Relationship Between Structure and Metabolism of HDL Apolipoproteins; Study with Synthetic Peptides

  • Gabriel Ponsin
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 243)

Abstract

In blood, lipids are transported in complex structures referred to as lipoproteins. These are formed of a monomolecular surface of phospholipids surrounding a core of neutral lipids (cholesterol esters and triglycerides)1. The polar phospholipid surface contains unesterified cholesterol and apolipoproteins. Apolipoproteins play several roles which may be summarized as follows:
  • They participate to the structural stability and to the solubility of lipoprotein particles.

  • Certain apolipoproteins act as effectors of lipolytic enzymes2,3.

  • Apolipoproteins may be recognized by specific receptors4–7.

Keywords

Cholesterol Lipase Electrophoresis Serine Proline 

Preview

Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.

References

  1. 1.
    L.C. Smith, H.J. Pownall, and A.M. Gotto Jr., The plasma lipoproteins. Structure and metabolism, Ann. Rev. Biochem. 47:751 (1978).,PubMedCrossRefGoogle Scholar
  2. 2.
    C.J. Fielding, V.G. Shore, and P.E. