메뉴 건너뛰기




Volumn 19, Issue 3, 2008, Pages 307-313

Heparan sulfate proteoglycans and triglyceride-rich lipoprotein metabolism

Author keywords

Cholesterol; Lipoprotein clearance; Proteoglycans; Sulfation; Triglycerides

Indexed keywords

APOLIPOPROTEIN; CHOLESTEROL; LIPOPROTEIN; LOW DENSITY LIPOPROTEIN RECEPTOR; PROTEOHEPARAN SULFATE; TRIACYLGLYCEROL; TRIACYLGLYCEROL LIPASE;

EID: 43249093217     PISSN: 09579672     EISSN: None     Source Type: Journal    
DOI: 10.1097/MOL.0b013e3282feec2d     Document Type: Review
Times cited : (43)

References (70)
  • 1
    • 34447511196 scopus 로고    scopus 로고
    • Nonfasting triglycerides and risk of myocardial infarction, ischemic heart disease, and death in men and women
    • Nordestgaard BG, Benn M, Schnohr P, Tybjaerg-Hansen A. Nonfasting triglycerides and risk of myocardial infarction, ischemic heart disease, and death in men and women. JAMA 2007; 298:299-308.
    • (2007) JAMA , vol.298 , pp. 299-308
    • Nordestgaard, B.G.1    Benn, M.2    Schnohr, P.3    Tybjaerg-Hansen, A.4
  • 2
    • 34447520136 scopus 로고    scopus 로고
    • Fasting compared with nonfasting triglycerides and risk of cardiovascular events in women
    • Bansal S, Buring JE, Rifai N, et al. Fasting compared with nonfasting triglycerides and risk of cardiovascular events in women. JAMA 2007; 298:309-316.
    • (2007) JAMA , vol.298 , pp. 309-316
    • Bansal, S.1    Buring, J.E.2    Rifai, N.3
  • 3
    • 1042268030 scopus 로고    scopus 로고
    • Hepatic catabolism of remnant lipoproteins: Where the action is
    • Havel RJ, Hamilton RL. Hepatic catabolism of remnant lipoproteins: where the action is. Arterioscler Thromb Vasc Biol 2004; 24:213-215.
    • (2004) Arterioscler Thromb Vasc Biol , vol.24 , pp. 213-215
    • Havel, R.J.1    Hamilton, R.L.2
  • 4
    • 0024368285 scopus 로고
    • The asialoglycoprotein receptor: Properties and modulation by ligand
    • Weiss P, Ashwell G. The asialoglycoprotein receptor: properties and modulation by ligand. Prog Clin Biol Res 1989; 300:169-184.
    • (1989) Prog Clin Biol Res , vol.300 , pp. 169-184
    • Weiss, P.1    Ashwell, G.2
  • 5
    • 0035229308 scopus 로고    scopus 로고
    • The man/GalNAc-4-SO4-receptor has multiple specificities and functions
    • Woodworth A, Baenziger JU. The man/GalNAc-4-SO4-receptor has multiple specificities and functions. Results Probl Cell Differ 2001; 33:123-138.
    • (2001) Results Probl Cell Differ , vol.33 , pp. 123-138
    • Woodworth, A.1    Baenziger, J.U.2
  • 6
    • 0037136420 scopus 로고    scopus 로고
    • Glycans as endocytosis signals: The cases of the asialoglycoprotein and hyaluronan/chondroitin sulfate receptors
    • Weigel PH, Yik JHN. Glycans as endocytosis signals: the cases of the asialoglycoprotein and hyaluronan/chondroitin sulfate receptors. Biochim Biophys Acta Gen Subj 2002; 1572:341-363.
    • (2002) Biochim Biophys Acta Gen Subj , vol.1572 , pp. 341-363
    • Weigel, P.H.1    Yik, J.H.N.2
  • 7
    • 0019473234 scopus 로고
    • Regulation of plasma cholesterol by lipoprotein receptors
    • Brown MS, Kovanen PT, Goldstein JL. Regulation of plasma cholesterol by lipoprotein receptors. Science 1981; 212:628-635.
    • (1981) Science , vol.212 , pp. 628-635
    • Brown, M.S.1    Kovanen, P.T.2    Goldstein, J.L.3
  • 8
    • 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
  • 9
    • 0034836428 scopus 로고    scopus 로고
    • LRP: A multifunctional scavenger and signaling receptor
    • Herz J, Strickland DK. LRP: a multifunctional scavenger and signaling receptor. J Clin Invest 2001; 108:779-784.
