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Volumn 1788, Issue 9, 2009, Pages 1901-1906

Apolipophorin III lysine modification: Effect on structure and lipid binding

Author keywords

Apolipophorin; Apolipoprotein; DMPC; DMPG; Lipid; Lipoprotein

Indexed keywords

APOLIPOPHORIN 3; APOLIPOPROTEIN; DIMYRISTOYLPHOSPHATIDYLCHOLINE; DIMYRISTOYLPHOSPHATIDYLGLYCEROL; GUANIDINE; HYDROCHLORIC ACID; LIPID; LOW DENSITY LIPOPROTEIN; LYSINE; PHOSPHOLIPID; UNCLASSIFIED DRUG;

EID: 68749110897     PISSN: 00052736     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbamem.2009.05.006     Document Type: Article
Times cited : (13)

References (41)
  • 2
    • 33645057448 scopus 로고    scopus 로고
    • Apolipophorin III: role model apolipoprotein. Insect Biochem
    • Weers P.M.M., and Ryan R.O. Apolipophorin III: role model apolipoprotein. Insect Biochem. Mol. Biol. 36 (2006) 231-240
    • (2006) Mol. Biol. , vol.36 , pp. 231-240
    • Weers, P.M.M.1    Ryan, R.O.2
  • 4
    • 84882556426 scopus 로고    scopus 로고
    • Lipoprotein structure
    • Vance D.E., and Vance J.E. (Eds), Elsevier BV, Amsterdam, Lipoproteins and Membranes
    • Jonas A., and Phillips M.C. Lipoprotein structure. In: Vance D.E., and Vance J.E. (Eds). Biochemistry of Lipids (2008), Elsevier BV, Amsterdam, Lipoproteins and Membranes 485-506
    • (2008) Biochemistry of Lipids , pp. 485-506
    • Jonas, A.1    Phillips, M.C.2
  • 5
    • 3242656580 scopus 로고    scopus 로고
    • Contributions of domain structure and lipid interaction to the functionality of exchangeable human apolipoproteins
    • Saito H., Lund-Katz S., and Phillips M.C. Contributions of domain structure and lipid interaction to the functionality of exchangeable human apolipoproteins. Prog. Lipid Res. 43 (2004) 350-380
    • (2004) Prog. Lipid Res. , vol.43 , pp. 350-380
    • Saito, H.1    Lund-Katz, S.2    Phillips, M.C.3
  • 7
    • 0037022281 scopus 로고    scopus 로고
    • Structural basis for the conformational adaptability of apolipophorin III, a helix bundle exchangeable apolipoprotein
    • Wang J., Sykes B.D., and Ryan R.O. Structural basis for the conformational adaptability of apolipophorin III, a helix bundle exchangeable apolipoprotein. Proc. Natl. Acad. Sci. U.S.A. 99 (2002) 1188-1193
    • (2002) Proc. Natl. Acad. Sci. U.S.A. , vol.99 , pp. 1188-1193
    • Wang, J.1    Sykes, B.D.2    Ryan, R.O.3
  • 8
    • 0038418381 scopus 로고    scopus 로고
    • NMR solution structure and dynamics of an exchangeable apolipoprotein, Locusta migratoria apolipophorin III
    • Fan D., Zheng Y., Yang D., and Wang J. NMR solution structure and dynamics of an exchangeable apolipoprotein, Locusta migratoria apolipophorin III. J. Biol. Chem. 278 (2003) 21212-21220
    • (2003) J. Biol. Chem. , vol.278 , pp. 21212-21220
    • Fan, D.1    Zheng, Y.2    Yang, D.3    Wang, J.4
  • 9
    • 0028108646 scopus 로고
    • Binding of insect apolipophorin III to dimyristoylphosphatidylcholine vesicles. Evidence for a conformational change
    • Wientzek M., Kay C.M., Oikawa K., and Ryan R.O. Binding of insect apolipophorin III to dimyristoylphosphatidylcholine vesicles. Evidence for a conformational change. J. Biol. Chem. 269 (1994) 4605-4612
    • (1994) J. Biol. Chem. , vol.269 , pp. 4605-4612
    • Wientzek, M.1    Kay, C.M.2    Oikawa, K.3    Ryan, R.O.4
  • 10
    • 0036384368 scopus 로고    scopus 로고
    • Lipid triggered molecular switch of apoLp-III helix bundle to an extended helix conformation
    • Sahoo D., Weers P.M.M., Ryan R.O., and Narayanaswami V. Lipid triggered molecular switch of apoLp-III helix bundle to an extended helix conformation. J. Mol. Biol. 321 (2002) 201-214
