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Volumn 53, Issue 2, 2014, Pages 361-375

Acrolein modification impairs key functional features of rat apolipoprotein E: Identification of modified sites by mass spectrometry

Author keywords

[No Author keywords available]

Indexed keywords

APOLIPOPROTEIN E (APOE); ATHEROSCLEROTIC LESIONS; ENVIRONMENTAL TOBACCO SMOKES; FLIGHT MASS SPECTROMETRY; FUNCTIONAL INTEGRITIES; LOW DENSITY LIPOPROTEINS; MATRIX ASSISTED LASER DESORPTION; OXIDATIVE MODIFICATION;

EID: 84892695616     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi401404u     Document Type: Article
Times cited : (24)

References (84)
  • 1
    • 66349085616 scopus 로고    scopus 로고
    • Apolipoprotein E: Structure determines function, from atherosclerosis to Alzheimer's disease to AIDS
    • Mahley, R. W., Weisgraber, K. H., and Huang, Y. (2009) Apolipoprotein E: Structure determines function, from atherosclerosis to Alzheimer's disease to AIDS J. Lipid. Res. 50 (Suppl) S183-188
    • (2009) J. Lipid. Res. , vol.50 , Issue.SUPPL. , pp. 183-188
    • Mahley, R.W.1    Weisgraber, K.H.2    Huang, Y.3
  • 2
    • 78650686441 scopus 로고    scopus 로고
    • Apolipoprotein E: From lipid transport to neurobiology
    • Hauser, P. S., Narayanaswami, V., and Ryan, R. O. (2010) Apolipoprotein E: From lipid transport to neurobiology Prog. Lipid Res. 50, 62-74
    • (2010) Prog. Lipid Res. , vol.50 , pp. 62-74
    • Hauser, P.S.1    Narayanaswami, V.2    Ryan, R.O.3
  • 5
    • 0028303072 scopus 로고
    • Apolipoprotein E: Structure-function relationships
    • Weisgraber, K. H. (1994) Apolipoprotein E: Structure-function relationships Adv. Protein Chem. 45, 249-302
    • (1994) Adv. Protein Chem. , vol.45 , pp. 249-302
    • Weisgraber, K.H.1
  • 6
    • 0035170229 scopus 로고    scopus 로고
    • High density lipoproteins and arteriosclerosis. Role of cholesterol efflux and reverse cholesterol transport
    • von Eckardstein, A., Nofer, J. R., and Assmann, G. (2001) High density lipoproteins and arteriosclerosis. Role of cholesterol efflux and reverse cholesterol transport Arterioscler. Thromb. Vasc. Biol. 21, 13-27
    • (2001) Arterioscler. Thromb. Vasc. Biol. , vol.21 , pp. 13-27
    • Von Eckardstein, A.1    Nofer, J.R.2    Assmann, G.3
  • 8
    • 0026592806 scopus 로고
    • Spontaneous hypercholesterolemia and arterial lesions in mice lacking apolipoprotein e
    • Zhang, S. H., Reddick, R. L., Piedrahita, J. A., and Maeda, N. (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
  • 10
    • 0019820184 scopus 로고
    • Type III hyperlipoproteinemia associated with apolipoprotein e deficiency
    • Ghiselli, G., Schaefer, E. J., Gascon, P., and Breser, H. B., Jr. (1981) Type III hyperlipoproteinemia associated with apolipoprotein E deficiency Science 214, 1239-1241
    • (1981) Science , vol.214 , pp. 1239-1241
    • Ghiselli, G.1    Schaefer, E.J.2    Gascon, P.3    Breser Jr., H.B.4
  • 12
    • 0024546356 scopus 로고
    • Development of coronary heart disease in familial hypercholesterolemia
    • Mabuchi, H., Koizumi, J., Shimizu, M., and Takeda, R. (1989) Development of coronary heart disease in familial hypercholesterolemia Circulation 79, 225-232
    • (1989) Circulation , vol.79 , pp. 225-232
    • Mabuchi, H.1    Koizumi, J.2    Shimizu, M.3    Takeda, R.4
  • 14
    • 77955615512 scopus 로고    scopus 로고
    • Oxidative stress and endothelial dysfunction: Say no to cigarette smoking!
    • Grassi, D., Desideri, G., Ferri, L., Aggio, A., Tiberti, S., and Ferri, C. (2010) Oxidative stress and endothelial dysfunction: Say no to cigarette smoking! Curr. Pharm. Des. 16, 2539-2550
    • (2010) Curr. Pharm. Des. , vol.16 , pp. 2539-2550
    • Grassi, D.1    Desideri, G.2    Ferri, L.3    Aggio, A.4    Tiberti, S.5    Ferri, C.6
  • 15
    • 66349100479 scopus 로고    scopus 로고
    • The LDL modification hypothesis of atherogenesis: An update
    • Steinberg, D. (2009) The LDL modification hypothesis of atherogenesis: an update J. Lipid. Res. 50 (Suppl) S376-381
    • (2009) J. Lipid. Res. , vol.50 , Issue.SUPPL. , pp. 376-381
    • Steinberg, D.1
  • 16
    • 43049168951 scopus 로고    scopus 로고
    • In vivo markers of oxidative stress and therapeutic interventions
    • Tsimikas, S. (2008) In vivo markers of oxidative stress and therapeutic interventions Am. J. Cardiol. 101, 34D-42D
    • (2008) Am. J. Cardiol. , vol.101
    • Tsimikas, S.1
  • 17
    • 33748563198 scopus 로고    scopus 로고
    • Clinical applications of circulating oxidized low-density lipoprotein biomarkers in cardiovascular disease
    • Fraley, A. E. and Tsimikas, S. (2006) Clinical applications of circulating oxidized low-density lipoprotein biomarkers in cardiovascular disease Curr. Opin. Lipidol. 17, 502-509
    • (2006) Curr. Opin. Lipidol. , vol.17 , pp. 502-509
    • Fraley, A.E.1    Tsimikas, S.2
  • 18
    • 0020972414 scopus 로고
    • Lipoprotein metabolism in the macrophage: Implications for cholesterol deposition in atherosclerosis
    • Brown, M. S. and Goldstein, J. L. (1983) Lipoprotein metabolism in the macrophage: Implications for cholesterol deposition in atherosclerosis Annu. Rev. Biochem. 52, 223-261
    • (1983) Annu. Rev. Biochem. , vol.52 , pp. 223-261
    • Brown, M.S.1    Goldstein, J.L.2
  • 20
    • 0025838106 scopus 로고
    • Characterization of a more electronegatively charged LDL subfraction by ion exchange HPLC
    • Cazzolato, G., Avogaro, P., and Bittolo-Bon, G. (1991) Characterization of a more electronegatively charged LDL subfraction by ion exchange HPLC Free Radical Biol. Med. 11, 247-253
    • (1991) Free Radical Biol. Med. , vol.11 , pp. 247-253
    • Cazzolato, G.1    Avogaro, P.2    Bittolo-Bon, G.3
  • 21
    • 17944387960 scopus 로고    scopus 로고
    • Structural identification by mass spectrometry of oxidized phospholipids in minimally oxidized low density lipoprotein that induce monocyte/endothelial interactions and evidence for their presence in vivo
    • Watson, A. D., Leitinger, N., Navab, M., Faull, K. F., Horkko, S., Witztum, J. L., Palinski, W., Schwenke, D., Salomon, R. G., Sha, W., Subbanagounder, G., Fogelman, A. M., and Berliner, J. A. (1997) Structural identification by mass spectrometry of oxidized phospholipids in minimally oxidized low density lipoprotein that induce monocyte/endothelial interactions and evidence for their presence in vivo J. Biol. Chem. 272, 13597-13607
    • (1997) J. Biol. Chem. , vol.272 , pp. 13597-13607
    • Watson, A.D.1    Leitinger, N.2    Navab, M.3    Faull, K.F.4    Horkko, S.5    Witztum, J.L.6    Palinski, W.7    Schwenke, D.8    Salomon, R.G.9    Sha, W.10    Subbanagounder, G.11    Fogelman, A.M.12    Berliner, J.A.13
  • 22
    • 0034659139 scopus 로고    scopus 로고
    • Bioactive products of phospholipid oxidation: Isolation, identification, measurement and activities
    • Subbanagounder, G., Watson, A. D., and Berliner, J. A. (2000) Bioactive products of phospholipid oxidation: isolation, identification, measurement and activities Free Radical Biol. Med. 28, 1751-1761
    • (2000) Free Radical Biol. Med. , vol.28 , pp. 1751-1761
    • Subbanagounder, G.1    Watson, A.D.2    Berliner, J.A.3
  • 23
    • 0033516656 scopus 로고    scopus 로고
    • Oxidative cross-linking of ApoB100 and hemoglobin results in low density lipoprotein modification in blood. Relevance to atherogenesis caused by hemodialysis
    • Ziouzenkova, O., Asatryan, L., Akmal, M., Tetta, C., Wratten, M. L., Loseto-Wich, G., Jurgens, G., Heinecke, J., and Sevanian, A. (1999) Oxidative cross-linking of ApoB100 and hemoglobin results in low density lipoprotein modification in blood. Relevance to atherogenesis caused by hemodialysis J. Biol. Chem. 274, 18916-18924
    • (1999) J. Biol. Chem. , vol.274 , pp. 18916-18924
