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Volumn 6, Issue 3, 1995, Pages 117-122

Receptors for triglyceride-rich lipoproteins and their role in lipoprotein metabolism

Author keywords

[No Author keywords available]

Indexed keywords

APOLIPOPROTEIN B; APOLIPOPROTEIN E; CHYLOMICRON; LIPOPROTEIN; LIPOPROTEIN RECEPTOR; LOW DENSITY LIPOPROTEIN RECEPTOR; PROTEOGLYCAN; RECEPTOR PROTEIN; VERY LOW DENSITY LIPOPROTEIN;

EID: 0029027459     PISSN: 09579672     EISSN: None     Source Type: Journal    
DOI: 10.1097/00041433-199506000-00002     Document Type: Review
Times cited : (64)

References (37)
  • 1
    • 0022549920 scopus 로고
    • A receptor-mediated pathway for cholesterol homeostasis
    • Brown MS, Goldstein JL: A receptor-mediated pathway for cholesterol homeostasis. Science 1986, 232:34-47.
    • (1986) Science , vol.232 , pp. 34-47
    • Brown, M.S.1    Goldstein, J.L.2
  • 2
    • 0024449363 scopus 로고
    • The LDL-receptor-related protein, LRP, is an apolipoprotein E binding protein
    • Beisiegel U, Weber W, Ihrke G, Herz J, Stanley KK: The LDL-receptor-related protein, LRP, is an apolipoprotein E binding protein. Nature 1989, 341:162-164.
    • (1989) Nature , vol.341 , pp. 162-164
    • Beisiegel, U.1    Weber, W.2    Ihrke, G.3    Herz, J.4    Stanley, K.K.5
  • 3
    • 0025940314 scopus 로고
    • Lipoprotein lipase enhances the binding of chylomicrons to low density lipoprotein receptor-related protein
    • Beisiegel U, Weber W, Bengtsson-Olivecrona G: Lipoprotein lipase enhances the binding of chylomicrons to low density lipoprotein receptor-related protein. Proc Natl Acad Sci USA 1991, 88:8342-8346.
    • (1991) Proc Natl Acad Sci USA , vol.88 , pp. 8342-8346
    • Beisiegel, U.1    Weber, W.2    Bengtsson-Olivecrona, G.3
  • 4
    • 0028172032 scopus 로고
    • 2M receptor/LRP in chylomicron remnant metabolism
    • Edited by Borth W, Feinmann RD, Gonias SL, Quigley JP, Strickland DK. New York: The New York Academy of Science
    • 2-macroglobulin, its receptor and related proteins (Annals of New York Academy of Science, vol 737). Edited by Borth W, Feinmann RD, Gonias SL, Quigley JP, Strickland DK. New York: The New York Academy of Science; 1994:53-69. This overview on the function of LRP as the chylomicron remnant receptor summarizes the current knowledge on the interaction between apoE, LPL and hepatic lipase and the cell surface. These ligands bind to cell-surface proteoglycans first and their uptake is subsequently mediated by receptors, most probably LRP. The LRP-mediated uptake is compared in different cell lines.
    • (1994) 2-macroglobulin, Its Receptor and Related Proteins (Annals of New York Academy of Science, Vol 737) , vol.737 , pp. 53-69
    • Beisiegel, U.1    Krapp, A.2    Weber, W.3    Olivecrona, G.4
  • 5
    • 0028263619 scopus 로고
    • Enhanced binding and uptake of remnant lipoproteins by hepatic lipase-secreting hepatoma cells in culture
    • Ji Z-S, Lauer Sj, Fazio S, Bensadoun A, Taylor JM, Mahley RW: Enhanced binding and uptake of remnant lipoproteins by hepatic lipase-secreting hepatoma cells in culture. J Biol Chem 1994, 269:13429-13436. The role of hepatic lipase in mediating lipoprotein binding to cells, as described in this paper, underlines the current concept that lipase binding to cells and potential receptors is mediated through an interaction with cell-surface heparan sulphate proteoglycans.
