.9
  • 71
    • 0028206237 scopus 로고
    • The carboxyl-terminal domain of lipoprotein lipase binds to the low density lipoprotein receptor-related protein/alpha 2-macroglobulin receptor (LRP) and mediates binding of normal very low density lipoproteins to LRP
    • Williams, S. E., I. Inoue, H. Tran, G. L. Fry, M. W. Pladet, P. H. Iverius, J. M. Lalouel, D. A. Chappell, and D. K. Strickland. 1994. The carboxyl-terminal domain of lipoprotein lipase binds to the low density lipoprotein receptor-related protein/alpha 2-macroglobulin receptor (LRP) and mediates binding of normal very low density lipoproteins to LRP. J. Biol. Chem. 269: 8653-8658.
    • (1994) J. Biol. Chem. , vol.269 , pp. 8653-8658
    • Williams, S.E.1    Inoue, I.2    Tran, H.3    Fry, G.L.4    Pladet, M.W.5    Iverius, P.H.6    Lalouel, J.M.7    Chappell, D.A.8    Strickland, D.K.9
  • 72
    • 0027079937 scopus 로고
    • Low density lipoprotein receptor-related protein and gp330 bind similar ligands, including plasminogen activator-inhibitor complexes and lactoferrin, an inhibitor of chylomicron remnant clearance
    • Willnow, T. E., J. L. Goldstein, K. Orth, M. S. Brown, and J. Herz. 1992. Low density lipoprotein receptor-related protein and gp330 bind similar ligands, including plasminogen activator-inhibitor complexes and lactoferrin, an inhibitor of chylomicron remnant clearance. J. Biol. Chem. 267: 26172-26180.
    • (1992) J. Biol. Chem. , vol.267 , pp. 26172-26180
    • Willnow, T.E.1    Goldstein, J.L.2    Orth, K.3    Brown, M.S.4    Herz, J.5
  • 73
    • 0028848182 scopus 로고
    • The very low density lipoprotein receptor mediates the cellular catabolism of lipoprotein lipase and urokinase-plasminogen activator inhibitor type I complexes
    • Argraves, K. M., F. D. Battey, C. D. MacCalman, M. K. R. M. Gafvels, K. F. Kozarsky, D. A. Chappell, J. F. Straus III, and D. K. Strickland. 1995. The very low density lipoprotein receptor mediates the cellular catabolism of lipoprotein lipase and urokinase-plasminogen activator inhibitor type I complexes. J. Biol. Chem. 270: 26550-26557.
    • (1995) J. Biol. Chem. , vol.270 , pp. 26550-26557
    • Argraves, K.M.1    Battey, F.D.2    MacCalman, C.D.3    Gafvels, M.K.R.M.4    Kozarsky, K.F.5    Chappell, D.A.6    Straus III, J.F.7    Strickland, D.K.8
  • 75
    • 0028126081 scopus 로고
    • Lipoprotein metabolism and its relationship to atherosclerosis
    • Ginsberg, H. N. 1994. Lipoprotein metabolism and its relationship to atherosclerosis. Med. Clin. North Am. 78: 1-20.
    • (1994) Med. Clin. North Am. , vol.78 , pp. 1-20
    • Ginsberg, H.N.1
  • 76
    • 0025284868 scopus 로고
    • Conversion of plasma VLDL and IDL precursors into various LDL subpopulations using density gradient ultracentrifugation
    • Marzetta, C. A., D. M. Foster, and J. D. Brunzell. 1990. Conversion of plasma VLDL and IDL precursors into various LDL subpopulations using density gradient ultracentrifugation. J. Lipid Res. 31: 975-984.
    • (1990) J. Lipid Res. , vol.31 , pp. 975-984
    • Marzetta, C.A.1    Foster, D.M.2    Brunzell, J.D.3
  • 77
    • 0020421218 scopus 로고
    • Lipoprotein metabolism during acute inhibition of hepatic triglyceride lipase in the cynomolgus monkey
    • Goldberg, I. J., N. A. Le, J. R. J. Paterniti, H. N. Ginsberg, F. T. Lindgren, and W. V. Brown. 1982. Lipoprotein metabolism during acute inhibition of hepatic triglyceride lipase in the cynomolgus monkey. J. Clin. Invest. 70: 1184-1192.
    • (1982) J. Clin. Invest. , vol.70 , pp. 1184-1192
    • Goldberg, I.J.1    Le, N.A.2    Paterniti, J.R.J.3    Ginsberg, H.N.4    Lindgren, F.T.5    Brown, W.V.6
  • 78
    • 0025020619 scopus 로고
    • Role of triglyceride-rich lipoproteins in progression of atherosclerosis
    • Havel, R. J. 1990. Role of triglyceride-rich lipoproteins in progression of atherosclerosis. Circulation. 81: 694-696.
    • (1990) Circulation , vol.81 , pp. 694-696
    • Havel, R.J.1
  • 79
    • 0021963038 scopus 로고
    • Regulation of the production and catabolism of plasma low density lipoproteins in hypertriglyceridemic subjects: Effect of weight loss
    • Ginsberg, H. N., N-A. Le, and J. C. Gibson. 1985. Regulation of the production and catabolism of plasma low density lipoproteins in hypertriglyceridemic subjects: effect of weight loss. J. Clin. Invest. 75: 614-623.
    • (1985) J. Clin. Invest. , vol.75 , pp. 614-623
    • Ginsberg, H.N.1    Le, N.-A.2    Gibson, J.C.3
  • 80
    • 0025878691 scopus 로고
    • Lipoprotein physiology in nondiabetic and diabetic states. Relationship to atherogenesis
    • Ginsberg, H. N. 1991. Lipoprotein physiology in nondiabetic and diabetic states. Relationship to atherogenesis. Diabetes Care. 14: 839-855.
