메뉴 건너뛰기




Volumn 50, Issue 12, 2011, Pages 2040-2047

Enhanced binding of apolipoprotein A-I variants associated with hypertriglyceridemia to triglyceride-rich particles

Author keywords

[No Author keywords available]

Indexed keywords

APOLIPOPROTEIN A-I; APOLIPOPROTEIN E (APOE); APOLIPOPROTEINS; BIOPHYSICAL PROPERTIES; HYDROPHOBIC SURFACES; HYPERCHOLESTEROLEMIA; HYPERTRIGLYCERIDEMIA; OVER-EXPRESSION; PLASMA TRIGLYCERIDES; PROTEIN DESTABILIZATION; WILD TYPES;

EID: 79952922720     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi200158b     Document Type: Article
Times cited : (7)

References (40)
  • 1
    • 0029838433 scopus 로고    scopus 로고
    • Plasma triglyceride level is a risk factor for cardiovascular disease independent of high-density lipoprotein cholesterol level: A meta-analysis of population-based prospective studies
    • Hokanson, J. E. and Austin, M. A. (1996) Plasma triglyceride level is a risk factor for cardiovascular disease independent of high-density lipoprotein cholesterol level: A meta-analysis of population-based prospective studies J. Cardiovasc. Risk 3 (2) 213-219 (Pubitemid 26266496)
    • (1996) Journal of Cardiovascular Risk , vol.3 , Issue.2 , pp. 213-219
    • Hokanson, J.E.1    Austin, M.A.2
  • 2
    • 68049109461 scopus 로고    scopus 로고
    • Catabolism of lipoproteins and metabolic syndrome
    • Therond, P. (2009) Catabolism of lipoproteins and metabolic syndrome Curr. Opin. Clin. Nutr. Metab. Care 12, 366-371
    • (2009) Curr. Opin. Clin. Nutr. Metab. Care , vol.12 , pp. 366-371
    • Therond, P.1
  • 3
    • 79952276408 scopus 로고    scopus 로고
    • Metabolic syndrome: What are the risks for humans?
    • Gupta, A. and Gupta, V. (2010) Metabolic syndrome: What are the risks for humans? Biosci. Trends 4 (5) 204-212
    • (2010) Biosci. Trends , vol.4 , Issue.5 , pp. 204-212
    • Gupta, A.1    Gupta, V.2
  • 4
    • 73849123494 scopus 로고    scopus 로고
    • Triglyceride-rich lipoproteins and plasma lipid transport
    • Havel, R. J. (2010) Triglyceride-rich lipoproteins and plasma lipid transport Arterioscler., Thromb., Vasc. Biol. 30, 9-19
    • (2010) Arterioscler., Thromb., Vasc. Biol. , vol.30 , pp. 9-19
    • Havel, R.J.1
  • 6
    • 0035827693 scopus 로고    scopus 로고
    • Domains of apolipoprotein e contributing to triglyceride and cholesterol homeostasis in Vivo. Carboxyl-terminal region 203-299 promotes hepatic very low density lipoprotein-triglyceride secretion
    • Kypreos, K. E., van Dijk, K. W., van Der Zee, A., Havekes, L. M., and Zannis, V. I. (2001) Domains of apolipoprotein E contributing to triglyceride and cholesterol homeostasis In Vivo. Carboxyl-terminal region 203-299 promotes hepatic very low density lipoprotein-triglyceride secretion J. Biol. Chem. 276, 19778-19786
    • (2001) J. Biol. Chem. , vol.276 , pp. 19778-19786
    • Kypreos, K.E.1    Van Dijk, K.W.2    Van Der Zee, A.3    Havekes, L.M.4    Zannis, V.I.5
  • 7
    • 14844327766 scopus 로고    scopus 로고
    • Generation of a recombinant apolipoprotein E variant with improved biological functions: Hydrophobic residues (LEU-261, TRP-264, PHE-265, LEU-268, VAL-269) of apoE can account for the apoE-induced hypertriglyceridemia
    • DOI 10.1074/jbc.M413458200