    • (1994) J Biol Chem , vol.269 , pp. 13429-13436
    • Ji, Z.-S.1    Lauer, Sj.2    Fazio, S.3    Bensadoun, A.4    Taylor, J.M.5    Mahley, R.W.6
  • 6
    • 0026778830 scopus 로고
    • Rabbit very low density lipoprotein receptor: A low density lipoprotein receptor-like protein with distinct ligand specificity
    • Takahashi S, Kawarabayasi Y, Nakai T, Sakai J, Yamamoto T: Rabbit very low density lipoprotein receptor: a low density lipoprotein receptor-like protein with distinct ligand specificity. Proc Natl Acad Sci USA 1992, 89.9252-9256.
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 9252-9256
    • Takahashi, S.1    Kawarabayasi, Y.2    Nakai, T.3    Sakai, J.4    Yamamoto, T.5
  • 8
    • 0027989299 scopus 로고
    • Cellular binding site and membrane binding proteins for triglyceride-rich lipoproteins in human monocyte-macrophages and THP-1 monocytic cells
    • Gianturco SH, Ramprasad MP, Lin AH-Y, Song R, Bradley WA: Cellular binding site and membrane binding proteins for triglyceride-rich lipoproteins in human monocyte-macrophages and THP-1 monocytic cells. J Lipid Res 1994, 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
  • 9
    • 0028097841 scopus 로고
    • Structure, chromosome location, and expression of the human very low density lipoprotein receptor gene
    • Sakai J, Hishino A, Takahashi S, Miura Y, Ishii H, Suzuki H, Kawarabayasi Y, Yamamoto T: Structure, chromosome location, and expression of the human very low density lipoprotein receptor gene. J Biol Chem 1994, 269:2173-2181. This paper describes the isolation and characterization of VLDL complementary DNA from humans The organization of the receptor gene has been demonstrated and compared with the rabbit receptor, and its expression is not down-regulated by sterols.
    • (1994) J Biol Chem , vol.269 , pp. 2173-2181
    • Sakai, J.1    Hishino, A.2    Takahashi, S.3    Miura, Y.4    Ishii, H.5    Suzuki, H.6    Kawarabayasi, Y.7    Yamamoto, T.8
  • 10
    • 0028213695 scopus 로고
    • Hepatic lipase may act as a ligand in the uptake of artificial chylomicron remnant-like particles by isolated rat hepatocytes
    • Diaro P, Malewiak M-I, Lagrange D, Griglio S: Hepatic lipase may act as a ligand in the uptake of artificial chylomicron remnant-like particles by isolated rat hepatocytes. Biochem J 1994, 299-889-894.
    • (1994) Biochem J , vol.299 , pp. 889-894
    • Diaro, P.1    Malewiak, M.-I.2    Lagrange, D.3    Griglio, S.4
  • 11
    • 0028007160 scopus 로고
    • A carboxylterminal fragment of lipoprotein lipase binds to the low density lipoprotein receptor-related protein and inhibits lipase-mediated uptake of lipoproteins to cells
    • Nykjaer A, Nielsen M, Lookene A, Meyer N, Roigaard H, Etzerodt M, Beisiegel U, Olivecrona G, Gliemann J: A carboxylterminal fragment of lipoprotein lipase binds to the low density lipoprotein receptor-related protein and inhibits lipase-mediated uptake of lipoproteins to cells. J Biol Chem 1994, 269:31747-31755. The LRP binding site has been located within residues 378-423 in human LPL. Studies performed with fragments containing these residues demonstrated that these fragments were able to inhibit the binding of LPL to LRP and LPL-mediated binding of lipoprotein to cells.
    • (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
  • 12
    • 0028284556 scopus 로고
    • Inhibition of hepatic chylomicron remnant uptake by gene transfer of a receptor antagonist
    • Willnow E, Sheng Z, Ishibashi S, Herz J: Inhibition of hepatic chylomicron remnant uptake by gene transfer of a receptor antagonist. Science 1994, 264:1471-1474. The importance of this model is that it represents the first demonstration of the function of LRP as a lipoprotein receptor in vivo. It has also shed some light on the open question of the role of the LDL receptor in remnant catabolism in vivo. The data suggest that both the LDL receptor and LRP could be involved in remnant clearance in mice.