    • Ziouzenkova, O.1    Asatryan, L.2    Akmal, M.3    Tetta, C.4    Wratten, M.L.5    Loseto-Wich, G.6    Jurgens, G.7    Heinecke, J.8    Sevanian, A.9
  • 24
    • 0024603895 scopus 로고
    • Beyond cholesterol. Modifications of low-density lipoprotein that increase its atherogenicity
    • Steinberg, D., Parthasarathy, S., Carew, T. E., Khoo, J. C., and Witztum, J. L. (1989) Beyond cholesterol. Modifications of low-density lipoprotein that increase its atherogenicity N. Engl. J. Med. 320, 915-924
    • (1989) N. Engl. J. Med. , vol.320 , pp. 915-924
    • Steinberg, D.1    Parthasarathy, S.2    Carew, T.E.3    Khoo, J.C.4    Witztum, J.L.5
  • 26
    • 0023192020 scopus 로고
    • Oxidatively modified low density lipoproteins: A potential role in recruitment and retention of monocyte/macrophages during atherogenesis
    • Quinn, M. T., Parthasarathy, S., Fong, L. G., and Steinberg, D. (1987) Oxidatively modified low density lipoproteins: a potential role in recruitment and retention of monocyte/macrophages during atherogenesis Proc. Natl. Acad. Sci. U. S. A. 84, 2995-2998
    • (1987) Proc. Natl. Acad. Sci. U. S. A. , vol.84 , pp. 2995-2998
    • Quinn, M.T.1    Parthasarathy, S.2    Fong, L.G.3    Steinberg, D.4
  • 27
    • 38949113159 scopus 로고    scopus 로고
    • Acrolein: Sources, metabolism, and biomolecular interactions relevant to human health and disease
    • Stevens, J. F. and Maier, C. S. (2008) Acrolein: Sources, metabolism, and biomolecular interactions relevant to human health and disease Mol. Nutr. Food Res. 52, 7-25
    • (2008) Mol. Nutr. Food Res. , vol.52 , pp. 7-25
    • Stevens, J.F.1    Maier, C.S.2
  • 29
    • 84870295540 scopus 로고    scopus 로고
    • Biochemical and biophysical characterization of recombinant rat apolipoprotein E: Similarities to human apolipoprotein E3
    • Tran, T. N., Kim, S. H., Gallo, C., Amaya, M., Kyees, J., and Narayanaswami, V. (2012) Biochemical and biophysical characterization of recombinant rat apolipoprotein E: Similarities to human apolipoprotein E3 Arch. Biochem. Biophys. 529, 18-25
    • (2012) Arch. Biochem. Biophys. , vol.529 , pp. 18-25
    • Tran, T.N.1    Kim, S.H.2    Gallo, C.3    Amaya, M.4    Kyees, J.5    Narayanaswami, V.6
  • 30
    • 0032568935 scopus 로고    scopus 로고
    • Acrolein is a product of lipid peroxidation reaction. Formation of free acrolein and its conjugate with lysine residues in oxidized low density lipoproteins
    • Uchida, K., Kanematsu, M., Morimitsu, Y., Osawa, T., Noguchi, N., and Niki, E. (1998) Acrolein is a product of lipid peroxidation reaction. Formation of free acrolein and its conjugate with lysine residues in oxidized low density lipoproteins J. Biol. Chem. 273, 16058-16066
    • (1998) J. Biol. Chem. , vol.273 , pp. 16058-16066
    • Uchida, K.1    Kanematsu, M.2    Morimitsu, Y.3    Osawa, T.4    Noguchi, N.5    Niki, E.6
  • 31
    • 0034672122 scopus 로고    scopus 로고
    • Estimation of protein secondary structure from circular dichroism spectra: Inclusion of denatured proteins with native proteins in the analysis
    • Sreerama, N., Venyaminov, S. Y., and Woody, R. W. (2000) Estimation of protein secondary structure from circular dichroism spectra: Inclusion of denatured proteins with native proteins in the analysis Anal. Biochem. 287, 243-251
    • (2000) Anal. Biochem. , vol.287 , pp. 243-251
    • Sreerama, N.1    Venyaminov, S.Y.2    Woody, R.W.3
  • 32
    • 0034718456 scopus 로고    scopus 로고
    • Differences in stability among the human apolipoprotein e isoforms determined by the amino-terminal domain
    • Morrow, J. A., Segall, M. L., Lund-Katz, S., Phillips, M. C., Knapp, M., Rupp, B., and Weisgraber, K. H. (2000) Differences in stability among the human apolipoprotein E isoforms determined by the amino-terminal domain Biochemistry 39, 11657-11666
    • (2000) Biochemistry , vol.39 , pp. 11657-11666
    • Morrow, J.A.1    Segall, M.L.2    Lund-Katz, S.3    Phillips, M.C.4    Knapp, M.5    Rupp, B.6    Weisgraber, K.H.7
  • 33
    • 77749255554 scopus 로고    scopus 로고
    • Pyrene fluorescence analysis offers new insights into the conformation of the lipoprotein-binding domain of human apolipoprotein e
    • Patel, A. B., Khumsupan, P., and Narayanaswami, V. (2010) Pyrene fluorescence analysis offers new insights into the conformation of the lipoprotein-binding domain of human apolipoprotein E Biochemistry 49, 1766-1775
    • (2010) Biochemistry , vol.49 , pp. 1766-1775
    • Patel, A.B.1    Khumsupan, P.2    Narayanaswami, V.3
  • 34
    • 0023900109 scopus 로고
    • Human apolipoprotein E3 in aqueous solution. I. Evidence for two structural domains
    • Wetterau, J. R., Aggerbeck, L. P., Rall, S. C., Jr., and Weisgraber, K. H. (1988) Human apolipoprotein E3 in aqueous solution. I. Evidence for two structural domains J. Biol. Chem. 263, 6240-6248
    • (1988) J. Biol. Chem. , vol.263 , pp. 6240-6248
    • Wetterau, J.R.1    Aggerbeck, L.P.2    Rall Jr., S.C.3    Weisgraber, K.H.4
  • 35
    • 0018798895 scopus 로고
    • Determining globular protein stability: Guanidine hydrochloride denaturation of myoglobin
    • Pace, C. N. and Vanderburg, K. E. (1979) Determining globular protein stability: Guanidine hydrochloride denaturation of myoglobin Biochemistry 18, 288-292
    • (1979) Biochemistry , vol.18 , pp. 288-292
    • Pace, C.N.1    Vanderburg, K.E.2
  • 36
    • 20544455385 scopus 로고    scopus 로고
    • Role of buried polar residues in helix bundle stability and lipid binding of apolipophorin III: Destabilization by threonine 31
    • Weers, P. M., Abdullahi, W. E., Cabrera, J. M., and Hsu, T. C. (2005) Role of buried polar residues in helix bundle stability and lipid binding of apolipophorin III: destabilization by threonine 31 Biochemistry 44, 8810-8816
    • (2005) Biochemistry , vol.44 , pp. 8810-8816
    • Weers, P.M.1    Abdullahi, W.E.2    Cabrera, J.M.3    Hsu, T.C.4
  • 37
    • 0034721777 scopus 로고    scopus 로고
    • The lipid-associated conformation of the low density lipoprotein receptor binding domain of human apolipoprotein e
    • Fisher, C. A., Narayanaswami, V., and Ryan, R. O. (2000) The lipid-associated conformation of the low density lipoprotein receptor binding domain of human apolipoprotein E J. Biol. Chem. 275, 33601-33606
    • (2000) J. Biol. Chem. , vol.275 , pp. 33601-33606
    • Fisher, C.A.1    Narayanaswami, V.2    Ryan, R.O.3
  • 38
    • 0035851137 scopus 로고    scopus 로고
    • Lipid association-induced N- and C-terminal domain reorganization in human apolipoprotein E3
    • Narayanaswami, V., Szeto, S. S., and Ryan, R. O. (2001) Lipid association-induced N- and C-terminal domain reorganization in human apolipoprotein E3 J. Biol. Chem. 276, 37853-37860
    • (2001) J. Biol. Chem. , vol.276 , pp. 37853-37860
    • Narayanaswami, V.1    Szeto, S.S.2    Ryan, R.O.3
  • 40
    • 0942268917 scopus 로고    scopus 로고
    • A two-module region of the low-density lipoprotein receptor sufficient for formation of complexes with apolipoprotein e ligands
    • Fisher, C., Abdul-Aziz, D., and Blacklow, S. C. (2004) A two-module region of the low-density lipoprotein receptor sufficient for formation of complexes with apolipoprotein E ligands Biochemistry 43, 1037-1044
    • (2004) Biochemistry , vol.43 , pp. 1037-1044
    • Fisher, C.1    Abdul-Aziz, D.2    Blacklow, S.C.3
  • 41
    • 0038497959 scopus 로고    scopus 로고
    • Structure-guided protein engineering modulates helix bundle exchangeable apolipoprotein properties
    • Kiss, R. S., Weers, P. M., Narayanaswami, V., Cohen, J., Kay, C. M., and Ryan, R. O. (2003) Structure-guided protein engineering modulates helix bundle exchangeable apolipoprotein properties J. Biol. Chem. 278, 21952-21959
    • (2003) J. Biol. Chem. , vol.278 , pp. 21952-21959
    • Kiss, R.S.1    Weers, P.M.2    Narayanaswami, V.3    Cohen, J.4    Kay, C.M.5    Ryan, R.O.6
  • 42
    • 34447542267 scopus 로고    scopus 로고
    • Modification by acrolein, a component of tobacco smoke and age-related oxidative stress, mediates functional impairment of human apolipoprotein e
    • Tamamizu-Kato, S., Wong, J. Y., Jairam, V., Uchida, K., Raussens, V., Kato, H., Ruysschaert, J. M., and Narayanaswami, V. (2007) Modification by acrolein, a component of tobacco smoke and age-related oxidative stress, mediates functional impairment of human apolipoprotein E Biochemistry 46, 8392-8400
    • (2007) Biochemistry , vol.46 , pp. 8392-8400
    • Tamamizu-Kato, S.1    Wong, J.Y.2    Jairam, V.3    Uchida, K.4    Raussens, V.5    Kato, H.6    Ruysschaert, J.M.7    Narayanaswami, V.8
  • 43
    • 33947205478 scopus 로고    scopus 로고
    • The C-terminal lipid-binding domain of apolipoprotein e is a highly efficient mediator of ABCA1-dependent cholesterol efflux that promotes the assembly of high-density lipoproteins