    • Kypreos, K. E., van Dijk, K. W., Havekes, L. M., and Zannis, V. I. (2005) Generation of a recombinant apolipoprotein E variant with improved biological functions: Hydrophobic residues (Leu-261, Trp-264, Phe-265, Leu-268, Val-269) of apoE can account for the apoE-induced hypertriglyceridemia J. Biol. Chem. 280, 6276-6284 (Pubitemid 40341173)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.8 , pp. 6276-6284
    • Kypreos, K.E.1    Van Dijk, K.W.2    Havekes, L.M.3    Zannis, V.I.4
  • 8
    • 33646855426 scopus 로고    scopus 로고
    • The unique role of apolipoprotein A-I in HDL remodeling and metabolism
    • DOI 10.1097/01.mol.0000226110.66942.e8, PII 0004143320060600000002
    • Pownall, H. J. and Ehnholm, C. (2006) The unique role of apolipoprotein A-I in HDL remodeling and metabolism Curr. Opin. Lipidol. 17, 209-213 (Pubitemid 43786052)
    • (2006) Current Opinion in Lipidology , vol.17 , Issue.3 , pp. 209-213
    • Pownall, H.J.1    Ehnholm, C.2
  • 10
    • 0036234218 scopus 로고    scopus 로고
    • The effects of altered apolipoprotein A-I structure on plasma HDL concentration
    • DOI 10.1016/S1050-1738(01)00163-3, PII S1050173801001633
    • Sorci-Thomas, M. G. and Thomas, M. J. (2002) The effects of altered apolipoprotein A-I structure on plasma HDL concentration Trends Cardiovasc. Med. 12, 121-128 (Pubitemid 34462182)
    • (2002) Trends in Cardiovascular Medicine , vol.12 , Issue.3 , pp. 121-128
    • Sorci-Thomas, M.G.1    Thomas, M.J.2
  • 11
    • 0036689537 scopus 로고    scopus 로고
    • Structure-function studies of apoA-I variants: Site-directed mutagenesis and natural mutations
    • Sviridov, D., Hoang, A., Huang, W., and Sasaki, J. (2002) Structure-function studies of apoA-I variants: Site-directed mutagenesis and natural mutations J. Lipid Res. 43 (8) 1283-1292 (Pubitemid 34988176)
    • (2002) Journal of Lipid Research , vol.43 , Issue.8 , pp. 1283-1292
    • Sviridov, D.1    Hoang, A.2    Huang, W.3    Sasaki, J.4
  • 12
    • 67650541109 scopus 로고    scopus 로고
    • Structural and functional consequences of the Milano mutation (R173C) in human apolipoprotein A-I
    • Alexander, E. T., Tanaka, M., Kono, M., Saito, H., Rader, D. J., and Phillips, M. C. (2009) Structural and functional consequences of the Milano mutation (R173C) in human apolipoprotein A-I J. Lipid Res. 50 (7) 1409-1419
    • (2009) J. Lipid Res. , vol.50 , Issue.7 , pp. 1409-1419
    • Alexander, E.T.1    Tanaka, M.2    Kono, M.3    Saito, H.4    Rader, D.J.5    Phillips, M.C.6
  • 13
    • 4043125999 scopus 로고    scopus 로고
    • Substitutions of glutamate 110 and 111 in the middle helix 4 of human apolipoprotein A-I (apoA-I) by alanine affect the structure and in vitro functions of apoA-I and induce severe hypertriglyceridemia in apoA-I-deficient mice
    • DOI 10.1021/bi049782p
    • Chroni, A., Kan, H.-Y., Kypreos, K. E., Gorshkova, I. N., Shkodrani, A., and Zannis, V. I. (2004) Substitutions of Glu110 and Glu111 in the middle helix 4 of human apoA-I by alanine affect the structure and in vitro functions of apoA-I and induce severe hypertriglyceridemia in apoA-I-deficient mice Biochemistry 43, 10442-10457 (Pubitemid 39079318)
    • (2004) Biochemistry , vol.43 , Issue.32 , pp. 10442-10457
    • Chroni, A.1    Kan, H.-Y.2    Kypreos, K.E.3    Gorshkova, I.N.4    Shkodrani, A.5    Zannis, V.I.6
  • 14
    • 14844357362 scopus 로고    scopus 로고