    • (1994) Science , vol.264 , pp. 1471-1474
    • Willnow, E.1    Sheng, Z.2    Ishibashi, S.3    Herz, J.4
  • 13
    • 0028284381 scopus 로고
    • Effect of the 39-kDa receptor-associated protein on the hepatic uptake and endocytosis of chylomicron remnants and low density lipoproteins in the rat
    • Mokuno H, Brady S, Kotite L, Herz J, Havel J: Effect of the 39-kDa receptor-associated protein on the hepatic uptake and endocytosis of chylomicron remnants and low density lipoproteins in the rat. J Biol Chem 1994, 269:13238-13243. The pathway by which chylomicron remnants are taken up in the liver is shown to be clearly inhibited by RAP. This finding is very important because it might have decisive relevance for the regulation of this pathway. The authors also demonstrate that RAP interferes not only with LRP binding but also with the binding of ligands to the LDL receptor.
    • (1994) J Biol Chem , vol.269 , pp. 13238-13243
    • Mokuno, H.1    Brady, S.2    Kotite, L.3    Herz, J.4    Havel, J.5
  • 14
    • 0028093321 scopus 로고
    • The 39-kDa receptor-associated protein regulates ligand binding by the very low density lipoprotein receptor
    • Battey FD, Gafvels ME, FitzGerald DJ, Argraves WS, Chappell DA, Strauss JF, Strickland DK: The 39-kDa receptor-associated protein regulates ligand binding by the very low density lipoprotein receptor. J Biol Chem 1994, 269.23268-23273. The purified VLDL receptor (130kDa) bound VLDL on nitrocellulose membranes but not LDL VLDL binding was completely inhibited by RAP, and this protein also inhibited the uptake of VLDL by cells over-expressing the VLDL receptor. This suggests a common functional role for RAP in modulating ligand binding by members of the LDL receptor gene family.
    • (1994) J Biol Chem , vol.269 , pp. 23268-23273
    • Battey, F.D.1    Gafvels, M.E.2    FitzGerald, D.J.3    Argraves, W.S.4    Chappell, D.A.5    Strauss, J.F.6    Strickland, D.K.7
  • 15
    • 0028347117 scopus 로고
    • Secretion-recapture process of apolipoprotein E in hepatic uptake of chylomicron remnants in transgenic mice
    • Shimano H, Namba Y, Ohsuga J, Kawamura M, Yamamoto K, Shimada M, Gotoda T, Harada K, Yazaki Y, Yamada N: Secretion-recapture process of apolipoprotein E in hepatic uptake of chylomicron remnants in transgenic mice. J Clin Invest 1994, 93:2215-2223. Surplus rat apoE, demonstrated on the surface of hepatocytes in transgenic mice, was markedly reduced after chylomicron infusion. This indicated that chylomicrons were captured by apoE on the cell surface, and the chylomicron-apoE complex was subsequently taken up through receptor-mediated endocytosis. This mechanism could only be demonstrated for chylomicrons, but not for VLDL or LDL. It might, therefore, be an important step in the rapid clearance of chylomicron remnants.
    • (1994) J Clin Invest , vol.93 , pp. 2215-2223
    • Shimano, H.1    Namba, Y.2    Ohsuga, J.3    Kawamura, M.4    Yamamoto, K.5    Shimada, M.6    Gotoda, T.7    Harada, K.8    Yazaki, Y.9    Yamada, N.10
  • 16
    • 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, Herz J, Maeda N, Goldstein JL, Brown MS: 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 1994, 91:4431-4435. The important finding in this paper is that apoB48, a marker for chylomicrons, increases more dramatically in apoE deficiency than in LDL receptor deficiency. This means that without the LDL receptor, chylomicrons can be cleared through other receptors, most likely LRP, but the lack of apoE as a ligand cannot be easily compensated.
    • (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
  • 17
    • 0028339789 scopus 로고
    • Variable heparan sulfate proteoglycan binding of apolipoprotein E variants may modulate the expression of type III hyperlipoproteinemia
    • Ji ZS, Fazio S, Mahley RW: Variable heparan sulfate proteoglycan binding of apolipoprotein E variants may modulate the expression of type III hyperlipoproteinemia. J Biol Chem 1994, 269:13421-13428
    • (1994) J Biol Chem , vol.269 , pp. 13421-13428
    • Ji, Z.S.1    Fazio, S.2    Mahley, R.W.3
  • 18
    • 0028939751 scopus 로고
    • Apolipoprotein E isoforms and rate mutations: Parallel reduction in binding to cells and to heparin reflects severity of associated type III hyperlipoproteinemia
    • in press
    • Mann WA, Meyer N, Weber W, Meyer S, Greten H, Beisiegel U: Apolipoprotein E isoforms and rate mutations: parallel reduction in binding to cells and to heparin reflects severity of associated type III hyperlipoproteinemia. J Lipid Res 1995 (in press).