    • (1991) Diabetes Care , vol.14 , pp. 839-855
    • Ginsberg, H.N.1
  • 81
    • 0017752356 scopus 로고
    • The effect of treatment with clofibrale on hepatic triglyceride and lipoprotein lipase activities from human postheparin plasma in male patients with hyperlipoproteinemia
    • Boberg, J., M. Boberg, R. Gross, S. Grundy, J. Augustin, and W. V. Brown. 1977. The effect of treatment with clofibrale on hepatic triglyceride and lipoprotein lipase activities from human postheparin plasma in male patients with hyperlipoproteinemia. Atherosclerosis. 27: 499-503.
    • (1977) Atherosclerosis , vol.27 , pp. 499-503
    • Boberg, J.1    Boberg, M.2    Gross, R.3    Grundy, S.4    Augustin, J.5    Brown, W.V.6
  • 82
    • 0026731011 scopus 로고
    • Familial combined hyperlipidemia and abnormal lipoprotein lipase
    • Babirak, S. P., B. G. Brown, and J. D. Brunzell. 1992. Familial combined hyperlipidemia and abnormal lipoprotein lipase. Arterioscler. Thromb. 12: 1176-1183.
    • (1992) Arterioscler. Thromb. , vol.12 , pp. 1176-1183
    • Babirak, S.P.1    Brown, B.G.2    Brunzell, J.D.3
  • 83
    • 0026012340 scopus 로고
    • Lipoprotein lipase modulates net secretory output of apolipoprotein B in vitro. A possible pathophysiologic explanation for familial combined hyperlipidemia
    • Williams, K. J., K. A. Petrie, R. W. Brocia, and T. L. Swenson. 1991. Lipoprotein lipase modulates net secretory output of apolipoprotein B in vitro. A possible pathophysiologic explanation for familial combined hyperlipidemia. J. Clin. Invest. 88: 1300-1306.
    • (1991) J. Clin. Invest. , vol.88 , pp. 1300-1306
    • Williams, K.J.1    Petrie, K.A.2    Brocia, R.W.3    Swenson, T.L.4
  • 84
    • 15844379377 scopus 로고
    • Uptake of hypertriglyceridemia VLDL by HepG2 cells requires active lipoprotein lipase and cell surface proteoglycans
    • Abstract
    • Huff, M. W., D. B. Miller, B. M. Wilfe, and C. G. Sawyez. 1994. Uptake of hypertriglyceridemia VLDL by HepG2 cells requires active lipoprotein lipase and cell surface proteoglycans. Circulation. 90: I-289 Abstract.
    • (1994) Circulation , vol.90
    • Huff, M.W.1    Miller, D.B.2    Wilfe, B.M.3    Sawyez, C.G.4
  • 85
    • 0024551698 scopus 로고
    • Lipoprotein lipase and hepatic lipase mRNA tissue specific expression, developmental regulation, and evolution
    • Semenkovich, C., S. Chen, M. Wims, C. Luo, W. Li, and L. Chan. 1989. Lipoprotein lipase and hepatic lipase mRNA tissue specific expression, developmental regulation, and evolution. J. Lipid Res. 30: 423-431.
    • (1989) J. Lipid Res. , vol.30 , pp. 423-431
    • Semenkovich, C.1    Chen, S.2    Wims, M.3    Luo, C.4    Li, W.5    Chan, L.6
  • 88
    • 0024549336 scopus 로고
    • Role of triglyceride-rich lipoproteins from the liver and intestine in the etiology of postprandial peaks in plasma triglyceride concentration
    • Cohn, J. S., J. R. McNamara, S. D. Krasinski, R. M. Russell, and E. J. Schaefer. 1989. Role of triglyceride-rich lipoproteins from the liver and intestine in the etiology of postprandial peaks in plasma triglyceride concentration. Metabolism. 38: 484-490.
    • (1989) Metabolism , vol.38 , pp. 484-490
    • Cohn, J.S.1    McNamara, J.R.2    Krasinski, S.D.3    Russell, R.M.4    Schaefer, E.J.5
  • 91
    • 0028364882 scopus 로고
    • Dissociation of lipid-free apolipoprotein A-I from high density lipoproteins
    • Liang, H. Q., K. A. Rye, and P. J. Barter. 1994. Dissociation of lipid-free apolipoprotein A-I from high density lipoproteins. J. Lipid Res. 35: 1187-1199.
    • (1994) J. Lipid Res. , vol.35 , pp. 1187-1199
    • Liang, H.Q.1    Rye, K.A.2    Barter, P.J.3
  • 92
    • 0026509641 scopus 로고
    • Changes in particle size of high density lipoproteins during incubation with very low density lipoproteins, cholesteryl ester transfer protein and lipoprotein lipase
    • Newnham, H. H., and P. J. Barter. 1992. Changes in particle size of high density lipoproteins during incubation with very low density lipoproteins, cholesteryl ester transfer protein and lipoprotein lipase. Biochim. Biophys. Acta. 1125: 297-304.
    • (1992) Biochim. Biophys. Acta , vol.1125 , pp. 297-304
    • Newnham, H.H.1    Barter, P.J.2
  • 93
    • 0027215121 scopus 로고
    • Increased plasma and renal clearance of an exchangeable pool of apolipoprotein A-I in subjects with low levels of high density lipoprotein cholesterol
    • Horowitz, B. S., I. J. Goldberg, J. Merab, T. M. Vanni, R. Ramakrishnan, and H. N. Ginsberg. 1993. Increased plasma and renal clearance of an exchangeable pool of apolipoprotein A-I in subjects with low levels of high density lipoprotein cholesterol. J. Clin. Invest. 91: 1743-1752.