    • Deletions of helices 2 and 3 of human apoA-I are associated with severe dyslipidemia following adenovirus-mediated gene transfer in apoA-I-deficient mice
    • DOI 10.1021/bi047998l
    • Chroni, A., Kan, H.-Y., Shkodrani, A., Liu, T., and Zannis, V. I. (2005) Deletions of helices 2 and 3 of human apoA-I are associated with severe dyslipidemia following adenovirus-mediated gene transfer in apoA-I-deficient mice Biochemistry 44, 4108-4117 (Pubitemid 40358064)
    • (2005) Biochemistry , vol.44 , Issue.10 , pp. 4108-4117
    • Chroni, A.1    Kan, H.-Y.2    Shkodrani, A.3    Liu, T.4    Zannis, V.I.5
  • 15
    • 56749119973 scopus 로고    scopus 로고
    • Biophysical properties of apolipoprotein E4 variants: Implications in molecular mechanisms of correction of HTG
    • Gorshkova, I. N., Kypreos, K. E., Gantz, D. L., Zannis, V. I., and Atkinson, D. (2008) Biophysical properties of apolipoprotein E4 variants: Implications in molecular mechanisms of correction of HTG Biochemistry 47, 12644-12654
    • (2008) Biochemistry , vol.47 , pp. 12644-12654
    • Gorshkova, I.N.1    Kypreos, K.E.2    Gantz, D.L.3    Zannis, V.I.4    Atkinson, D.5
  • 16
    • 31544431989 scopus 로고    scopus 로고
    • Structure and stability of apolipoprotein A-I in solution and in discoidal high-density lipoprotein probed by double charge ablation and deletion mutation
    • DOI 10.1021/bi051669r
    • Gorshkova, I. N., Liu, T., Kan, H. Y., Chroni, A., Zannis, V. I., and Atkinson, D. (2006) Structure and stability of apolipoprotein A-I in solution and in discoidal high-density lipoprotein probed by double charge ablation and deletion mutation Biochemistry 45, 1242-1254 (Pubitemid 43167191)
    • (2006) Biochemistry , vol.45 , Issue.4 , pp. 1242-1254
    • Gorshkova, I.N.1    Liu, T.2    Kan, H.-Y.3    Chroni, A.4    Zannis, V.I.5    Atkinson, D.6
  • 17
    • 0015522150 scopus 로고
    • Determination of the secondary structures of proteins by circular dichroism and optical rotatory dispersion
    • Chen, Y. H., Yang, J. T., and Martinez, H. M. (1972) Determination of the secondary structures of proteins by circular dichroism and optical rotatory dispersion Biochemistry 11 (22) 4120-4131
    • (1972) Biochemistry , vol.11 , Issue.22 , pp. 4120-4131
    • Chen, Y.H.1    Yang, J.T.2    Martinez, H.M.3
  • 18
    • 0037143582 scopus 로고    scopus 로고
    • Lipid-free structure and stability of apolipoprotein A-I: Probing the central region by mutation
    • Gorshkova, I. N., Liu, T., Zannis, V. I., and Atkinson, D. (2002) Lipid-free structure and stability of apolipoprotein A-I: Probing the central region by mutation Biochemistry 41, 10529-10539
    • (2002) Biochemistry , vol.41 , pp. 10529-10539
    • Gorshkova, I.N.1    Liu, T.2    Zannis, V.I.3    Atkinson, D.4
  • 20
    • 70449246528 scopus 로고
    • Phosphorus assay in column chromatography
    • Bartlett, G. R. (1959) Phosphorus assay in column chromatography J. Biol. Chem. 234, 466-468
    • (1959) J. Biol. Chem. , vol.234 , pp. 466-468
    • Bartlett, G.R.1
  • 21
    • 0035798681 scopus 로고    scopus 로고
    • Lipid binding-induced conformational change in human apolipoprotein E. Evidence for two lipid-bound states on spherical particles
    • Saito, H., Dhanasekaran, P., Baldwin, F., Weisgraber, K. H., Lund-Katz, S., and Phillips, M. C. (2001) Lipid binding-induced conformational change in human apolipoprotein E. Evidence for two lipid-bound states on spherical particles J. Biol. Chem. 276, 40949-40954