    • Vedhachalam, C., Narayanaswami, V., Neto, N., Forte, T. M., Phillips, M. C., Lund-Katz, S., and Bielicki, J. K. (2007) The C-terminal lipid-binding domain of apolipoprotein E is a highly efficient mediator of ABCA1-dependent cholesterol efflux that promotes the assembly of high-density lipoproteins Biochemistry 46, 2583-2593
    • (2007) Biochemistry , vol.46 , pp. 2583-2593
    • Vedhachalam, C.1    Narayanaswami, V.2    Neto, N.3    Forte, T.M.4    Phillips, M.C.5    Lund-Katz, S.6    Bielicki, J.K.7
  • 44
    • 77952737056 scopus 로고    scopus 로고
    • A new HDL mimetic peptide that stimulates cellular cholesterol efflux with high efficiency greatly reduces atherosclerosis in mice
    • Bielicki, J. K., Zhang, H., Cortez, Y., Zheng, Y., Narayanaswami, V., Patel, A., Johansson, J., and Azhar, S. (2010) A new HDL mimetic peptide that stimulates cellular cholesterol efflux with high efficiency greatly reduces atherosclerosis in mice J. Lipid Res. 51, 1496-1503
    • (2010) J. Lipid Res. , vol.51 , pp. 1496-1503
    • Bielicki, J.K.1    Zhang, H.2    Cortez, Y.3    Zheng, Y.4    Narayanaswami, V.5    Patel, A.6    Johansson, J.7    Azhar, S.8
  • 45
    • 79955867694 scopus 로고    scopus 로고
    • HDL mimetic peptide ATI-5261 forms an oligomeric assembly in solution that dissociates to monomers upon dilution
    • Zheng, Y., Patel, A. B., Narayanaswami, V., Hura, G. L., Hang, B., and Bielicki, J. K. (2011) HDL mimetic peptide ATI-5261 forms an oligomeric assembly in solution that dissociates to monomers upon dilution Biochemistry 50, 4068-4076
    • (2011) Biochemistry , vol.50 , pp. 4068-4076
    • Zheng, Y.1    Patel, A.B.2    Narayanaswami, V.3    Hura, G.L.4    Hang, B.5    Bielicki, J.K.6
  • 47
    • 27744572151 scopus 로고    scopus 로고
    • Acrolein impairs ATP binding cassette transporter A1-dependent cholesterol export from cells through site-specific modification of apolipoprotein A-I
    • Shao, B., Fu, X., McDonald, T. O., Green, P. S., Uchida, K., O'Brien, K. D., Oram, J. F., and Heinecke, J. W. (2005) Acrolein impairs ATP binding cassette transporter A1-dependent cholesterol export from cells through site-specific modification of apolipoprotein A-I J. Biol. Chem. 280, 36386-36396
    • (2005) J. Biol. Chem. , vol.280 , pp. 36386-36396
    • Shao, B.1    Fu, X.2    McDonald, T.O.3    Green, P.S.4    Uchida, K.5    O'Brien, K.D.6    Oram, J.F.7    Heinecke, J.W.8
  • 48
    • 0032568935 scopus 로고    scopus 로고
    • Acrolein is a product of lipid peroxidation reaction. Formation of free acrolein and its conjugate with lysine residues in oxidized low density lipoproteins
    • Uchida, K., Kanematsu, M., Morimitsu, Y., Osawa, T., Noguchi, N., and Niki, E. (1998) Acrolein is a product of lipid peroxidation reaction. Formation of free acrolein and its conjugate with lysine residues in oxidized low density lipoproteins J. Biol. Chem. 273, 16058-16066
    • (1998) J. Biol. Chem. , vol.273 , pp. 16058-16066
    • Uchida, K.1    Kanematsu, M.2    Morimitsu, Y.3    Osawa, T.4    Noguchi, N.5    Niki, E.6
  • 49
    • 34547103281 scopus 로고    scopus 로고
    • Acrolein inhibits cytokine gene expression by alkylating cysteine and arginine residues in the NF-kappaB1 DNA binding domain
    • Lambert, C., Li, J., Jonscher, K., Yang, T. C., Reigan, P., Quintana, M., Harvey, J., and Freed, B. M. (2007) Acrolein inhibits cytokine gene expression by alkylating cysteine and arginine residues in the NF-kappaB1 DNA binding domain J. Biol. Chem. 282, 19666-19675
    • (2007) J. Biol. Chem. , vol.282 , pp. 19666-19675
    • Lambert, C.1    Li, J.2    Jonscher, K.3    Yang, T.C.4    Reigan, P.5    Quintana, M.6    Harvey, J.7    Freed, B.M.8
  • 50
    • 1542677102 scopus 로고    scopus 로고
    • N(epsilon)-(3-methylpyridinium)lysine, a major antigenic adduct generated in acrolein-modified protein
    • Furuhata, A., Ishii, T., Kumazawa, S., Yamada, T., Nakayama, T., and Uchida, K. (2003) N(epsilon)-(3-methylpyridinium)lysine, a major antigenic adduct generated in acrolein-modified protein J. Biol. Chem. 278, 48658-48665
    • (2003) J. Biol. Chem. , vol.278 , pp. 48658-48665
    • Furuhata, A.1    Ishii, T.2    Kumazawa, S.3    Yamada, T.4    Nakayama, T.5    Uchida, K.6
  • 51
    • 84892674196 scopus 로고    scopus 로고
    • Pathophysiology of lipoprotein oxidation
    • (Frank, S. and Kostner, G. Eds.), InTech, Rijeka, Croatia.