    • (1993) J. Clin. Invest. , vol.91 , pp. 1743-1752
    • Horowitz, B.S.1    Goldberg, I.J.2    Merab, J.3    Vanni, T.M.4    Ramakrishnan, R.5    Ginsberg, H.N.6
  • 94
    • 0026073753 scopus 로고
    • Increased apoA-I and apoA-II fractional catabolic rate in patients with low high density lipoprotein-cholesterol levels with or without hypertriglyceridemia
    • Brinton, E. A., S. Eisenberg, and J. L. Breslow. 1991. Increased apoA-I and apoA-II fractional catabolic rate in patients with low high density lipoprotein-cholesterol levels with or without hypertriglyceridemia. J. Clin. Invest. 87: 536-544.
    • (1991) J. Clin. Invest. , vol.87 , pp. 536-544
    • Brinton, E.A.1    Eisenberg, S.2    Breslow, J.L.3
  • 95
    • 0025033939 scopus 로고
    • Role of lipoprotein lipase in the regulation of high density lipoprotein apolipoprotein metabolism. Studies in normal and lipoprotein lipase-inhibited monkeys
    • Goldberg, I. J., W. S. Blaner, T. M. Vanni, M. Moukides, and R. Ramakrishnan. 1990. Role of lipoprotein lipase in the regulation of high density lipoprotein apolipoprotein metabolism. Studies in normal and lipoprotein lipase-inhibited monkeys. J. Clin. Invest. 86: 463-473.
    • (1990) J. Clin. Invest. , vol.86 , pp. 463-473
    • Goldberg, I.J.1    Blaner, W.S.2    Vanni, T.M.3    Moukides, M.4    Ramakrishnan, R.5
  • 96
    • 0029086881 scopus 로고
    • Lipoprotein lipase mass and activity in plasma and increase after heparin are separate parameters with different relations to plasma lipoproteins
    • Tornvall, P., G. Olivecrona, F. Karpe, A. Hamsten, and T. Olivecrona. 1995. Lipoprotein lipase mass and activity in plasma and increase after heparin are separate parameters with different relations to plasma lipoproteins. Arterioscler. Thromb. Vasc. Biol. 15: 1086-1093.
    • (1995) Arterioscler. Thromb. Vasc. Biol. , vol.15 , pp. 1086-1093
    • Tornvall, P.1    Olivecrona, G.2    Karpe, F.3    Hamsten, A.4    Olivecrona, T.5
  • 97
    • 0027220709 scopus 로고
    • Activities of lipoprotein lipase and hepatic triglyceride lipase in postheparin plasma of patients with low concentrations of HDL cholesterol
    • Blades, B., G. L. Vega, and S. M. Grundy. 1993. Activities of lipoprotein lipase and hepatic triglyceride lipase in postheparin plasma of patients with low concentrations of HDL cholesterol. Arterioscler. Thromb. 13: 1227-1235.
    • (1993) Arterioscler. Thromb. , vol.13 , pp. 1227-1235
    • Blades, B.1    Vega, G.L.2    Grundy, S.M.3
  • 98
    • 0023160916 scopus 로고
    • High density lipoprotein: Relationship of the plasma levels of this lipoprotein species to its composition, to the magnitude of postprandial lipidemia, and to the activities of lipoprotein lipase and hepatic lipase
    • Patsch, J. R., S. Prasad, A. M. Gotto Jr., and W. Patsch. 1987. High density lipoprotein: relationship of the plasma levels of this lipoprotein species to its composition, to the magnitude of postprandial lipidemia, and to the activities of lipoprotein lipase and hepatic lipase. J. Clin. Invest. 80: 341-347.
    • (1987) J. Clin. Invest. , vol.80 , pp. 341-347
    • Patsch, J.R.1    Prasad, S.2    Gotto Jr., A.M.3    Patsch, W.4
  • 99
  • 100
    • 0025850858 scopus 로고
    • Dissociation between postprandial lipemia and high density lipoprotein cholesterol concentrations in endurance-trained men
    • Cohen, J. C., G. J. Stray, and S. M. Grundy. 1991. Dissociation between postprandial lipemia and high density lipoprotein cholesterol concentrations in endurance-trained men. Arterioscler. Thromb. 11: 838-843.
    • (1991) Arterioscler. Thromb. , vol.11 , pp. 838-843
    • Cohen, J.C.1    Stray, G.J.2    Grundy, S.M.3
  • 101
    • 0028231188 scopus 로고
    • Postprandial hyperlipidemia and remnant lipoproteins
    • Havel, R. J. 1994. Postprandial hyperlipidemia and remnant lipoproteins. Curr. Opin. Lipidol. 5: 102-109.
    • (1994) Curr. Opin. Lipidol. , vol.5 , pp. 102-109
    • Havel, R.J.1
  • 102
    • 0027260912 scopus 로고
    • The novel compound NO-1886 increases lipoprotein lipase activity with resulting elevation of high density lipoprotein cholesterol, and long-term administration inhibits atherogenesis in the coronary arteries of rats with experimental atherosclerosis
    • Tsutsumi, K., Y. Inoue, A. Shima, K. Iwasaki, M. Kawamura, and T. Murase. 1993. The novel compound NO-1886 increases lipoprotein lipase activity with resulting elevation of high density lipoprotein cholesterol, and long-term administration inhibits atherogenesis in the coronary arteries of rats with experimental atherosclerosis. J. Clin. Invest. 92: 411-417.