    • (2001) J Clin Invest , vol.108 , pp. 779-784
    • Herz, J.1    Strickland, D.K.2
  • 11
    • 0032004972 scopus 로고    scopus 로고
    • Inducible inactivation of hepatic LRP gene by cre-mediated recombination confirms role of LRP in clearance of chylomicron remnants
    • Rohlmann A, Gotthardt M, Hammer RE, Herz J. Inducible inactivation of hepatic LRP gene by cre-mediated recombination confirms role of LRP in clearance of chylomicron remnants. J Clin Invest 1998; 101:689-695.
    • (1998) J Clin Invest , vol.101 , pp. 689-695
    • Rohlmann, A.1    Gotthardt, M.2    Hammer, R.E.3    Herz, J.4
  • 12
    • 0037422571 scopus 로고    scopus 로고
    • Low-density lipoprotein receptor-related protein 5 (LRP5) is essential for normal cholesterol metabolism and glucose-induced insulin secretion
    • Fujino T, Asaba H, Kang MJ, et al. Low-density lipoprotein receptor-related protein 5 (LRP5) is essential for normal cholesterol metabolism and glucose-induced insulin secretion. Proc Natl Acad Sci U S A 2003; 100:229-234.
    • (2003) Proc Natl Acad Sci U S A , vol.100 , pp. 229-234
    • Fujino, T.1    Asaba, H.2    Kang, M.J.3
  • 13
    • 0030775796 scopus 로고    scopus 로고
    • Cell-surface heparan sulfate proteoglycans: Dynamic molecules mediating ligand catabolism
    • Williams KJ, Fuki IV. Cell-surface heparan sulfate proteoglycans: dynamic molecules mediating ligand catabolism. Curr Opin Lipidol 1997; 8:253-262.
    • (1997) Curr Opin Lipidol , vol.8 , pp. 253-262
    • Williams, K.J.1    Fuki, I.V.2
  • 14
    • 0032895028 scopus 로고    scopus 로고
    • Remnant lipoprotein metabolism: Key pathways involving cell-surface heparan sulfate proteoglycans and apolipoprotein E
    • Mahley RW, Ji ZS. Remnant lipoprotein metabolism: key pathways involving cell-surface heparan sulfate proteoglycans and apolipoprotein E. J Lipid Res 1999; 40:1-16.
    • (1999) J Lipid Res , vol.40 , pp. 1-16
    • Mahley, R.W.1    Ji, Z.S.2
  • 15
    • 0028913217 scopus 로고
    • Intravenous heparinase inhibits remnant lipoprotein clearance from the plasma and uptake by the liver: In vivo role of heparan sulfate proteoglycans
    • Ji ZS, Sanan DA, Mahley RW. Intravenous heparinase inhibits remnant lipoprotein clearance from the plasma and uptake by the liver: in vivo role of heparan sulfate proteoglycans. J Lipid Res 1995; 36:583-592.
    • (1995) J Lipid Res , vol.36 , pp. 583-592
    • Ji, Z.S.1    Sanan, D.A.2    Mahley, R.W.3
  • 16
    • 33846012847 scopus 로고    scopus 로고
    • MacArthur JM, Bishop JR, Wang L, et al. Liver heparan sulfate proteoglycans mediate clearance of triglyceride-rich lipoproteins independently of LDL receptor family members. J Clin Invest 2007; 117:153-164. This paper provides the first genetic evidence showing that heparan sulfate proteoglycans facilitate clearance of hepatic and dietary triglycerides in the liver and that in the absence of LDL receptors they can aid in clearance of cholesterol-rich particles. Moreover, the authors showed that altering endothelial and leukocyte heparan sulfate has no effect on plasma triglycerides.
    • MacArthur JM, Bishop JR, Wang L, et al. Liver heparan sulfate proteoglycans mediate clearance of triglyceride-rich lipoproteins independently of LDL receptor family members. J Clin Invest 2007; 117:153-164. This paper provides the first genetic evidence showing that heparan sulfate proteoglycans facilitate clearance of hepatic and dietary triglycerides in the liver and that in the absence of LDL receptors they can aid in clearance of cholesterol-rich particles. Moreover, the authors showed that altering endothelial and leukocyte heparan sulfate has no effect on plasma triglycerides.
  • 17
    • 33846007667 scopus 로고    scopus 로고
    • Atherogenic remnant lipoproteins: Role for proteoglycans in trapping, transferring, and internalizing
    • Mahley RW, Huang Y. Atherogenic remnant lipoproteins: role for proteoglycans in trapping, transferring, and internalizing. J Clin Invest 2007; 117:94-98.