    • (2001) J. Biol. Chem. , vol.276 , pp. 40949-40954
    • Saito, H.1    Dhanasekaran, P.2    Baldwin, F.3    Weisgraber, K.H.4    Lund-Katz, S.5    Phillips, M.C.6
  • 22
    • 0141733182 scopus 로고    scopus 로고
    • Interfacial properties of an amphipathic α-helix consensus peptide of exchangeable apolipoproteins at air/water and oil/water interfaces
    • DOI 10.1074/jbc.M303133200
    • Wang, L., Atkinson, D., and Small, D. M. (2003) Interfacial properties of an amphipathic α-helix consensus peptide of exchangeable apolipoproteins at air/water and oil/water interfaces J. Biol. Chem. 278, 37480-37491 (Pubitemid 37175269)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.39 , pp. 37480-37491
    • Wang, L.1    Atkinson, D.2    Small, D.M.3
  • 26
    • 0033991858 scopus 로고    scopus 로고
    • Molecular basis of exchangeable apolipoprotein function
    • Narayanaswami, V. and Ryan, R. O. (2000) Molecular basis of exchangeable apolipoprotein function Biochim. Biophys. Acta 1483, 15-36
    • (2000) Biochim. Biophys. Acta , vol.1483 , pp. 15-36
    • Narayanaswami, V.1    Ryan, R.O.2
  • 27
    • 33748645937 scopus 로고    scopus 로고
    • Contributions of the N- and C-terminal helical segments to the lipid-free structure and lipid interaction of apolipoprotein A-I
    • DOI 10.1021/bi060726t
    • Tanaka, M., Dhanasekaran, P., Nguyen, D., Ohta, S., Lund-Katz, S., Phillips, M. C., and Saito, H. (2006) Contributions of the N- and C-terminal helical segments to the lipid-free structure and lipid interaction of apolipoprotein A-I Biochemistry 45, 10351-10358 (Pubitemid 44384811)
    • (2006) Biochemistry , vol.45 , Issue.34 , pp. 10351-10358
    • Tanaka, M.1    Dhanasekaran, P.2    Nguyen, D.3    Ohta, S.4    Lund-Katz, S.5    Phillips, M.C.6    Saito, H.7
  • 30
    • 39649104095 scopus 로고    scopus 로고
    • Influence of tertiary structure domain properties on the functionality of apolipoprotein A-I
    • DOI 10.1021/bi702332b
    • Tanaka, M., Koyama, M., Dhanasekaran, P., Nguyen, D., Nickel, M., Lund-Katz, S., Saito, H., and Phillips, M. C. (2008) Influence of tertiary structure domain properties on the functionality of apolipoprotein A-I Biochemistry 47 (7) 2172-2180 (Pubitemid 351287143)
    • (2008) Biochemistry , vol.47 , Issue.7 , pp. 2172-2180
    • Tanaka, M.1    Koyama, M.2    Dhanasekaran, P.3    Nguyen, D.4    Nickel, M.5    Lund-Katz, S.6    Saito, H.7    Phillips, M.C.8
  • 31
    • 64849086373 scopus 로고    scopus 로고
    • Interaction between the N- and C-terminal domains modulates the stability and lipid binding of apolipoprotein A-I
    • Koyama, M., Tanaka, M., Dhanasekaran, P., Lund-Katz, S., Phillips, M. C., and Saito, H. (2009) Interaction between the N- and C-terminal domains modulates the stability and lipid binding of apolipoprotein A-I Biochemistry 48, 2529-2537
    • (2009) Biochemistry , vol.48 , pp. 2529-2537
    • Koyama, M.1    Tanaka, M.2    Dhanasekaran, P.3    Lund-Katz, S.4    Phillips, M.C.5    Saito, H.6
  • 33
    • 0030347890 scopus 로고    scopus 로고
    • All-or-none solvent-induced transitions between native, molten globule and unfolded states in globular proteins
    • Uversky, V. N. and Ptitsyn, O. B. (1996) All-or-none solvent-induced transitions between native, molten globule and unfolded states in globular proteins Folding Des. 1 (2) 117-122 (Pubitemid 126748166)