    • (1993) J. Clin. Invest. , vol.92 , pp. 411-417
    • Tsutsumi, K.1    Inoue, Y.2    Shima, A.3    Iwasaki, K.4    Kawamura, M.5    Murase, T.6
  • 103
    • 0016176637 scopus 로고
    • Selective measurement of two lipase activities in postheparin plasma from normal subjects and patients with hyperlipoproteinemia
    • Krauss, R. M., R. I. Levy, and D. S. Frederickson. 1974. Selective measurement of two lipase activities in postheparin plasma from normal subjects and patients with hyperlipoproteinemia. J. Clin. Invest. 54: 1107-1124.
    • (1974) J. Clin. Invest. , vol.54 , pp. 1107-1124
    • Krauss, R.M.1    Levy, R.I.2    Frederickson, D.S.3
  • 104
    • 0017202148 scopus 로고
    • A stable, radioactive substrate emulsion for assay of lipoprotein lipase
    • Nilsson-Ehle, P., and M. C. Schotz. 1976. A stable, radioactive substrate emulsion for assay of lipoprotein lipase. J. Lipid Res. 17: 536-541.
    • (1976) J. Lipid Res. , vol.17 , pp. 536-541
    • Nilsson-Ehle, P.1    Schotz, M.C.2
  • 105
    • 0015783897 scopus 로고
    • Evidence for a common, saturable triglyceride removal mechanism for chylomicrons and very low density lipoproteins in man
    • Brunzell, J. D., W. R. Hazzard, D. J. Porte, and E. L. Bierman. 1973. Evidence for a common, saturable triglyceride removal mechanism for chylomicrons and very low density lipoproteins in man. J. Clin. Invest. 52: 1578-1585.
    • (1973) J. Clin. Invest. , vol.52 , pp. 1578-1585
    • Brunzell, J.D.1    Hazzard, W.R.2    Porte, D.J.3    Bierman, E.L.4
  • 108
    • 0028230229 scopus 로고
    • Liposome-like particles isolated from human atherosclerotic plaques are structurally and compositionally similar to surface remnants of triglyceride-rich lipoproteins
    • Chung, B. H., G. Tallis, V. Yalamoori, G. M. Anantharamaiah, and J. P. Segrest. 1994. Liposome-like particles isolated from human atherosclerotic plaques are structurally and compositionally similar to surface remnants of triglyceride-rich lipoproteins. Arterioscler. Thromb. 14: 622-635.
    • (1994) Arterioscler. Thromb. , vol.14 , pp. 622-635
    • Chung, B.H.1    Tallis, G.2    Yalamoori, V.3    Anantharamaiah, G.M.4    Segrest, J.P.5
  • 109
    • 0021135449 scopus 로고
    • Exposure to free fatty acids increases the transfer of albumin across cultured endothelial monolayers
    • Hennig, B., D. M. Shasby, A. B. Fulton, and A. A. Spector. 1984. Exposure to free fatty acids increases the transfer of albumin across cultured endothelial monolayers. Arteriosclerosis. 4: 489-497.
    • (1984) Arteriosclerosis , vol.4 , pp. 489-497
    • Hennig, B.1    Shasby, D.M.2    Fulton, A.B.3    Spector, A.A.4
  • 110
    • 0026604386 scopus 로고
    • Lipoprotein lipase increases low density lipoprotein (LDL) retention by subendothelial cell matrix
    • Saxena, U., M. G. Klein, T. M. Vanni, and I. J. Goldberg. 1992. Lipoprotein lipase increases low density lipoprotein (LDL) retention by subendothelial cell matrix. J. Clin. Invest. 89: 373-380.
    • (1992) J. Clin. Invest. , vol.89 , pp. 373-380
    • Saxena, U.1    Klein, M.G.2    Vanni, T.M.3    Goldberg, I.J.4
  • 111
    • 0018649439 scopus 로고
    • Atherogenesis: A postprandial phenomenon
    • Zilversmit, D. B. 1979. Atherogenesis: a postprandial phenomenon. Circulation. 60: 473-485.
    • (1979) Circulation , vol.60 , pp. 473-485
    • Zilversmit, D.B.1
  • 113
    • 0026751376 scopus 로고
    • Lipoprotein lipase is synthesized by macrophage-derived foam cells in human coronary atherosclerotic plaques
    • O'Brien, K., D. Gordon, S. Deeb, M. Ferguson, and A. Chait. 1992. Lipoprotein lipase is synthesized by macrophage-derived foam cells in human coronary atherosclerotic plaques. J. Clin. Invest. 89: 1544-1550.
    • (1992) J. Clin. Invest. , vol.89 , pp. 1544-1550
    • O'Brien, K.1    Gordon, D.2    Deeb, S.3    Ferguson, M.4    Chait, A.5
  • 114
    • 0027435105 scopus 로고
    • Expression of lipoprotein lipase mRNA and secretion in macrophages isolated from human atherosclerotic aorta
    • Mattson, L., H. Johansson, M. Ottosson, G. Bondjers, and O. Wiflund. 1993. Expression of lipoprotein lipase mRNA and secretion in macrophages isolated from human atherosclerotic aorta. J. Clin. Invest. 92: 1759-1765.
    • (1993) J. Clin. Invest. , vol.92 , pp. 1759-1765
    • Mattson, L.1    Johansson, H.2    Ottosson, M.3    Bondjers, G.4    Wiflund, O.5
  • 115
    • 0027393983 scopus 로고
    • High macrophage lipoprotein lipase expression and secretion are associated in inbred murine strains with susceptibility to atherosclerosis
    • Renier, G., E. Skamene, J. B. DeSanctis, and D. Radzioch. 1993. High macrophage lipoprotein lipase expression and secretion are associated in inbred murine strains with susceptibility to atherosclerosis. Arterioscler. Thromb. 13: 190-196.