    • (2007) J Clin Invest , vol.117 , pp. 94-98
    • Mahley, R.W.1    Huang, Y.2
  • 18
    • 34247373762 scopus 로고    scopus 로고
    • Liver heparan sulfate proteoglycans: Old molecules provide new insights on lipoprotein metabolism
    • Cortes V, Rigotti A. Liver heparan sulfate proteoglycans: old molecules provide new insights on lipoprotein metabolism. Hepatology 2007; 45:1078-1080.
    • (2007) Hepatology , vol.45 , pp. 1078-1080
    • Cortes, V.1    Rigotti, A.2
  • 19
    • 0034947648 scopus 로고    scopus 로고
    • Molecular diversity of heparan sulfate
    • Esko JD, Lindahl U. Molecular diversity of heparan sulfate. J Clin Invest 2001; 108:169-173.
    • (2001) J Clin Invest , vol.108 , pp. 169-173
    • Esko, J.D.1    Lindahl, U.2
  • 20
    • 0018727068 scopus 로고
    • Cell-surface heparan sulfate. Isolation and characterization of a proteoglycan from rat liver membranes
    • Oldberg Å, Kjellén L, Höö k M. Cell-surface heparan sulfate. Isolation and characterization of a proteoglycan from rat liver membranes. J Biol Chem 1979; 254:8505-8510.
    • (1979) J Biol Chem , vol.254 , pp. 8505-8510
    • Oldberg, A.1    Kjellén, L.2    Höö k, M.3
  • 21
    • 0028346379 scopus 로고
    • Liver heparan sulfate structure. A novel molecular design
    • Lyon M, Deakin JA, Gallagher JT. Liver heparan sulfate structure. A novel molecular design. J Biol Chem 1994; 269:11208-11215.
    • (1994) J Biol Chem , vol.269 , pp. 11208-11215
    • Lyon, M.1    Deakin, J.A.2    Gallagher, J.T.3
  • 22
    • 0028122383 scopus 로고
    • Amino acid determinants that drive heparan sulfate assembly in a proteoglycan
    • Zhang L, Esko JD. Amino acid determinants that drive heparan sulfate assembly in a proteoglycan. J Biol Chem 1994; 269:19295-19299.
    • (1994) J Biol Chem , vol.269 , pp. 19295-19299
    • Zhang, L.1    Esko, J.D.2
  • 23
    • 0028892362 scopus 로고
    • Repetitive Ser-Gly sequences enhance heparan sulfate assembly in proteoglycans
    • Zhang L, David G, Esko JD. Repetitive Ser-Gly sequences enhance heparan sulfate assembly in proteoglycans. J Biol Chem 1995; 270:27127-27135.
    • (1995) J Biol Chem , vol.270 , pp. 27127-27135
    • Zhang, L.1    David, G.2    Esko, J.D.3
  • 24
    • 34247610845 scopus 로고    scopus 로고
    • Bishop JR, Schuksz M, Esko JD. Heparan sulphate proteoglycans fine-tune mammalian physiology. Nature 2007; 446:1030-1037. In this review, the authors describe the various functions of heparan sulfate proteoglycans in animal cells, which includes co-receptor activation of growth factors, endocytosis, cell adhesion and motility, and barrier functions in basement membranes.
    • Bishop JR, Schuksz M, Esko JD. Heparan sulphate proteoglycans fine-tune mammalian physiology. Nature 2007; 446:1030-1037. In this review, the authors describe the various functions of heparan sulfate proteoglycans in animal cells, which includes co-receptor activation of growth factors, endocytosis, cell adhesion and motility, and barrier functions in basement membranes.
  • 25
    • 23144436642 scopus 로고    scopus 로고
    • Basement membrane proteoglycans: From cellar to ceiling
    • Iozzo RV. Basement membrane proteoglycans: from cellar to ceiling. Nat Rev Mol Cell Biol 2005; 6:646-656.
    • (2005) Nat Rev Mol Cell Biol , vol.6 , pp. 646-656
    • Iozzo, R.V.1
  • 26
    • 3943056897 scopus 로고    scopus 로고
    • Role of glycosylation in development
    • Haltiwanger RS, Lowe JB. Role of glycosylation in development. Annu Rev Biochem 2004; 73:491-537.
    • (2004) Annu Rev Biochem , vol.73 , pp. 491-537
    • Haltiwanger, R.S.1    Lowe, J.B.2
  • 27
    • 21744450786 scopus 로고    scopus 로고
    • Heparan sulphate proteoglycans: The sweet side of development
    • Hacker U, Nybakken K, Perrimon N. Heparan sulphate proteoglycans: the sweet side of development. Nat Rev Mol Cell Biol 2005; 6:530-541.