    • (1995) J Lipid Res
    • Mann, W.A.1    Meyer, N.2    Weber, W.3    Meyer, S.4    Greten, H.5    Beisiegel, U.6
  • 20
    • 0028206237 scopus 로고
    • 2-macroglobulin receptor (LRP) and mediates binding of normal very low density lipoproteins to LRP
    • 2-macroglobulin receptor (LRP) and mediates binding of normal very low density lipoproteins to LRP. J Biol Chem 1994, 269:8653-8658. By using a fragment that included residues 313-448 of human LPL, the authors demonstrated that the LRP binding site was located in the carboxyl-terminal region of the protein. Site-directed mutagenesis identified residue 407 as being important for LRP binding and residues 393 and 394 as being significant for lipoprotein binding.
    • (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
  • 22
    • 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, Hamann U, Rogne S, Myklebost O, Gausepohl H, Stanley KK: 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 1988, 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
  • 26
    • 0028355715 scopus 로고
    • The low density lipoprotein receptor-related protein mediates the cellular degradation of tissue factor pathway inhibitor
    • Warshawsky I, Broze GJ Jr, Schwartz AL: The low density lipoprotein receptor-related protein mediates the cellular degradation of tissue factor pathway inhibitor. Proc Natl Acad Sci USA 1994, 91:6664-6668.
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 6664-6668
    • Warshawsky, I.1    Broze Jr., G.J.2    Schwartz, A.L.3
  • 27
    • 0026731852 scopus 로고
    • 2-macroglobulin receptor/low density lipoprotein receptor-related protein in human tissues
    • 2-macroglobulin receptor/low density lipoprotein receptor-related protein in human tissues. Cell Tissue Res 1992, 269:375-382.
    • (1992) Cell Tissue Res , vol.269 , pp. 375-382
    • Moestrup, S.K.1    Gliemann, J.2    Pallesen, G.3
  • 28
    • 0028298886 scopus 로고
    • Expression and function of the low density lipoprotein receptor-related protein (LRP) in mammalian central neurons
    • Bu G, Maksymovitch EA, Nerbonne JM, Schwartz AL: Expression and function of the low density lipoprotein receptor-related protein (LRP) in mammalian central neurons. J Biol Chem 1994, 269:18521-18528. Functional LRP has been found in cortical neurons. In addition, the expression of RAP messenger RNA was 100-fold greater than in the liver. These results suggest that the function of LRP is tightly regulated in the brain, which indicates that it has an important role in neuronal lipoprotein metabolism.
    • (1994) J Biol Chem , vol.269 , pp. 18521-18528
    • Bu, G.1    Maksymovitch, E.A.2    Nerbonne, J.M.3    Schwartz, A.L.4
  • 29
    • 0028410543 scopus 로고
    • The apolipoprotein E connection
    • Utermann G: The apolipoprotein E connection. Curr Biol 1994, 4:362-365.
    • (1994) Curr Biol , vol.4 , pp. 362-365
    • Utermann, G.1
  • 31
    • 0028210044 scopus 로고
    • 2-macroglobulin receptor/low density lipoprotein receptor-related protein and scavenger receptor in human atherosclerotic lesions
    • 2-macroglobulin receptor/low density lipoprotein receptor-related protein and scavenger receptor in human atherosclerotic lesions. J Clin Invest 1994, 93.2014-2021. The first demonstration of the possible importance of LRP in atherogenesis. Like the scavenger receptor, LRP might contribute significantly to the development of lesions. In particular, it was shown that smooth muscle cells express LRP, which might be responsible for their transformation into foam cells.
    • (1994) J Clin Invest , vol.93 , pp. 2014-2021
    • Luoma, J.1    Hiltunen, T.2    Sarkioja, T.3    Moestrup, S.K.4    Gliemann, J.5    Kodama, T.6    Nikkari, T.7    Yla-Herttuala, S.8
  • 32
    • 0027935931 scopus 로고
    • Expression of LDL receptor-related protein/alpha2-macroglobulin receptor in human normal and atherosclerotic arteries
    • Lupu F, Heim D, Bachman F, Kruithof EKO: Expression of LDL receptor-related protein/alpha2-macroglobulin receptor in human normal and atherosclerotic arteries. Arterioscler Thromb 1994, 14:1438-1444. The authors confirmed the results of Luoma et al. [31**]. In addition, they found LRP messenger RNA in endothelial cells and located a high expression of LRP in the cap of the necrotic core, which was particular to macrophages.