    • (1993) Arterioscler. Thromb. , vol.13 , pp. 190-196
    • Renier, G.1    Skamene, E.2    Desanctis, J.B.3    Radzioch, D.4
  • 116
    • 0028148295 scopus 로고
    • Endothelial cells and atherosclerosis: Lipoprotein metabolism, matrix interactions, and monocyte recruitment
    • Saxena, U., and I. J. Goldberg. 1994. Endothelial cells and atherosclerosis: lipoprotein metabolism, matrix interactions, and monocyte recruitment. Curr. Opin. Lipidol. 5: 316-322.
    • (1994) Curr. Opin. Lipidol. , vol.5 , pp. 316-322
    • Saxena, U.1    Goldberg, I.J.2
  • 118
    • 0027447261 scopus 로고
    • Lipoprotein-proteoglycan complexes induce continued cholesteryl ester accumulation in foam cells from rabbit atherosclerotic lesions
    • Vijayagopal, P., S. R. Srinivasan, J. H. Xu, E. J. Dalferes, B. Radhakrishnamurthy, and G. S. Berenson. 1993. Lipoprotein-proteoglycan complexes induce continued cholesteryl ester accumulation in foam cells from rabbit atherosclerotic lesions. J. Clin. Invest. 91: 1011-1018.
    • (1993) J. Clin. Invest. , vol.91 , pp. 1011-1018
    • Vijayagopal, P.1    Srinivasan, S.R.2    Xu, J.H.3    Dalferes, E.J.4    Radhakrishnamurthy, B.5    Berenson, G.S.6
  • 119
    • 0023765741 scopus 로고
    • Identification of apoB-100 segments mediating the interaction of low density lipoproteins with arterial proteoglycans
    • Camejo, G., S. O. Olofsson, F. Lopez, P. Carlsson, and G. Bondjers. 1988. Identification of apoB-100 segments mediating the interaction of low density lipoproteins with arterial proteoglycans. Arteriosclerosis. 8: 368-377.
    • (1988) Arteriosclerosis , vol.8 , pp. 368-377
    • Camejo, G.1    Olofsson, S.O.2    Lopez, F.3    Carlsson, P.4    Bondjers, G.5
  • 120
    • 0027210886 scopus 로고
    • Binding of low density lipoproteins by proteoglycans synthesized by proliferating and quiescent human arterial smooth muscle cells
    • Camejo, G., G. Fager, B. Rosengren, E. Hurt-Camejo, and G. Bondjers. 1993. Binding of low density lipoproteins by proteoglycans synthesized by proliferating and quiescent human arterial smooth muscle cells. J. Biol. Chem. 268: 14131-14137.
    • (1993) J. Biol. Chem. , vol.268 , pp. 14131-14137
    • Camejo, G.1    Fager, G.2    Rosengren, B.3    Hurt-Camejo, E.4    Bondjers, G.5
  • 121
    • 0027315587 scopus 로고
    • Injury to the arterial wall of rabbits produces proteoglycan variants with enhanced low-density lipoprotein-binding property
    • Srinivasan, S., J-H. Xu, P. Vijayagopal, B. Radhakrisnamurthy, and G. Berenson. 1993. Injury to the arterial wall of rabbits produces proteoglycan variants with enhanced low-density lipoprotein-binding property. Biochim. Biophys. Acta. 1168: 158-166.
    • (1993) Biochim. Biophys. Acta , vol.1168 , pp. 158-166
    • Srinivasan, S.1    Xu, J.-H.2    Vijayagopal, P.3    Radhakrisnamurthy, B.4    Berenson, G.5
  • 122
    • 0018094816 scopus 로고
    • Aortic total glycosaminoglycan and dermatan sulfate changes in atherosclerotic rhesus monkeys
    • Wagner, W. D., and B. G. J. Salisbury. 1978. Aortic total glycosaminoglycan and dermatan sulfate changes in atherosclerotic rhesus monkeys. Lab. Invest. 39: 322-328.
    • (1978) Lab. Invest. , vol.39 , pp. 322-328
    • Wagner, W.D.1    Salisbury, B.G.J.2
  • 123
    • 0028277932 scopus 로고
    • Apolipoprotein E localization in human coronary atherosclerotic plaques by in situ hybridization and immunohistochemistry and comparison with lipoprotein lipase
    • O'Brien, K. D., S. S. Deeb, M. Ferguson, T. O. McDonald, M. D. Allen, C. E. Alpers, and A. Chait. 1994. Apolipoprotein E localization in human coronary atherosclerotic plaques by in situ hybridization and immunohistochemistry and comparison with lipoprotein lipase. Am. J. Pathol. 144: 538-548.
    • (1994) Am. J. Pathol. , vol.144 , pp. 538-548
    • O'Brien, K.D.1    Deeb, S.S.2    Ferguson, M.3    McDonald, T.O.4    Allen, M.D.5    Alpers, C.E.6    Chait, A.7
  • 124
    • 0026442201 scopus 로고
    • Lipoprotein lipase enhances the binding of lipoprotein to heparan sulfate on cell surfaces and extracellular matrix
    • Eisenberg, S., E. Sehayek, T. Olivecrona, and I. Vlodavsky. 1992. Lipoprotein lipase enhances the binding of lipoprotein 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
  • 125
    • 0027199612 scopus 로고
    • Apolipoprotein E modulates low density lipoprotein retention by lipoprotein lipase anchored to the subendothelial matrix
    • Saxena, U., E. Ferguson, and C. L. Bisgaier. 1993. Apolipoprotein E modulates low density lipoprotein retention by lipoprotein lipase anchored to the subendothelial matrix. J. Biol. Chem. 268: 14812-14819.