    • Jairam, V., Uchida, K., and Narayanaswami, V. (2012) Pathophysiology of lipoprotein oxidation, in Lipoproteins-Role in Health and Diseases (Frank, S. and Kostner, G., Eds.), InTech, Rijeka, Croatia.
    • (2012) Lipoproteins - Role in Health and Diseases
    • Jairam, V.1    Uchida, K.2    Narayanaswami, V.3
  • 52
    • 0025814980 scopus 로고
    • Chemistry and biochemistry of 4-hydroxynonenal, malonaldehyde and related aldehydes
    • Esterbauer, H., Schaur, R. J., and Zollner, H. (1991) Chemistry and biochemistry of 4-hydroxynonenal, malonaldehyde and related aldehydes Free Radical Biol. Med. 11, 81-128
    • (1991) Free Radical Biol. Med. , vol.11 , pp. 81-128
    • Esterbauer, H.1    Schaur, R.J.2    Zollner, H.3
  • 53
    • 0028800748 scopus 로고
    • Role of low-density lipoproteins in atherogenesis and development of coronary heart disease
    • Grundy, S. M. (1995) Role of low-density lipoproteins in atherogenesis and development of coronary heart disease Clin. Chem. 41, 139-146
    • (1995) Clin. Chem. , vol.41 , pp. 139-146
    • Grundy, S.M.1
  • 54
    • 0026695202 scopus 로고
    • Role of oxidized low density lipoprotein in atherogenesis
    • Parthasarathy, S. and Rankin, S. M. (1992) Role of oxidized low density lipoprotein in atherogenesis Prog. Lipid Res. 31, 127-143
    • (1992) Prog. Lipid Res. , vol.31 , pp. 127-143
    • Parthasarathy, S.1    Rankin, S.M.2
  • 55
    • 0028092997 scopus 로고
    • Human apolipoprotein E. Role of arginine 61 in mediating the lipoprotein preferences of the E3 and E4 isoforms
    • Dong, L. M., Wilson, C., Wardell, M. R., Simmons, T., Mahley, R. W., Weisgraber, K. H., and Agard, D. A. (1994) Human apolipoprotein E. Role of arginine 61 in mediating the lipoprotein preferences of the E3 and E4 isoforms J. Biol. Chem. 269, 22358-22365
    • (1994) J. Biol. Chem. , vol.269 , pp. 22358-22365
    • Dong, L.M.1    Wilson, C.2    Wardell, M.R.3    Simmons, T.4    Mahley, R.W.5    Weisgraber, K.H.6    Agard, D.A.7
  • 56
    • 0029766916 scopus 로고    scopus 로고
    • Human apolipoprotein E4 domain interaction. Arginine 61 and glutamic acid 255 interact to direct the preference for very low density lipoproteins
    • Dong, L. M. and Weisgraber, K. H. (1996) Human apolipoprotein E4 domain interaction. Arginine 61 and glutamic acid 255 interact to direct the preference for very low density lipoproteins J. Biol. Chem. 271, 19053-19057
    • (1996) J. Biol. Chem. , vol.271 , pp. 19053-19057
    • Dong, L.M.1    Weisgraber, K.H.2
  • 57
    • 0035949490 scopus 로고    scopus 로고
    • Introduction of human apolipoprotein E4 "domain interaction" into mouse apolipoprotein e
    • Raffai, R. L., Dong, L. M., Farese, R. V., Jr., and Weisgraber, K. H. (2001) Introduction of human apolipoprotein E4 "domain interaction" into mouse apolipoprotein E Proc. Natl. Acad. Sci. U. S. A. 98, 11587-11591
    • (2001) Proc. Natl. Acad. Sci. U. S. A. , vol.98 , pp. 11587-11591
    • Raffai, R.L.1    Dong, L.M.2    Farese Jr., R.V.3    Weisgraber, K.H.4
  • 58
    • 0032895028 scopus 로고    scopus 로고
    • Remnant lipoprotein metabolism: Key pathways involving cell-surface heparan sulfate proteoglycans and apolipoprotein e
    • Mahley, R. W. and Ji, Z. S. (1999) Remnant lipoprotein metabolism: key pathways involving cell-surface heparan sulfate proteoglycans and apolipoprotein E J. Lipid Res. 40, 1-16
    • (1999) J. Lipid Res. , vol.40 , pp. 1-16
    • Mahley, R.W.1    Ji, Z.S.2
  • 59
    • 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., Brecht, W. J., Miranda, R. D., Hussain, M. M., Innerarity, T. L., and Mahley, R. W. (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
  • 60
    • 22244478077 scopus 로고    scopus 로고
    • Structure and physiologic function of the low-density lipoprotein receptor
    • Jeon, H. and Blacklow, S. C. (2005) Structure and physiologic function of the low-density lipoprotein receptor Annu. Rev. Biochem. 74, 535-562
    • (2005) Annu. Rev. Biochem. , vol.74 , pp. 535-562
    • Jeon, H.1    Blacklow, S.C.2
  • 61
    • 33646046808 scopus 로고    scopus 로고
    • Structure of an LDLR-RAP complex reveals a general mode for ligand recognition by lipoprotein receptors
    • Fisher, C., Beglova, N., and Blacklow, S. C. (2006) Structure of an LDLR-RAP complex reveals a general mode for ligand recognition by lipoprotein receptors Mol. Cell 22, 277-283
    • (2006) Mol. Cell , vol.22 , pp. 277-283
    • Fisher, C.1    Beglova, N.2    Blacklow, S.C.3
  • 62
    • 0025860481 scopus 로고
    • Three-dimensional structure of the LDL receptor-binding domain of human apolipoprotein e
    • Wilson, C., Wardell, M. R., Weisgraber, K. H., Mahley, R. W., and Agard, D. A. (1991) Three-dimensional structure of the LDL receptor-binding domain of human apolipoprotein E Science 252, 1817-1822
    • (1991) Science , vol.252 , pp. 1817-1822
    • Wilson, C.1    Wardell, M.R.2    Weisgraber, K.H.3    Mahley, R.W.4    Agard, D.A.5
  • 63
    • 0034723189 scopus 로고    scopus 로고
    • Effect of arginine 172 on the binding of apolipoprotein e to the low density lipoprotein receptor
    • Morrow, J. A., Arnold, K. S., Dong, J., Balestra, M. E., Innerarity, T. L., and Weisgraber, K. H. (2000) Effect of arginine 172 on the binding of apolipoprotein E to the low density lipoprotein receptor J. Biol. Chem. 275, 2576-2580
    • (2000) J. Biol. Chem. , vol.275 , pp. 2576-2580
    • Morrow, J.A.1    Arnold, K.S.2    Dong, J.3    Balestra, M.E.4    Innerarity, T.L.5    Weisgraber, K.H.6
  • 64
    • 0018238837 scopus 로고
    • Role of lysine residues of plasma lipoproteins in high affinity binding to cell surface receptors on human fibroblasts
    • Weisgraber, K. H., Innerarity, T. L., and Mahley, R. W. (1978) Role of lysine residues of plasma lipoproteins in high affinity binding to cell surface receptors on human fibroblasts J. Biol. Chem. 253, 9053-9062
    • (1978) J. Biol. Chem. , vol.253 , pp. 9053-9062
    • Weisgraber, K.H.1    Innerarity, T.L.2    Mahley, R.W.3
  • 65
    • 34548819619 scopus 로고    scopus 로고
    • Versatility in ligand recognition by LDL receptor family proteins: Advances and frontiers
    • Blacklow, S. C. (2007) Versatility in ligand recognition by LDL receptor family proteins: Advances and frontiers Curr. Opin. Struct. Biol. 17, 419-426
    • (2007) Curr. Opin. Struct. Biol. , vol.17 , pp. 419-426
    • Blacklow, S.C.1
  • 66
    • 16744362713 scopus 로고    scopus 로고
    • Apolipoprotein E-low density lipoprotein receptor binding: Study of protein-protein interaction in rationally selected docked complexes
    • Prevost, M. and Raussens, V. (2004) Apolipoprotein E-low density lipoprotein receptor binding: study of protein-protein interaction in rationally selected docked complexes Proteins 55, 874-884
    • (2004) Proteins , vol.55 , pp. 874-884
    • Prevost, M.1    Raussens, V.2
  • 67
    • 76749135871 scopus 로고    scopus 로고
    • Decoding of lipoprotein-receptor interactions: Properties of ligand binding modules governing interactions with apolipoprotein e
    • Guttman, M., Prieto, J. H., Croy, J. E., and Komives, E. A. (2010) Decoding of lipoprotein-receptor interactions: properties of ligand binding modules governing interactions with apolipoprotein E Biochemistry 49, 1207-1216
    • (2010) Biochemistry , vol.49 , pp. 1207-1216
    • Guttman, M.1    Prieto, J.H.2    Croy, J.E.3    Komives, E.A.4
  • 68
    • 0032743737 scopus 로고    scopus 로고
    • Pathogenesis of type III hyperlipoproteinemia (dysbetalipoproteinemia). Questions, quandaries, and paradoxes
    • Mahley, R. W., Huang, Y., and Rall, S. C., Jr. (1999) Pathogenesis of type III hyperlipoproteinemia (dysbetalipoproteinemia). Questions, quandaries, and paradoxes J. Lipid Res. 40, 1933-1949
    • (1999) J. Lipid Res. , vol.40 , pp. 1933-1949
    • Mahley, R.W.1    Huang, Y.2    Rall Jr., S.C.3
  • 69
    • 14044262236 scopus 로고    scopus 로고
    • Two-step mechanism of binding of apolipoprotein e to heparin: Implications for the kinetics of apolipoprotein E-heparan sulfate proteoglycan complex formation on cell surfaces