    • (2005) Nat Rev Mol Cell Biol , vol.6 , pp. 530-541
    • Hacker, U.1    Nybakken, K.2    Perrimon, N.3
  • 28
    • 33751187897 scopus 로고    scopus 로고
    • The molecular diversity of glycosaminoglycans shapes animal development
    • Bulow HE, Hobert O. The molecular diversity of glycosaminoglycans shapes animal development. Annu Rev Cell Dev Biol 2006; 22:375-407.
    • (2006) Annu Rev Cell Dev Biol , vol.22 , pp. 375-407
    • Bulow, H.E.1    Hobert, O.2
  • 29
    • 0035997376 scopus 로고    scopus 로고
    • Order out of chaos: Assembly of ligand binding sites in heparan sulfate
    • Esko JD, Selleck SB. Order out of chaos: Assembly of ligand binding sites in heparan sulfate. Annu Rev Biochem 2002; 71:435-471.
    • (2002) Annu Rev Biochem , vol.71 , pp. 435-471
    • Esko, J.D.1    Selleck, S.B.2
  • 30
    • 35848931896 scopus 로고    scopus 로고
    • Heparan sulfate proteoglycans provide a signal to Plasmodium sporozoites to stop migrating and productively invade host cells
    • Coppi A, Tewari R, Bishop JR, et al. Heparan sulfate proteoglycans provide a signal to Plasmodium sporozoites to stop migrating and productively invade host cells. Cell Host Microbe 2007; 2:316-327.
    • (2007) Cell Host Microbe , vol.2 , pp. 316-327
    • Coppi, A.1    Tewari, R.2    Bishop, J.R.3
  • 31
    • 0035914385 scopus 로고    scopus 로고
    • New insights into the heparan sulfate proteoglycan-binding activity of apolipoprotein E
    • Libeu CP, Lund-Katz S, Phillips MC, et al. New insights into the heparan sulfate proteoglycan-binding activity of apolipoprotein E. J Biol Chem 2001; 276:39138-39144.
    • (2001) J Biol Chem , vol.276 , pp. 39138-39144
    • Libeu, C.P.1    Lund-Katz, S.2    Phillips, M.C.3
  • 32
    • 11844304289 scopus 로고    scopus 로고
    • Structural characterization of human liver heparan sulfate
    • Vongchan P, Warda M, Toyoda H, et al. Structural characterization of human liver heparan sulfate. Biochim Biophys Acta 2005; 1721:1-8.
    • (2005) Biochim Biophys Acta , vol.1721 , pp. 1-8
    • Vongchan, P.1    Warda, M.2    Toyoda, H.3
  • 33
    • 0035814915 scopus 로고    scopus 로고
    • Interaction of the N-terminal domain of apolipoprotein E4with heparin
    • Dong J, Peters-Libeu CA, Weisgraber KH, et al. Interaction of the N-terminal domain of apolipoprotein E4with heparin. Biochemistry 2001; 40:2826-2834.
    • (2001) Biochemistry , vol.40 , pp. 2826-2834
    • Dong, J.1    Peters-Libeu, C.A.2    Weisgraber, K.H.3
  • 34
    • 0038690329 scopus 로고    scopus 로고
    • Characterization of the heparin binding sites in human apolipoprotein E
    • Saito H, Dhanasekaran P, Nguyen D, et al. Characterization of the heparin binding sites in human apolipoprotein E. J Biol Chem 2003; 278:14782-14787.
    • (2003) J Biol Chem , vol.278 , pp. 14782-14787
    • Saito, H.1    Dhanasekaran, P.2    Nguyen, D.3
  • 35
    • 0026584011 scopus 로고
    • The functional characteristics of a human apolipoprotein E variant (cysteine at residue 142) may explain its association with dominant expression of type III hyperlipoproteinemia
    • Horie Y, Fazio S, Westerlund JR, et al. The functional characteristics of a human apolipoprotein E variant (cysteine at residue 142) may explain its association with dominant expression of type III hyperlipoproteinemia. J Biol Chem 1992; 267:1962-1968.
    • (1992) J Biol Chem , vol.267 , pp. 1962-1968
    • Horie, Y.1    Fazio, S.2    Westerlund, J.R.3
  • 36
    • 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
  • 37
    • 0028939751 scopus 로고
    • Apolipoprotein E isoforms and rare mutations: Parallel reduction in binding to cells and to heparin reflects severity of associated type III hyperlipoproteinemia
    • Mann WA, Meyer N, Weber W, et al. Apolipoprotein E isoforms and rare mutations: parallel reduction in binding to cells and to heparin reflects severity of associated type III hyperlipoproteinemia. J Lipid Res 1995; 36:517-525.