    • (2002) J. Mol. Biol. , vol.321 , pp. 201-214
    • Sahoo, D.1    Weers, P.M.M.2    Ryan, R.O.3    Narayanaswami, V.4
  • 11
    • 0037205467 scopus 로고    scopus 로고
    • Structure of apolipophorin III in discoidal lipoproteins. Interhelical distances in the lipid-bound state and conformational change upon binding to lipid
    • Garda H.A., Arrese E.L., and Soulages J.L. Structure of apolipophorin III in discoidal lipoproteins. Interhelical distances in the lipid-bound state and conformational change upon binding to lipid. J. Biol. Chem. 277 (2002) 19773-19782
    • (2002) J. Biol. Chem. , vol.277 , pp. 19773-19782
    • Garda, H.A.1    Arrese, E.L.2    Soulages, J.L.3
  • 12
    • 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.M., Cabrera J., Abdullahi E.W., and Hsu T.C. Role of buried polar residues in helix bundle stability and lipid binding of apolipophorin III: destabilization by threonine 31. Biochemistry 44 (2005) 8810-8816
    • (2005) Biochemistry , vol.44 , pp. 8810-8816
    • Weers, P.M.M.1    Cabrera, J.2    Abdullahi, E.W.3    Hsu, T.C.4
  • 13
    • 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. Three dimensional structure of the LDL receptor-binding domain of human apolipoprotein E. Science 252 (1991) 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
  • 14
    • 84985727741 scopus 로고
    • Role of charged amino acid side chains in the stability and lipid binding of Manduca sexta apolipophorin
    • Upadhyaya M., Oikawa K., Kay C.M., Scraba D.G., Bradley R., and Ryan R.O. Role of charged amino acid side chains in the stability and lipid binding of Manduca sexta apolipophorin. Arch. Insect Biochem. Physiol. 30 (1995) 211-223
    • (1995) Arch. Insect Biochem. Physiol. , vol.30 , pp. 211-223
    • Upadhyaya, M.1    Oikawa, K.2    Kay, C.M.3    Scraba, D.G.4    Bradley, R.5    Ryan, R.O.6
  • 17
    • 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. Differences in stability among the human apolipoprotein E isoforms determined by the amino-terminal domain. Biochemistry 39 (2000) 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
  • 19
    • 0027524130 scopus 로고
    • Prevention of phospholipase-C induced aggregation of low-density lipoprotein by amphipathic apolipoproteins
    • Liu H., Scraba D.G., and Ryan R.O. Prevention of phospholipase-C induced aggregation of low-density lipoprotein by amphipathic apolipoproteins. FEBS Lett. 316 (1993) 27-33
    • (1993) FEBS Lett. , vol.316 , pp. 27-33
    • Liu, H.1    Scraba, D.G.2    Ryan, R.O.3
  • 20
    • 0842303042 scopus 로고    scopus 로고
    • Visible fluorescent detection of proteins in polyacrylamide gels without staining
    • Ladner C.L., Yang J.Y., Turner R.J., and Edwards R.A. Visible fluorescent detection of proteins in polyacrylamide gels without staining. Anal. Biochem. 326 (2004) 13-20
    • (2004) Anal. Biochem. , vol.326 , pp. 13-20
    • Ladner, C.L.1    Yang, J.Y.2    Turner, R.J.3    Edwards, R.A.4
  • 21
    • 0027391142 scopus 로고
    • Conformational, thermodynamic and stability properties of Manduca sexta apolipophorin III
    • Ryan R.O., Oikawa K., and Kay C.M. Conformational, thermodynamic and stability properties of Manduca sexta apolipophorin III. J. Biol. Chem. 268 (1993) 1525-1530
    • (1993) J. Biol. Chem. , vol.268 , pp. 1525-1530
    • Ryan, R.O.1    Oikawa, K.2    Kay, C.M.3
  • 22
    • 0028331057 scopus 로고
    • Factors affecting the stability and conformation of Locusta migratoria apolipophorin III
