Apolipoprotein A‐I structure in high‐density lipoproteins

References

• Jonas A. Lipoprotein Structure. Biochemistry of Lipids, Lipoproteins and Membranes, D. E Vance, J. E Vance. Elsevier Science, New York 2002; 483–504
   Google Scholar
• Brouillette C. G., Anantharamaiah G. M. Structural models of human apolipoprotein A‐I:. Biochim Biophys Acta 1995; 1256: 103–29
   PubMed Web of Science ®Google Scholar
• Brouillette C. G., Anantharamaiah G. M., Engler J. A., Borhani D. W. Structural models of human apolipoprotein A‐I: a critical analysis and review. Biochim Biophys Acta 2001; 1531: 4–46
   PubMed Web of Science ®Google Scholar
• Blanco‐Vaca F., Escola‐Gil J. C., Martin‐Campos J. M., Julve J. Role of apoA‐II in lipid metabolism and atherosclerosis: advances in the study of an enigmatic protein. J Lipid Res 2001; 42: 1727–39
   PubMedGoogle Scholar
• Escola‐Gil J. C., Marzal‐Casacuberta A., Julve‐Gil J., Ishida B. Y., Ordonez‐Llanos J., Chan L., et al. Human apolipoprotein A‐II is a pro‐atherogenic molecule when it is expressed in transgenic mice at a level similar to that in humans: evidence of a potentially relevant species‐specific interaction with diet. J Lipid Res 1998; 39: 457–62
   PubMedGoogle Scholar
• Kalopissis A. D., Pastier D., Chambaz J. Apolipoprotein A‐II: Beyond genetic associations with lipid disorders and insulin resistance. Curr Opin Lipidol 2003; 14: 165–72
   PubMedGoogle Scholar
• Rye K. A., Barter P. J. Formation and Metabolism of Prebeta‐Migrating, Lipid‐Poor Apolipoprotein A‐I. Arterioscler Thromb Vasc Biol 2003; 24: 421–8
   Google Scholar
• Vitello L. B., Scanu A. M. Studies on human serum high density lipoproteins. Self‐association of apolipoprotein A‐I in aqueous solutions. J Biol Chem 1976; 251: 1131–6
   Google Scholar
• Gursky O., Atkinson D. Thermal unfolding of human high‐density apolipoprotein A‐1: implications for a lipid‐free molten globular state. Proc Natl Acad Sci U S A 1996; 93: 2991–5
   PubMed Web of Science ®Google Scholar
• Borhani D. W., Rogers D. P., Engler J. A., Brouillette C. G. Crystal structure of truncated human apolipoprotein A‐I suggests a lipid‐bound conformation. Proc Natl Acad Sci U S A 1997; 94: 12291–6
   PubMed Web of Science ®Google Scholar
• Ajees A. A., Anantharamaiah G. M., Mishra V. K., Hussain M. M., Murthy H. M. Crystal structure of human apolipoprotein A‐I: Insights into its protective effect against cardiovascular diseases. Proc Natl Acad Sci U S A 2006; 103: 2126–31
   PubMed Web of Science ®Google Scholar
• Roberts L. M., Ray M. J., Shih T. W., Hayden E., Reader M. M., Brouillette C. G. Structural analysis of apolipoprotein A‐I: limited proteolysis of methionine‐reduced and ‐oxidized lipid‐free and lipid‐bound human apo A‐I. Biochemistry 1997; 36: 7615–24
   PubMed Web of Science ®Google Scholar
• Rogers D. P., Brouillette C. G., Engler J. A., Tendian S. W., Roberts L., Mishra V. K., et al. Truncation of the amino terminus of human apolipoprotein A‐I substantially alters only the lipid‐free conformation. Biochemistry 1997; 36: 288–300
   Google Scholar
• Wilson C., Wardell M. R., Weisgraber K. H., Mahley R. W., Agard D. A. Three‐dimensional structure of the LDL receptor‐binding domain of human apolipoprotein E. Science 1991; 252: 1817–22
   PubMedGoogle Scholar
• Wang J., Sykes B. D., Ryan R. O. Structural basis for the conformational adaptability of apolipophorin III, a helix‐bundle exchangeable apolipoprotein. Proc Natl Acad Sci U S A 2002; 99: 1188–93
   PubMed Web of Science ®Google Scholar
• Rogers D. P., Roberts L. M., Lebowitz J., Datta G., Anantharamaiah G. M., Engler J. A., et al. The lipid‐free structure of apolipoprotein A‐I: effects of amino‐terminal deletions. Biochemistry 1998; 37: 11714–25
   Google Scholar