    • (1995) J Lipid Res , vol.36 , pp. 517-525
    • Mann, W.A.1    Meyer, N.2    Weber, W.3
  • 38
    • 0028795696 scopus 로고
    • Identification and characterization of a novel apolipoprotein E variant, apolipoprotein E30 (Arg136->His): Association with mild dyslipidemia and double prebeta very low density lipoproteins
    • Minnich A, Weisgraber KH, Newhouse Y, et al. Identification and characterization of a novel apolipoprotein E variant, apolipoprotein E30 (Arg136->His): association with mild dyslipidemia and double prebeta very low density lipoproteins. J Lipid Res 1995; 36:57-66.
    • (1995) J Lipid Res , vol.36 , pp. 57-66
    • Minnich, A.1    Weisgraber, K.H.2    Newhouse, Y.3
  • 39
    • 0031594336 scopus 로고    scopus 로고
    • Apolipoprotein E2 (Arg136-> Cys) mutation in the receptor binding domain of apoE is not associated with dominant type III hyperlipoproteinemia
    • Marz W, Hoffmann MM, Scharnagl H, et al. Apolipoprotein E2 (Arg136-> Cys) mutation in the receptor binding domain of apoE is not associated with dominant type III hyperlipoproteinemia. J Lipid Res 1998; 39:658-669.
    • (1998) J Lipid Res , vol.39 , pp. 658-669
    • Marz, W.1    Hoffmann, M.M.2    Scharnagl, H.3
  • 40
    • 0032567251 scopus 로고    scopus 로고
    • The NH2-terminal region of apolipoprotein B is sufficient for lipoprotein association with glycosaminoglycans
    • Goldberg IJ, Wagner WD, Pang L, et al. The NH2-terminal region of apolipoprotein B is sufficient for lipoprotein association with glycosaminoglycans. J Biol Chem 1998; 273:35355-35361.
    • (1998) J Biol Chem , vol.273 , pp. 35355-35361
    • Goldberg, I.J.1    Wagner, W.D.2    Pang, L.3
  • 41
    • 0032526201 scopus 로고    scopus 로고
    • Identification of the principal proteoglycan-binding site in LDL: A single-point mutation in apo-B100 severely affects proteoglycan interaction without affecting LDL receptor binding
    • Borén J, Olin K, Lee I, et al. Identification of the principal proteoglycan-binding site in LDL: a single-point mutation in apo-B100 severely affects proteoglycan interaction without affecting LDL receptor binding. J Clin Invest 1998; 101:2658-2664.
    • (1998) J Clin Invest , vol.101 , pp. 2658-2664
    • Borén, J.1    Olin, K.2    Lee, I.3
  • 42
    • 0037200065 scopus 로고    scopus 로고
    • Identification of the proteoglycan binding site in apolipoprotein B48
    • Flood C, Gustafsson M, Richardson PE, et al. Identification of the proteoglycan binding site in apolipoprotein B48. J Biol Chem 2002; 277:32228-32233.
    • (2002) J Biol Chem , vol.277 , pp. 32228-32233
    • Flood, C.1    Gustafsson, M.2    Richardson, P.E.3
  • 43
    • 34248343423 scopus 로고    scopus 로고
    • Characterization of apolipoprotein A-V structure and mode of plasma triacylglycerol regulation
    • This review describes our current understanding of apoA-V structure and its role in triglyceride metabolism in the periphery. ApoA-V binds to heparan sulfate, which may faciliate the interaction of Lpl with its substrate lipoproteins
    • Wong K, Ryan RO. Characterization of apolipoprotein A-V structure and mode of plasma triacylglycerol regulation. Curr Opin Lipidol 2007; 18:319-324. This review describes our current understanding of apoA-V structure and its role in triglyceride metabolism in the periphery. ApoA-V binds to heparan sulfate, which may faciliate the interaction of Lpl with its substrate lipoproteins.
    • (2007) Curr Opin Lipidol , vol.18 , pp. 319-324
    • Wong, K.1    Ryan, R.O.2
  • 44
    • 0035292694 scopus 로고    scopus 로고
    • Lipoprotein lipase: Physiology, biochemistry, and molecular biology
    • Goldberg IJ, Merkel M. Lipoprotein lipase: physiology, biochemistry, and molecular biology. Front Biosci 2001; 6:D388-405.
    • (2001) Front Biosci , vol.6
    • Goldberg, I.J.1    Merkel, M.2
  • 45
    • 0028121995 scopus 로고
    • Oligosaccharide sequences of endothelial cell surface heparan sulfate proteoglycan with affinity for lipoprotein lipase
    • Parthasarathy N, Goldberg IJ, Sivaram P, et al. Oligosaccharide sequences of endothelial cell surface heparan sulfate proteoglycan with affinity for lipoprotein lipase. J Biol Chem 1994; 269:22391-22396.
    • (1994) J Biol Chem , vol.269 , pp. 22391-22396
    • Parthasarathy, N.1    Goldberg, I.J.2    Sivaram, P.3
  • 46
    • 33747714599 scopus 로고    scopus 로고
    • Isolation and characterization of low sulfated heparan sulfate sequences with affinity for lipoprotein lipase
    • Spillmann D, Lookene A, Olivecrona G. Isolation and characterization of low sulfated heparan sulfate sequences with affinity for lipoprotein lipase. J Biol Chem 2006; 281:23405-23413.
    • (2006) J Biol Chem , vol.281 , pp. 23405-23413
    • Spillmann, D.1    Lookene, A.2    Olivecrona, G.3
  • 47
    • 0000492939 scopus 로고
    • The role of heparin in lipoprotein metabolism
    • Anfinsen CB, Boyle E, Brown RK. The role of heparin in lipoprotein metabolism. Science 1952; 115:583-586.
    • (1952) Science , vol.115 , pp. 583-586
    • Anfinsen, C.B.1    Boyle, E.2    Brown, R.K.3
  • 48
    • 33947573537 scopus 로고    scopus 로고
    • Beigneux AP, Davies BS, Gin P, et al. Glycosylphosphatidylinositol-anchored high-density lipoprotein-binding protein 1 plays a critical role in the lipolytic processing of chylomicrons. Cell Metab 2007; 5:279-291. These authors provide genetic evidence that glycosylphosphatidylinositol-anchored high-density lipoprotein-binding protein 1 (GPIHBP1) plays a crucial role in the lipolytic processing of chylomicron by binding LPL and chylomicron substrates. The work challenges the dogma that LPL is bound predominantly to heparan sulfate proteoglycans.
    • Beigneux AP, Davies BS, Gin P, et al. Glycosylphosphatidylinositol-anchored high-density lipoprotein-binding protein 1 plays a critical role in the lipolytic processing of chylomicrons. Cell Metab 2007; 5:279-291. These authors provide genetic evidence that glycosylphosphatidylinositol-anchored high-density lipoprotein-binding protein 1 (GPIHBP1) plays a crucial role in the lipolytic processing of chylomicron by binding LPL and chylomicron substrates. The work challenges the dogma that LPL is bound predominantly to heparan sulfate proteoglycans.
  • 49
    • 34447314745 scopus 로고    scopus 로고
    • GPIHBP1: An endothelial cell molecule important for the lipolytic processing of chylomicrons
    • Young SG, Davies BS, Fong LG, et al. GPIHBP1: an endothelial cell molecule important for the lipolytic processing of chylomicrons. Curr Opin Lipidol 2007; 18:389-396.
    • (2007) Curr Opin Lipidol , vol.18 , pp. 389-396
    • Young, S.G.1    Davies, B.S.2    Fong, L.G.3
  • 52
    • 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 KJ, Fless GM, Petrie KA, et al. 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 1992; 267:13284-13292.
    • (1992) J Biol Chem , vol.267 , pp. 13284-13292
    • Williams, K.J.1    Fless, G.M.2    Petrie, K.A.3
  • 53
    • 0035937147 scopus 로고    scopus 로고
    • Multiple isozymes of heparan sulfate/heparin GlcNAc N-deacetylase/N-sulfotransferase: Structure and activity of the fourth member, NDST4
    • Aikawa J, Grobe K, Tsujimoto M, Esko JD. Multiple isozymes of heparan sulfate/heparin GlcNAc N-deacetylase/N-sulfotransferase: structure and activity of the fourth member, NDST4. J Biol Chem 2001; 276:5876-5882.
    • (2001) J Biol Chem , vol.276 , pp. 5876-5882
    • Aikawa, J.1    Grobe, K.2    Tsujimoto, M.3    Esko, J.D.4
  • 54
    • 0034059141 scopus 로고    scopus 로고
    • DNA excision in liver by an albumin-Cre transgene occurs progressively with age
    • Postic C, Magnuson MA. DNA excision in liver by an albumin-Cre transgene occurs progressively with age. Genesis 2000; 26:149-150.
    • (2000) Genesis , vol.26 , pp. 149-150
    • Postic, C.1    Magnuson, M.A.2
  • 55
    • 34547189740 scopus 로고    scopus 로고
    • Polycystic disease caused by deficiency in xylosyltransferase 2, an initiating enzyme of glycosaminoglycan biosynthesis
    • Condac E, Silasi-Mansat R, Kosanke S, et al. Polycystic disease caused by deficiency in xylosyltransferase 2, an initiating enzyme of glycosaminoglycan biosynthesis. Proc Natl Acad Sci U S A 2007; 104:9416-9421.
    • (2007) Proc Natl Acad Sci U S A , vol.104 , pp. 9416-9421
    • Condac, E.1    Silasi-Mansat, R.2    Kosanke, S.3
  • 56
    • 0030803636 scopus 로고    scopus 로고
    • The syndecan family of proteoglycans. Novel receptors mediating internalization of atherogenic lipoproteins in vitro
    • Fuki IV, Kuhn KM, Lomazov IR, et al. The syndecan family of proteoglycans. Novel receptors mediating internalization of atherogenic lipoproteins in vitro. J Clin Invest 1997; 100:1611-1622.
    • (1997) J Clin Invest , vol.100 , pp. 1611-1622
    • Fuki, I.V.1    Kuhn, K.M.2    Lomazov, I.R.3
  • 57
    • 0031967097 scopus 로고    scopus 로고
    • Chylomicron remnant uptake is regulated by the expression and function of heparan sulfate proteoglycan in hepatocytes
    • Zeng BJ, Mortimer BC, Martins IJ, et al. Chylomicron remnant uptake is regulated by the expression and function of heparan sulfate proteoglycan in hepatocytes. J Lipid Res 1998; 39:845-860.
    • (1998) J Lipid Res , vol.39 , pp. 845-860
    • Zeng, B.J.1    Mortimer, B.C.2    Martins, I.J.3
  • 58
    • 33749641662 scopus 로고    scopus 로고
    • Syndecan-1 mediates internalization of apoE-VLDL through a low density lipoprotein receptor-related protein (LRP)-independent, nonclathrin-mediated pathway
    • Wilsie LC, Gonzales AM, Orlando RA. Syndecan-1 mediates internalization of apoE-VLDL through a low density lipoprotein receptor-related protein (LRP)-independent, nonclathrin-mediated pathway. Lipids Health Dis 2006; 5:23.
    • (2006) Lipids Health Dis , vol.5 , pp. 23
    • Wilsie, L.C.1    Gonzales, A.M.2    Orlando, R.A.3
  • 59
    • 34047236123 scopus 로고    scopus 로고
    • Adenovirus-mediated hepatic syndecan-1 overexpression induces hepatocyte proliferation and hyperlipidaemia in mice
    • Cortes V, Amigo L, Donoso K, et al. Adenovirus-mediated hepatic syndecan-1 overexpression induces hepatocyte proliferation and hyperlipidaemia in mice. Liver Int 2007; 27:569-581.
    • (2007) Liver Int , vol.27 , pp. 569-581
    • Cortes, V.1    Amigo, L.2    Donoso, K.3
  • 60
    • 16244380777 scopus 로고    scopus 로고
    • Syndecans: New kids on the signaling block
    • Tkachenko E, Rhodes JM, Simons M. Syndecans: new kids on the signaling block. Circ Res 2005; 96:488-500.
    • (2005) Circ Res , vol.96 , pp. 488-500
    • Tkachenko, E.1    Rhodes, J.M.2    Simons, M.3
  • 61
    • 0026744148 scopus 로고
    • Cell surface heparan sulfate proteoglycans
    • Yanagishita M, Hascall V. Cell surface heparan sulfate proteoglycans. J Biol Chem 1992; 267:9451-9454.
    • (1992) J Biol Chem , vol.267 , pp. 9451-9454
    • Yanagishita, M.1    Hascall, V.2
  • 62
    • 0026633977 scopus 로고
    • Recycling of transferrin receptors and heparan sulfate proteoglycans in a rat parathyroid cell line
    • Takeuchi Y, Yanagishita M, Hascall VC. Recycling of transferrin receptors and heparan sulfate proteoglycans in a rat parathyroid cell line. J Biol Chem 1992; 267:14685-14690.
    • (1992) J Biol Chem , vol.267 , pp. 14685-14690
    • Takeuchi, Y.1    Yanagishita, M.2    Hascall, V.C.3
  • 64
    • 24144482654 scopus 로고    scopus 로고
    • Syndecan recycling [corrected] is controlled by syntenin-PIP2 interaction and Arf6
    • Zimmermann P, Zhang Z, Degeest G, et al. Syndecan recycling [corrected] is controlled by syntenin-PIP2 interaction and Arf6. Dev Cell 2005; 9:377-388.
    • (2005) Dev Cell , vol.9 , pp. 377-388
    • Zimmermann, P.1    Zhang, Z.2    Degeest, G.3
  • 65
    • 0034630099 scopus 로고    scopus 로고
    • Analysis of low-density lipoprotein catabolism by primary cultures of hepatic cells from normal and low-density lipoprotein receptor knockout mice
    • Truong TQ, Auger A, Denizeau F, Brissette L. Analysis of low-density lipoprotein catabolism by primary cultures of hepatic cells from normal and low-density lipoprotein receptor knockout mice. Biochim Biophys Acta 2000; 1484:307-315.
    • (2000) Biochim Biophys Acta , vol.1484 , pp. 307-315
    • Truong, T.Q.1    Auger, A.2    Denizeau, F.3    Brissette, L.4
  • 66
    • 0035006852 scopus 로고    scopus 로고
    • Low and high density lipoprotein metabolism in primary cultures of hepatic cells from normal and apolipoprotein E knockout mice
    • Auger A, Truong TQ, Rhainds D, et al. Low and high density lipoprotein metabolism in primary cultures of hepatic cells from normal and apolipoprotein E knockout mice. Eur J Biochem 2001; 268:2322-2330.
    • (2001) Eur J Biochem , vol.268 , pp. 2322-2330
    • Auger, A.1    Truong, T.Q.2    Rhainds, D.3
  • 67
    • 33947255616 scopus 로고    scopus 로고
    • Internalization and trafficking of cell surface proteoglycans and proteoglycan-binding ligands
    • This paper describes the channeling of polycationic ligands bound to cell surface proteoglycans via clathrin-independent and caveolin-independent endocytic pathways, which would distinguish uptake of lipoproteins via proteoglycans from the LDL receptor
    • Payne CK, Jones SA, Chen C, Zhuang X. Internalization and trafficking of cell surface proteoglycans and proteoglycan-binding ligands. Traffic 2007; 8:389-401. This paper describes the channeling of polycationic ligands bound to cell surface proteoglycans via clathrin-independent and caveolin-independent endocytic pathways, which would distinguish uptake of lipoproteins via proteoglycans from the LDL receptor.
    • (2007) Traffic , vol.8 , pp. 389-401
    • Payne, C.K.1    Jones, S.A.2    Chen, C.3    Zhuang, X.4
  • 68
    • 0028347117 scopus 로고
    • Secretion-recapture process of apolipoprotein E in hepatic uptake of chylomicron remnants in transgenic mice
    • Shimano H, Namba Y, Ohsuga J, et al. Secretion-recapture process of apolipoprotein E in hepatic uptake of chylomicron remnants in transgenic mice. J Clin Invest 1994; 93:2215-2223.
    • (1994) J Clin Invest , vol.93 , pp. 2215-2223
    • Shimano, H.1    Namba, Y.2    Ohsuga, J.3
  • 69
    • 34247471569 scopus 로고    scopus 로고
    • Hypertriglyceridemia: Its etiology, effects and treatment
    • Yuan G, Al-Shali KZ, Hegele RA. Hypertriglyceridemia: its etiology, effects and treatment. CMAJ 2007; 176:1113-1120.
    • (2007) CMAJ , vol.176 , pp. 1113-1120
    • Yuan, G.1    Al-Shali, K.Z.2    Hegele, R.A.3
  • 70
    • 34648851432 scopus 로고    scopus 로고
    • Fatty acid-induced atherogenic changes in extracellular matrix proteoglycans
    • The authors summarize data showing that nonesterified fatty acids change the expression and properties of the extracellular matrix proteoglycans of arterial and hepatic cells, which affects the affinity for VLDL
    • Rodriguez-Lee M, Bondjers G, Camejo G. Fatty acid-induced atherogenic changes in extracellular matrix proteoglycans. Curr Opin Lipidol 2007; 18:546-553. The authors summarize data showing that nonesterified fatty acids change the expression and properties of the extracellular matrix proteoglycans of arterial and hepatic cells, which affects the affinity for VLDL.
    • (2007) Curr Opin Lipidol , vol.18 , pp. 546-553
    • Rodriguez-Lee, M.1    Bondjers, G.2    Camejo, G.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.