    • (1996) Folding and Design , vol.1 , Issue.2 , pp. 117-122
    • Uversky, V.N.1    Ptitsyn, O.B.2
  • 34
    • 0029124248 scopus 로고
    • Molten globule and protein folding
    • Ptitsyn, O. B. (1995) Molten globule and protein folding Adv. Protein Chem. 47, 83-229
    • (1995) Adv. Protein Chem. , vol.47 , pp. 83-229
    • Ptitsyn, O.B.1
  • 35
    • 0037184994 scopus 로고    scopus 로고
    • Apolipoprotein E4 forms a molten globule: A potential basis for its association with disease
    • DOI 10.1074/jbc.M204898200
    • Morrow, J. A., Hatters, D. M., Lu, B., Hochtl, P., Oberg, K. A., Rupp, B., and Weisgraber, K. H. (2002) Apolipoprotein E4 forms a molten globule. A potential basis for its association with disease J. Biol. Chem. 277 (52) 50380-50385 (Pubitemid 36042188)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.52 , pp. 50380-50385
    • Morrow, J.A.1    Hatters, D.M.2    Lu, B.3    Hochtl, P.4    Oberg, K.A.5    Rupp, B.6    Weisgraber, K.H.7
  • 37
    • 78650487051 scopus 로고    scopus 로고
    • Molecular basis for the differences in lipid and lipoprotein binding properties of human apolipoproteins E3 and E4
    • Nguyen, D., Dhanasekaran, P., Nickel, M., Nakatani, R., Saito, H., Phillips, M. C., and Lund-Katz, S. (2010) Molecular basis for the differences in lipid and lipoprotein binding properties of human apolipoproteins E3 and E4 Biochemistry 49, 10881-10889
    • (2010) Biochemistry , vol.49 , pp. 10881-10889
    • Nguyen, D.1    Dhanasekaran, P.2    Nickel, M.3    Nakatani, R.4    Saito, H.5    Phillips, M.C.6    Lund-Katz, S.7
  • 38
    • 22544443366 scopus 로고    scopus 로고
    • Engineering conformational destabilization into mouse apolipoprotein E: A model for a unique property of human apolipoprotein E4
    • DOI 10.1074/jbc.M503910200
    • Hatters, D. M., Peters-Libeu, C. A., and Weisgraber, K. H. (2005) Engineering conformational destabilization into mouse apolipoprotein E. A model for a unique property of human apolipoprotein E4 J. Biol. Chem. 280, 26477-26482 (Pubitemid 41022244)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.28 , pp. 26477-26482
    • Hatters, D.M.1    Peters-Libeu, C.A.2    Weisgraber, K.H.3
  • 39
    • 20544455385 scopus 로고    scopus 로고
    • Role of buried polar residues in helix bundle stability and lipid binding of apolipophorin III: Destabilization by Threonine 31
    • DOI 10.1021/bi050502v
    • 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 (Pubitemid 40840446)
    • (2005) Biochemistry , vol.44 , Issue.24 , pp. 8810-8816
    • Weers, P.M.M.1    Abdullahi, W.E.2    Cabrera, J.M.3    Hsu, T.-C.4
  • 40
    • 77950615091 scopus 로고    scopus 로고
    • Surface plasmon resonance analysis of the mechanism of binding of apoA-I to high density lipoprotein particles
    • Lund-Katz, S., Nguyen, D., Dhanasekaran, P., Kono, M., Nickel, M., Saito, H., and Phillips, M. C. (2010) Surface plasmon resonance analysis of the mechanism of binding of apoA-I to high density lipoprotein particles J. Lipid Res. 51, 606-617
    • (2010) J. Lipid Res. , vol.51 , pp. 606-617
    • Lund-Katz, S.1    Nguyen, D.2    Dhanasekaran, P.3    Kono, M.4    Nickel, M.5    Saito, H.6    Phillips, M.C.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.