    • (1993) J. Biol. Chem. , vol.268 , pp. 14812-14819
    • Saxena, U.1    Ferguson, E.2    Bisgaier, C.L.3
  • 126
    • 0027257233 scopus 로고
    • Lipoprotein lipase and sphingomyelinase synergistically enhance the association of atherogenic lipoproteins with smooth muscle cells and extracellular matrix. A possible mechanism for low density lipoprotein and lipoprotein[a] retention and macrophage foam cell formation
    • Tabas, I., Y. Li, R. W. Brocia, S. W. Xu, T. L. Swenson, and K. J. Williams. 1993. Lipoprotein lipase and sphingomyelinase synergistically enhance the association of atherogenic lipoproteins with smooth muscle cells and extracellular matrix. A possible mechanism for low density lipoprotein and lipoprotein[a] retention and macrophage foam cell formation. J. Biol. Chem. 268: 20419-20432.
    • (1993) J. Biol. Chem. , vol.268 , pp. 20419-20432
    • Tabas, I.1    Li, Y.2    Brocia, R.W.3    Xu, S.W.4    Swenson, T.L.5    Williams, K.J.6
  • 127
    • 0028364881 scopus 로고
    • Lipoprotein lipase (LPL) affects low density lipoprotein (LDL) flux through vascular tissue: Evidence that LpL increases LDL accumulation in vascular tissue
    • Rutledge, J. C., and I. J. Goldberg. 1994. Lipoprotein lipase (LPL) affects low density lipoprotein (LDL) flux through vascular tissue: evidence that LpL increases LDL accumulation in vascular tissue. J. Lipid Res. 35: 1152-1160.
    • (1994) J. Lipid Res. , vol.35 , pp. 1152-1160
    • Rutledge, J.C.1    Goldberg, I.J.2
  • 128
    • 0027232531 scopus 로고
    • Lipoprotein lipase enhances the interaction of low density lipoproteins with artery-derived extracellular matrix proteoglycans
    • Edwards, I. J., I. J. Goldberg, J. S. Parks, H. Xu, and W. D. Wagner. 1993. Lipoprotein lipase enhances the interaction of low density lipoproteins with artery-derived extracellular matrix proteoglycans. J. Lipid Res. 34: 1155-1163.
    • (1993) J. Lipid Res. , vol.34 , pp. 1155-1163
    • Edwards, I.J.1    Goldberg, I.J.2    Parks, J.S.3    Xu, H.4    Wagner, W.D.5
  • 129
    • 0028919850 scopus 로고
    • Differentiated macrophages synthesize a heparan sulfate proteoglycan and an oversulfated chondroitin sulfate proteoglycan that bind lipoprotein lipase
    • Edwards, I. J., H. Xu, J. C. Obunike, I. J. Goldberg, and W. D. Wagner. 1995. Differentiated macrophages synthesize a heparan sulfate proteoglycan and an oversulfated chondroitin sulfate proteoglycan that bind lipoprotein lipase. Arteriosder. Thromb. Vasc. Biol. 15: 400-409.
    • (1995) Arteriosder. Thromb. Vasc. Biol. , vol.15 , pp. 400-409
    • Edwards, I.J.1    Xu, H.2    Obunike, J.C.3    Goldberg, I.J.4    Wagner, W.D.5
  • 130
    • 0022828956 scopus 로고
    • Association of plasma lipoproteins with postheparin plasma lipase activities
    • Goldberg, I. J., J. J. Kandell, C. B. Blum, and H. N. Ginsberg. 1986. Association of plasma lipoproteins with postheparin plasma lipase activities. J. Clin. Invest. 78: 1523-1528.
    • (1986) J. Clin. Invest. , vol.78 , pp. 1523-1528
    • Goldberg, I.J.1    Kandell, J.J.2    Blum, C.B.3    Ginsberg, H.N.4
  • 133
    • 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
  • 134
    • 0019489905 scopus 로고
    • Secretion of lipoprotein lipase by macrophages in culture
    • Khoo, J. C., E. Mahoney, and J. L. Witztum. 1981. Secretion of lipoprotein lipase by macrophages in culture. J. Biol. Chem. 256: 7105-7108.
    • (1981) J. Biol. Chem. , vol.256 , pp. 7105-7108
    • Khoo, J.C.1    Mahoney, E.2    Witztum, J.L.3
  • 135
    • 0020040736 scopus 로고
    • Lipoprotein lipase secretion by human monocyte-derived macrophages
    • Chait, A., P. H. Iverius, and J. D. Brunzell. 1982. Lipoprotein lipase secretion by human monocyte-derived macrophages. J. Clin. Invest. 69: 490-493.
    • (1982) J. Clin. Invest. , vol.69 , pp. 490-493
    • Chait, A.1    Iverius, P.H.2    Brunzell, J.D.3
  • 136
    • 0021869041 scopus 로고
    • Bovine milk lipoprotein lipase transfers tocopherol to human fibroblasts during triglyceride hydrolysis in vitro
    • Traber, M., T. Olivecrona, and H. Kayden. 1985. Bovine milk lipoprotein lipase transfers tocopherol to human fibroblasts during triglyceride hydrolysis in vitro. J. Clin. Invest. 75: 1729-1734.
    • (1985) J. Clin. Invest. , vol.75 , pp. 1729-1734
    • Traber, M.1    Olivecrona, T.2    Kayden, H.3
  • 138
    • 0020624151 scopus 로고
    • The role of lipoprotein lipase in the metabolism of triglyceride-rich lipoproteins by macrophages
    • Lindqvist, P., J. L. Ostlund-Lindqvist, J. L. Witztum, D. Steinberg, and J. A. Little. 1983. The role of lipoprotein lipase in the metabolism of triglyceride-rich lipoproteins by macrophages. J. Biol. Chem. 258: 9086-9092.