• Fang Y., Gursky O., Atkinson D. Structural studies of N‐ and C‐terminally truncated human apolipoprotein A‐I. Biochemistry 2003; 42: 6881–90
   Google Scholar
• Silva R. A., Hilliard G. M., Fang J., Macha S., Davidson W. S. A Three‐Dimensional Molecular Model of Lipid‐Free Apolipoprotein A‐I Determined by Cross‐Linking/Mass Spectrometry and Sequence Threading. Biochemistry 2005; 44: 2759–69
   Google Scholar
• Leroy A., Jonas A. Native‐like structure and self‐association behavior of apolipoprotein A‐I in a water/n‐propanol solution. Biochim Biophys Acta 1994; 1212: 285–94
   Google Scholar
• Saito H., Lund‐Katz S., Phillips M. C. Contributions of domain structure and lipid interaction to the functionality of exchangeable human apolipoproteins. Prog Lipid Res 2004; 43: 350–80
   PubMed Web of Science ®Google Scholar
• Ji Y., Jonas A. Properties of an N‐terminal proteolytic fragment of apolipoprotein AI in solution and in reconstituted high density lipoproteins. J Biol Chem 1995; 270: 11290–7
   PubMed Web of Science ®Google Scholar
• Davidson W. S., Arnvig‐McGuire K., Kennedy A., Kosman J., Hazlett T. L., Jonas A. Structural organization of the N‐terminal domain of apolipoprotein A‐I: studies of tryptophan mutants. Biochemistry 1999; 38: 14387–95
   Google Scholar
• Lagerstedt J. O., Budamagunta M. S., Oda M. N., Voss J. C. Electron Paramagnetic Resonance Spectroscopy of Site‐directed Spin Labels Reveals the Structural Heterogeneity in the N‐terminal Domain of ApoA‐I in Solution. J Biol Chem 2007; 282: 9143–9
   Google Scholar
• Oda M. N., Forte T. M., Ryan R. O., Voss J. C. The C‐terminal domain of apolipoprotein A‐I contains a lipid‐sensitive conformational trigger. Nat Struct Biol 2003; 10: 455–60
   PubMedGoogle Scholar
• Matz C. E., Jonas A. Micellar complexes of human apolipoprotein A‐I with phosphatidylcholines and cholesterol prepared from cholate‐lipid dispersions. J Biol Chem 1982; 257: 4535–40
   PubMed Web of Science ®Google Scholar
• Jonas A., Kezdy K. E., Wald J. H. Defined apolipoprotein A‐I conformations in reconstituted high density lipoprotein discs. J Biol Chem 1989; 264: 4818–24
   PubMed Web of Science ®Google Scholar
• Jonas A., Zorich N. L., Kezdy K. E., Trick W. E. Reaction of discoidal complexes of apolipoprotein A‐I and various phosphatidylcholines with lecithin cholesterol acyltransferase. Interfacial effects. J Biol Chem 1987; 262: 3969–74
   Google Scholar
• Jonas A., Wald J. H., Toohill K. L., Krul E. S., Kezdy K. E. Apolipoprotein A‐I structure and lipid properties in homogeneous, reconstituted spherical and discoidal high density lipoproteins. J Biol Chem 1990; 265: 22123–9
   PubMed Web of Science ®Google Scholar
• Jonas A. Reconstitution of high‐density lipoproteins. Methods Enzymol 1986; 128: 553–82
   PubMed Web of Science ®Google Scholar
• Phillips J. C., Wriggers W., Li Z., Jonas A., Schulten K. Predicting the structure of apolipoprotein A‐I in reconstituted high‐density lipoprotein disks. Biophys J 1997; 73: 2337–46
   PubMed Web of Science ®Google Scholar
• Segrest J. P. Amphipathic helixes and plasma lipoproteins: thermodynamic and geometric considerations. Chem Phys Lipids 1977; 18: 7–22
   Google Scholar
• Segrest J. P., Jones M. K., Klon A. E., Sheldahl C. J., Hellinger M., De Loof H., et al. A detailed molecular belt model for apolipoprotein A‐I in discoidal high density lipoprotein. J Biol Chem 1999; 274: 31755–8
   PubMed Web of Science ®Google Scholar
• Klon A. E., Segrest J. P., Harvey S. C. Comparative models for human apolipoprotein A‐I bound to lipid in discoidal high‐density lipoprotein particles. Biochemistry 2002; 41: 10895–905
   Google Scholar
• Koppaka V., Silvestro L., Engler J. A., Brouillette C. G., Axelsen P. H. The structure of human lipoprotein A‐I. Evidence for the ‘belt’ model. J Biol Chem 1999; 274: 14541–4