    • Weers P.M.M., Kay C.M., Oikawa K., Wientzek M., Van der Horst D.J., and Ryan R.O. Factors affecting the stability and conformation of Locusta migratoria apolipophorin III. Biochemistry 33 (1994) 3617-3624
    • (1994) Biochemistry , vol.33 , pp. 3617-3624
    • Weers, P.M.M.1    Kay, C.M.2    Oikawa, K.3    Wientzek, M.4    Van der Horst, D.J.5    Ryan, R.O.6
  • 24
    • 0034107475 scopus 로고    scopus 로고
    • Lipid transport biochemistry and role in energy production
    • Ryan R.O., and Van der Horst D.J. Lipid transport biochemistry and role in energy production. Ann. Rev. Entomol. 45 (2000) 233-260
    • (2000) Ann. Rev. Entomol. , vol.45 , pp. 233-260
    • Ryan, R.O.1    Van der Horst, D.J.2
  • 25
    • 0027405920 scopus 로고
    • Structures of the Asn-linked oligosaccharides of apolipophorin III from the insect Locusta migratoria. Carbohydrate-linked 2-aminoethylphosphonate as a constituent of a glycoprotein
    • Hård K., Van Doorn J.M., Thomas-Oates J.E., Kamerling J.P., and Van der Horst D.J. Structures of the Asn-linked oligosaccharides of apolipophorin III from the insect Locusta migratoria. Carbohydrate-linked 2-aminoethylphosphonate as a constituent of a glycoprotein. Biochemistry 32 (1993) 766-775
    • (1993) Biochemistry , vol.32 , pp. 766-775
    • Hård, K.1    Van Doorn, J.M.2    Thomas-Oates, J.E.3    Kamerling, J.P.4    Van der Horst, D.J.5
  • 26
    • 0034111173 scopus 로고    scopus 로고
    • Interaction of locust apolipophorin III with lipoproteins and phospholipid vesicles: effect of glycosylation
    • Weers P.M.M., Van der Horst D.J., and Ryan R.O. Interaction of locust apolipophorin III with lipoproteins and phospholipid vesicles: effect of glycosylation. J. Lipid Res. 41 (2000) 416-423
    • (2000) J. Lipid Res. , vol.41 , pp. 416-423
    • Weers, P.M.M.1    Van der Horst, D.J.2    Ryan, R.O.3
  • 27
    • 0022410254 scopus 로고
    • Why does Coomassie Brilliant Blue R interact differently with different proteins?
    • Tal M., Silberstein A., and Nusser E.J. Why does Coomassie Brilliant Blue R interact differently with different proteins?. J. Biol. Chem. 260 (1985) 9976-9980
    • (1985) J. Biol. Chem. , vol.260 , pp. 9976-9980
    • Tal, M.1    Silberstein, A.2    Nusser, E.J.3
  • 28
    • 33646022541 scopus 로고    scopus 로고
    • Apolipoprotein A-I lysine modification: effects on helical content, lipid binding and cholesterol acceptor activity
    • Brubaker G., Peng D.-Q., Somerlot B., Abdollahian D.J., and Smith J.D. Apolipoprotein A-I lysine modification: effects on helical content, lipid binding and cholesterol acceptor activity. Biochim. Biophys. Acta 1761 (2006) 64-72
    • (2006) Biochim. Biophys. Acta , vol.1761 , pp. 64-72
    • Brubaker, G.1    Peng, D.-Q.2    Somerlot, B.3    Abdollahian, D.J.4    Smith, J.D.5
  • 29
    • 0033618275 scopus 로고    scopus 로고
    • Interaction of an exchangeable apolipoprotein with phospholipid vesicles and lipoprotein particles. Role of leucines 32, 34 and 95 in Locusta migratoria apolipophorin III
    • Weers P.M.M., Narayanaswami V., Kay C.M., and Ryan R.O. Interaction of an exchangeable apolipoprotein with phospholipid vesicles and lipoprotein particles. Role of leucines 32, 34 and 95 in Locusta migratoria apolipophorin III. J. Biol. Chem. 274 (1999) 21804-21810
    • (1999) J. Biol. Chem. , vol.274 , pp. 21804-21810
    • Weers, P.M.M.1    Narayanaswami, V.2    Kay, C.M.3    Ryan, R.O.4
  • 30
    • 33144485711 scopus 로고    scopus 로고
    • Crystal structure of human apolipoprotein A-I: insights into its protective effect against cardiovascular diseases