    • (1983) J. Biol. Chem. , vol.258 , pp. 9086-9092
    • Lindqvist, P.1    Ostlund-Lindqvist, J.L.2    Witztum, J.L.3    Steinberg, D.4    Little, J.A.5
  • 139
    • 0020680963 scopus 로고
    • Transfer of cholesteryl linoleyl ether from phosphatidylcholine and phosphatidylethanolamine liposomes to cultured cells catalyzed by lipoprotein lipase
    • Stein, O., G. Friedman, T. Chajek-Shaul, G. Halperin, T. Olivecrona, and Y. Stein. 1983. Transfer of cholesteryl linoleyl ether from phosphatidylcholine and phosphatidylethanolamine liposomes to cultured cells catalyzed by lipoprotein lipase. Biochim. Biophys. Acta. 750: 306-316.
    • (1983) Biochim. Biophys. Acta , vol.750 , pp. 306-316
    • Stein, O.1    Friedman, G.2    Chajek-Shaul, T.3    Halperin, G.4    Olivecrona, T.5    Stein, Y.6
  • 140
    • 0023808098 scopus 로고
    • Modification of low density lipoprotein by lipoprotein lipase or hepatic lipase enhances uptake and cholesterol accumulation in cells
    • Aviram, M., E. L. Bierman, and A. Chait. 1988. Modification of low density lipoprotein by lipoprotein lipase or hepatic lipase enhances uptake and cholesterol accumulation in cells. J. Biol. Chem. 263: 15416-15422.
    • (1988) J. Biol. Chem. , vol.263 , pp. 15416-15422
    • Aviram, M.1    Bierman, E.L.2    Chait, A.3
  • 141
    • 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, B. T. Van, 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, B.T.4    Frants, R.R.5    Havekes, L.M.6
  • 142
    • 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
  • 145
    • 0029022909 scopus 로고
    • The stimulation of the cholesterol esterification pathway by atherogenic lipoproteins in macrophages
    • Tabas, I. 1995. The stimulation of the cholesterol esterification pathway by atherogenic lipoproteins in macrophages. Curr. Opin. Lipidol. 6: 260-268.
    • (1995) Curr. Opin. Lipidol. , vol.6 , pp. 260-268
    • Tabas, I.1
  • 146
    • 0024563653 scopus 로고
    • Lipolytic surface remnants of triglyceride-rich lipoproteins are cytotoxic to macrophages but not in the presence of high density lipoprotein. A possible mechanism of atherogenesis?
    • Chung, B. H., J. P. Segrest, K. Smith, F. M. Griffin, and C. G. Brouillette. 1989. Lipolytic surface remnants of triglyceride-rich lipoproteins are cytotoxic to macrophages but not in the presence of high density lipoprotein. A possible mechanism of atherogenesis? J. Clin. Invest. 83: 1363-1374.
    • (1989) J. Clin. Invest. , vol.83 , pp. 1363-1374
    • Chung, B.H.1    Segrest, J.P.2    Smith, K.3    Griffin, F.M.4    Brouillette, C.G.5
  • 147
    • 0028945953 scopus 로고
    • Oleate and other long chain fatty acids stimulate low density lipoprotein receptor activity by enhancing acyl coenzyme A:cholesterol acyltransferase activity and altering intracellular regulatory cholesterol pools in cultured cells
    • Rumsey, S. C., N. F. Galeano, B. Lipschitz, and R. J. Deckelbaum. 1995. Oleate and other long chain fatty acids stimulate low density lipoprotein receptor activity by enhancing acyl coenzyme A:cholesterol acyltransferase activity and altering intracellular regulatory cholesterol pools in cultured cells. J. Biol. Chem. 270: 10008-10016.
    • (1995) J. Biol. Chem. , vol.270 , pp. 10008-10016
    • Rumsey, S.C.1    Galeano, N.F.2    Lipschitz, B.3    Deckelbaum, R.J.4
  • 148
    • 0026581783 scopus 로고
    • Lipoprotein lipase and hepatic triglyceride lipase: Molecular and genetic aspects
    • Lalouel, J., D. Wilson, and P. Iverius. 1992. Lipoprotein lipase and hepatic triglyceride lipase: molecular and genetic aspects. Curr. Opin. Lipidol. 3: 86-95.
    • (1992) Curr. Opin. Lipidol. , vol.3 , pp. 86-95
    • Lalouel, J.1    Wilson, D.2    Iverius, P.3
  • 149
    • 0014055221 scopus 로고
    • Tissue lipoprotein lipase in normal individuals and in individuals with exogenous hypertriglyceridemia and the relationship of this enzyme to assimilation of fat
    • Harlan, W. R., P. S. Winesett, and A. J. Wasserman. 1967. Tissue lipoprotein lipase in normal individuals and in individuals with exogenous hypertriglyceridemia and the relationship of this enzyme to assimilation of fat. J. Clin. Invest. 46: 239-247.
    • (1967) J. Clin. Invest. , vol.46 , pp. 239-247
    • Harlan, W.R.1    Winesett, P.S.2    Wasserman, A.J.3
  • 150
    • 0025167797 scopus 로고
    • Phenotypic expression of heterozygous lipoprotein lipase deficiency in the extended pedigree of a proband homozygous for a missense mutation
    • Wilson, D., M. Emi, P. Iverius, A. Hata, L. Wu, E. Hillas, R. Williams, and J. Lalouel. 1990. Phenotypic expression of heterozygous lipoprotein lipase deficiency in the extended pedigree of a proband homozygous for a missense mutation. J. Clin. Invest. 86: 735-750.