    • (1994) Arterioscler Thromb , vol.14 , pp. 1438-1444
    • Lupu, F.1    Heim, D.2    Bachman, F.3    Kruithof, E.K.O.4
  • 33
    • 0028286829 scopus 로고
    • Human very-low-density lipoprotein receptor complentary DNA and deduced amino acid sequence and localization of its gene (VLDLR) to chromosome band 9p24 by fluorescence in situ hybridization
    • Oka K, Tzung KW, Sullivan M, Lindsay E, Baldini A, Chan L: Human very-low-density lipoprotein receptor complentary DNA and deduced amino acid sequence and localization of its gene (VLDLR) to chromosome band 9p24 by fluorescence in situ hybridization. Genomics 1994, 20:298-300.
    • (1994) Genomics , vol.20 , pp. 298-300
    • Oka, K.1    Tzung, K.W.2    Sullivan, M.3    Lindsay, E.4    Baldini, A.5    Chan, L.6
  • 34
    • 0028232714 scopus 로고
    • Cloning of a complementary deaoxyribonucleic acid encoding the murine homolog of the very low density lipoprotein/apolipoprotein E receptor: Expression pattern and assignment of the gene to mouse chromosome 19
    • Gafvels ME, Paavola LC, Boyd CO, Nolan PM, Wittmaack F, Chawla A, Lazar MA, Bucan M, Angelin B, Strauss JF: Cloning of a complementary deaoxyribonucleic acid encoding the murine homolog of the very low density lipoprotein/apolipoprotein E receptor: expression pattern and assignment of the gene to mouse chromosome 19. Endocrinology 1994, 135:387-394.
    • (1994) Endocrinology , vol.135 , pp. 387-394
    • Gafvels, M.E.1    Paavola, L.C.2    Boyd, C.O.3    Nolan, P.M.4    Wittmaack, F.5    Chawla, A.6    Lazar, M.A.7    Bucan, M.8    Angelin, B.9    Strauss, J.F.10
  • 35
    • 0028037117 scopus 로고
    • Regulation of the very low density lipoprotein receptor by thyroid hormone in rat skeletal muscle
    • Jokinen EV, Landschulz KT, Wyne KL, Ho YK, Frykman PK, Hobbs HH: Regulation of the very low density lipoprotein receptor by thyroid hormone in rat skeletal muscle. J Biol Chem 1994, 269:26411-26418.
    • (1994) J Biol Chem , vol.269 , pp. 26411-26418
    • Jokinen, E.V.1    Landschulz, K.T.2    Wyne, K.L.3    Ho, Y.K.4    Frykman, P.K.5    Hobbs, H.H.6
  • 36
    • 0026442201 scopus 로고
    • Lipoprotein lipase enhances binding of lipoproteins to heparan sulfate on cell surfaces and extracellular matrix
    • Eisenberg S, Sehayek E, Olivecrona T, Vlodavsky I: Lipoprotein lipase enhances binding of lipoproteins to heparan sulfate on cell surfaces and extracellular matrix. J Clin Invest 1992, 90:2013-2021.
    • (1992) J Clin Invest , vol.90 , pp. 2013-2021
    • Eisenberg, S.1    Sehayek, E.2    Olivecrona, T.3    Vlodavsky, I.4
  • 37
    • 0028118615 scopus 로고
    • The somatic cell-specific low density lipoprotein receptor-related protein of the chicken
    • Nimpf J Stifani S, Bilous PT, Schneider WJ: The somatic cell-specific low density lipoprotein receptor-related protein of the chicken. J Biol Chem 1994, 269:212-219. In the chicken, both the LDL receptor and LRP occur in two distinct forms that are different in somatic tissues and in growing follicles. The 600 kDa somatic LRP has an overall identity of 83% with human LRP. The second avian LRP is detected as a 380kDa vitellogenin-binding protein in the growing follicle. The chicken model indicates that the LRP genes have emerged from an ancestor that was designed to ensure an important event in reproduction.
    • (1994) J Biol Chem , vol.269 , pp. 212-219
    • Nimpf, J.1    Stifani, S.2    Bilous, P.T.3    Schneider, W.J.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.