    • Futamura, M., Dhanasekaran, P., Handa, T., Phillips, M. C., Lund-Katz, S., and Saito, H. (2005) Two-step mechanism of binding of apolipoprotein E to heparin: Implications for the kinetics of apolipoprotein E-heparan sulfate proteoglycan complex formation on cell surfaces J. Biol. Chem. 280, 5414-5422
    • (2005) J. Biol. Chem. , vol.280 , pp. 5414-5422
    • Futamura, M.1    Dhanasekaran, P.2    Handa, T.3    Phillips, M.C.4    Lund-Katz, S.5    Saito, H.6
  • 73
    • 0034975014 scopus 로고    scopus 로고
    • Effects of polymorphism on the microenvironment of the LDL receptor-binding region of human apoE
    • Lund-Katz, S., Wehrli, S., Zaiou, M., Newhouse, Y., Weisgraber, K. H., and Phillips, M. C. (2001) Effects of polymorphism on the microenvironment of the LDL receptor-binding region of human apoE J. Lipid Res. 42, 894-901
    • (2001) J. Lipid Res. , vol.42 , pp. 894-901
    • Lund-Katz, S.1    Wehrli, S.2    Zaiou, M.3    Newhouse, Y.4    Weisgraber, K.H.5    Phillips, M.C.6
  • 74
    • 84865117958 scopus 로고    scopus 로고
    • The positional specificity of EXXK motifs within an amphipathic alpha-helix dictates preferential lysine modification by acrolein: Implications for the design of high-density lipoprotein mimetic peptides
    • Zheng, Y., Kim, S. H., Patel, A. B., Narayanaswami, V., Iavarone, A. T., Hura, G. L., and Bielicki, J. K. (2012) The positional specificity of EXXK motifs within an amphipathic alpha-helix dictates preferential lysine modification by acrolein: Implications for the design of high-density lipoprotein mimetic peptides Biochemistry 51, 6400-6412
    • (2012) Biochemistry , vol.51 , pp. 6400-6412
    • Zheng, Y.1    Kim, S.H.2    Patel, A.B.3    Narayanaswami, V.4    Iavarone, A.T.5    Hura, G.L.6    Bielicki, J.K.7
  • 79
    • 0025728398 scopus 로고
    • Interaction of free apolipoproteins with macrophages. Formation of high density lipoprotein-like lipoproteins and reduction of cellular cholesterol
    • Hara, H. and Yokoyama, S. (1991) Interaction of free apolipoproteins with macrophages. Formation of high density lipoprotein-like lipoproteins and reduction of cellular cholesterol J. Biol. Chem. 266, 3080-3086
    • (1991) J. Biol. Chem. , vol.266 , pp. 3080-3086
    • Hara, H.1    Yokoyama, S.2
  • 80
    • 0030480126 scopus 로고    scopus 로고
    • Apolipoprotein-mediated removal of cellular cholesterol and phospholipids
    • Oram, J. F. and Yokoyama, S. (1996) Apolipoprotein-mediated removal of cellular cholesterol and phospholipids J. Lipid Res. 37, 2473-2491
    • (1996) J. Lipid Res. , vol.37 , pp. 2473-2491
    • Oram, J.F.1    Yokoyama, S.2
  • 81
    • 0029804198 scopus 로고    scopus 로고
    • Cyclic AMP induces apolipoprotein e binding activity and promotes cholesterol efflux from a macrophage cell line to apolipoprotein acceptors
    • Smith, J. D., Miyata, M., Ginsberg, M., Grigaux, C., Shmookler, E., and Plump, A. S. (1996) Cyclic AMP induces apolipoprotein E binding activity and promotes cholesterol efflux from a macrophage cell line to apolipoprotein acceptors J. Biol. Chem. 271, 30647-30655
    • (1996) J. Biol. Chem. , vol.271 , pp. 30647-30655
    • Smith, J.D.1    Miyata, M.2    Ginsberg, M.3    Grigaux, C.4    Shmookler, E.5    Plump, A.S.6
  • 83
    • 0026024295 scopus 로고
    • A simple test for predisposition to LDL oxidation based on the fluorescence development during copper-catalyzed oxidative modification
    • Cominacini, L., Garbin, U., Davoli, A., Micciolo, R., Bosello, O., Gaviraghi, G., Scuro, L. A., and Pastorino, A. M. (1991) A simple test for predisposition to LDL oxidation based on the fluorescence development during copper-catalyzed oxidative modification J. Lipid Res. 32, 349-358
    • (1991) J. Lipid Res. , vol.32 , pp. 349-358
    • Cominacini, L.1    Garbin, U.2    Davoli, A.3    Micciolo, R.4    Bosello, O.5    Gaviraghi, G.6    Scuro, L.A.7    Pastorino, A.M.8


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