    • (1990) J. Clin. Invest. , vol.86 , pp. 735-750
    • Wilson, D.1    Emi, M.2    Iverius, P.3    Hata, A.4    Wu, L.5    Hillas, E.6    Williams, R.7    Lalouel, J.8
  • 151
    • 0027299427 scopus 로고
    • Gene-environment interaction in the conversion of a mild-to-severe phenotype in a patient homozygous for a Ser172 → Cys mutation in the lipoprotein lipase gene
    • Ma, Y., M. S. Liu, D. Ginzinger, J. Frohlich, J. D. Brunzell, and M. R. Hayden. 1993. Gene-environment interaction in the conversion of a mild-to-severe phenotype in a patient homozygous for a Ser172 → Cys mutation in the lipoprotein lipase gene. J. Clin. Invest. 91: 1953-1958.
    • (1993) J. Clin. Invest. , vol.91 , pp. 1953-1958
    • Ma, Y.1    Liu, M.S.2    Ginzinger, D.3    Frohlich, J.4    Brunzell, J.D.5    Hayden, M.R.6
  • 152
    • 0028230993 scopus 로고
    • High frequency of mutations in the human lipoprotein lipase gene in pregnancy induced chylomicronemia: Possible association with apolipoprotein E2 isoform
    • Ma, Y., T. Ooi, M. Liu, H. Zhang, R. McPherson, A. Edwards, I. Forsythe, J. Frohlich, J. Brunzell, and M. Hayden. 1994. High frequency of mutations in the human lipoprotein lipase gene in pregnancy induced chylomicronemia: possible association with apolipoprotein E2 isoform. J. Lipid Res. 35: 1066-1075.
    • (1994) J. Lipid Res. , vol.35 , pp. 1066-1075
    • Ma, Y.1    Ooi, T.2    Liu, M.3    Zhang, H.4    McPherson, R.5    Edwards, A.6    Forsythe, I.7    Frohlich, J.8    Brunzell, J.9    Hayden, M.10
  • 153
    • 0025845830 scopus 로고
    • DNA polymorphism haplotypes of the human lipoprotein lipase gene: Possible association with high density lipoprotein levels
    • Heizmann, C., T. Kirchgessner, P. O. Kwiterovich, J. A. Ladias, C. Derby, S. E. Antonarakis, and A. J. Lusis. 1991. DNA polymorphism haplotypes of the human lipoprotein lipase gene: possible association with high density lipoprotein levels. Hum. Genet. 86: 578-584.
    • (1991) Hum. Genet. , vol.86 , pp. 578-584
    • Heizmann, C.1    Kirchgessner, T.2    Kwiterovich, P.O.3    Ladias, J.A.4    Derby, C.5    Antonarakis, S.E.6    Lusis, A.J.7
  • 156
    • 15844402552 scopus 로고
    • Lipoprotein lipase may contribute to the varient degree of atherosclerosis in homozygous familial hypercholesterolemia
    • abstract
    • Dugi, K. A., I. M. Feuerstein, S. Santamarina-Fojo, H. B. Brewer, Jr., and J. M. Hoeg. 1994. Lipoprotein lipase may contribute to the varient degree of atherosclerosis in homozygous familial hypercholesterolemia. Circulation. 90: I-405 (abstract).
    • (1994) Circulation , vol.90
    • Dugi, K.A.1    Feuerstein, I.M.2    Santamarina-Fojo, S.3    Brewer Jr., H.B.4    Hoeg, J.M.5
  • 157
    • 0027193327 scopus 로고
    • Prevention of raised low-density lipoprotein cholesterol in a patient with familial hypercholesterolaemia and lipoprolein lipase deficiency
    • Zambon, A., A. Torres, S. Bijvoet, C. Gagne, S. Moorjani, P. J. Lupien, M. R. Hayden, and J. D. Brunzell. 1993. Prevention of raised low-density lipoprotein cholesterol in a patient with familial hypercholesterolaemia and lipoprolein lipase deficiency. Lancet. 341: 1119-1121.
    • (1993) Lancet , vol.341 , pp. 1119-1121
    • Zambon, A.1    Torres, A.2    Bijvoet, S.3    Gagne, C.4    Moorjani, S.5    Lupien, P.J.6    Hayden, M.R.7    Brunzell, J.D.8
  • 160
    • 0027296725 scopus 로고
    • Overexpression of human lipoprotein lipase in transgenic mice. Resistance to diet-induced hypertriglyceridemia and hypercholesterolemia
    • Shimada, M., H. Shimano, T. Gotoda, K. Yamamoto, M. Kawamura, T. Inaba, Y. Yazaki, and N. Yamada. 1993. Overexpression of human lipoprotein lipase in transgenic mice. Resistance to diet-induced hypertriglyceridemia and hypercholesterolemia. J. Biol. Chem. 268: 17924-17929.
    • (1993) J. Biol. Chem. , vol.268 , pp. 17924-17929
    • Shimada, M.1    Shimano, H.2    Gotoda, T.3    Yamamoto, K.4    Kawamura, M.5    Inaba, T.6    Yazaki, Y.7    Yamada, N.8
  • 161
    • 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
  • 162
    • 0029079312 scopus 로고
    • COOH-disruption of lipoprotein lipase in mice is lethal in homozygotes, but heterozygotes have elevated triglycerides and impaired enzyme activity
    • Coleman, T., R. L. Seip, J. M. Gimble, D. Lee, N. Maeda, and C. F. Semenkovich. 1995. COOH-disruption of lipoprotein lipase in mice is lethal in homozygotes, but heterozygotes have elevated triglycerides and impaired enzyme activity. J. Biol. Chem. 270: 12518-12525.
    • (1995) J. Biol. Chem. , vol.270 , pp. 12518-12525
    • Coleman, T.1    Seip, R.L.2    Gimble, J.M.3    Lee, D.4    Maeda, N.5    Semenkovich, C.F.6


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