    • Ajees A.A., Anantharamaiah G.M., Mishra V.K., Hussain M.M., and Murthy H.M.K. Crystal structure of human apolipoprotein A-I: insights into its protective effect against cardiovascular diseases. Proc. Natl. Acad. Sci. U.S.A. 103 (2006) 2126-2131
    • (2006) Proc. Natl. Acad. Sci. U.S.A. , vol.103 , pp. 2126-2131
    • Ajees, A.A.1    Anantharamaiah, G.M.2    Mishra, V.K.3    Hussain, M.M.4    Murthy, H.M.K.5
  • 33
    • 0029761131 scopus 로고    scopus 로고
    • Interaction of model class A1, class A2, and class Y amphipathic helical peptides with membranes
    • Mishra V.K., and Palgunachari M.N. Interaction of model class A1, class A2, and class Y amphipathic helical peptides with membranes. Biochemistry 35 (1996) 11210-11220
    • (1996) Biochemistry , vol.35 , pp. 11210-11220
    • Mishra, V.K.1    Palgunachari, M.N.2
  • 34
    • 0023664091 scopus 로고
    • The role of apolipophorin III in vivo lipoprotein interconversions in adult Manduca sexta
    • Wells M.A., Ryan R.O., Kawooya J.K., and Law J.H. The role of apolipophorin III in vivo lipoprotein interconversions in adult Manduca sexta. J. Biol. Chem. 262 (1987) 4172-4176
    • (1987) J. Biol. Chem. , vol.262 , pp. 4172-4176
    • Wells, M.A.1    Ryan, R.O.2    Kawooya, J.K.3    Law, J.H.4
  • 37
    • 0026455019 scopus 로고
    • Organization of phosphatidylcholine and sphingomyelin in the surface monolayer of low density lipoprotein and lipoprotein(a) as determined by time-resolved fluorometry
    • Sommer A., Prenner E., Gorges R., Stütz H., Grillhofer H., Kostner G.M., Paltauf F., and Hermetter A. Organization of phosphatidylcholine and sphingomyelin in the surface monolayer of low density lipoprotein and lipoprotein(a) as determined by time-resolved fluorometry. J. Biol. Chem. 267 (1992) 24217-24222
    • (1992) J. Biol. Chem. , vol.267 , pp. 24217-24222
    • Sommer, A.1    Prenner, E.2    Gorges, R.3    Stütz, H.4    Grillhofer, H.5    Kostner, G.M.6    Paltauf, F.7    Hermetter, A.8
  • 38
    • 0031914422 scopus 로고    scopus 로고
    • Fluorescence studies of exchangeable apolipoprotein-lipid interactions. Superficial association of apolipophorin III with lipoprotein surfaces
    • Sahoo D., Narayanaswami V., Kay C.M., and Ryan R.O. Fluorescence studies of exchangeable apolipoprotein-lipid interactions. Superficial association of apolipophorin III with lipoprotein surfaces. J Biol. Chem. 273 (1998) 1403-1408
    • (1998) J Biol. Chem. , vol.273 , pp. 1403-1408
    • Sahoo, D.1    Narayanaswami, V.2    Kay, C.M.3    Ryan, R.O.4
  • 40
    • 0027286472 scopus 로고
    • Calorimetric and spectroscopic studies of the interaction of Manduca sexta apolipophorin III with zwitterionic, anionic, and nonionic lipids
    • Zhang Y., Lewis R.N.A.H., McElhaney R.N., and Ryan R.O. Calorimetric and spectroscopic studies of the interaction of Manduca sexta apolipophorin III with zwitterionic, anionic, and nonionic lipids. Biochemistry 32 (1993) 3942-3952
    • (1993) Biochemistry , vol.32 , pp. 3942-3952
    • Zhang, Y.1    Lewis, R.N.A.H.2    McElhaney, R.N.3    Ryan, R.O.4
  • 41
    • 0026535754 scopus 로고
    • Insect apolipophorin III: interaction of locust apolipophorin III with diacylglycerol
    • Demel R.A., Van Doorn J.M., and Van der Horst D.J. Insect apolipophorin III: interaction of locust apolipophorin III with diacylglycerol. Biochim. Biophys. Acta. 1124 (1992) 151-158
    • (1992) Biochim. Biophys. Acta. , vol.1124 , pp. 151-158
    • Demel, R.A.1    Van Doorn, J.M.2    Van der Horst, D.J.3


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