   Google Scholar
• Panagotopulos S. E., Horace E. M., Maiorano J. N., Davidson W. S. Apolipoprotein A‐I adopts a belt‐like orientation in reconstituted high density lipoproteins. J Biol Chem 2001; 276: 42965–70
   Google Scholar
• Li H., Lyles D. S., Thomas M. J., Pan W., Sorci‐Thomas M. G. Structural determination of lipid‐bound ApoA‐I using fluorescence resonance energy transfer. J Biol Chem 2000; 275: 37048–54
   Google Scholar
• Tricerri M. A., Behling Agree A. K., Sanchez S. A., Bronski J., Jonas A. Arrangement of apolipoprotein A‐I in reconstituted high‐density lipoprotein disks: an alternative model based on fluorescence resonance energy transfer experiments. Biochemistry 2001; 40: 5065–74
   Google Scholar
• Davidson W. S., Hilliard G. M. The spatial organization of apolipoprotein A‐I on the edge of discoidal high density lipoprotein particles: A mass spectrometry study. J Biol Chem 2003; 278: 27199–207
   Google Scholar
• Silva R. A., Hilliard G. M., Li L., Segrest J. P., Davidson W. S. A Mass Spectrometric Determination of the Conformation of Dimeric Apolipoprotein A‐I in Discoidal High Density Lipoproteins. Biochemistry 2005; 44: 8600–7
   PubMed Web of Science ®Google Scholar
• Bhat S., Sorci‐Thomas M. G., Alexander E. T., Samuel M. P., Thomas M. J. Intermolecular contact between globular N‐terminal fold and C‐terminal domain of ApoA‐I stabilizes its lipid‐bound conformation: studies employing chemical cross‐linking and mass spectrometry. J Biol Chem 2005; 280: 33015–25
   PubMed Web of Science ®Google Scholar
• Martin D. D., Budamagunta M. S., Ryan R. O., Voss J. C., Oda M. N. Apolipoprotein A‐I assumes a ‘looped belt’ conformation on reconstituted high density lipoprotein. J Biol Chem 2006; 281: 20418–26
   Google Scholar
• Li H. H., Lyles D. S., Pan W., Alexander E., Thomas M. J., Sorci‐Thomas M. G. ApoA‐I structure on discs and spheres. Variable helix registry and conformational states. J Biol Chem 2002; 277: 39093–101
   Google Scholar
• Li L., Chen J., Mishra V. K., Kurtz J. A., Cao D., Klon A. E., et al. Double belt structure of discoidal high density lipoproteins: molecular basis for size heterogeneity. J Mol Biol 2004; 343: 1293–311
   Google Scholar
• Zorich N. L., Kezdy K. E., Jonas A. Properties of discoidal complexes of human apolipoprotein A‐I with phosphatidylcholines containing various fatty acid chains. Biochim Biophys Acta 1987; 919: 181–9
   Google Scholar
• Calabresi L., Meng Q. H., Castro G. R., Marcel Y. L. Apolipoprotein A‐I conformation in discoidal particles: evidence for alternate structures. Biochemistry 1993; 32: 6477–84
   PubMed Web of Science ®Google Scholar
• Maiorano J. N., Jandacek R. J., Horace E. M., Davidson W. S. Identification and structural ramifications of a hinge domain in apolipoprotein A‐I discoidal high‐density lipoproteins of different size. Biochemistry 2004; 43: 11717–26
   Google Scholar
• Minnich A., Collet X., Roghani A., Cladaras C., Hamilton R. L., Fielding C. J., et al. Site‐directed mutagenesis and structure‐function analysis of the human apolipoprotein A‐I. Relation between lecithin‐cholesterol acyltransferase activation and lipid binding. J Biol Chem 1992; 267: 16553–60
   Google Scholar
• Sorci‐Thomas M. G., Curtiss L., Parks J. S., Thomas M. J., Kearns M. W., Landrum M. The hydrophobic face orientation of apolipoprotein A‐I amphipathic helix domain 143–164 regulates lecithin:cholesterol acyltransferase activation. J Biol Chem 1998; 273: 11776–82
   Google Scholar
• Mishra V. K., Palgunachari M. N., Segrest J. P., Anantharamaiah G. M. Interactions of synthetic peptide analogs of the class A amphipathic helix with lipids. Evidence for the snorkel hypothesis. J Biol Chem 1994; 269: 7185–91
   PubMed Web of Science ®Google Scholar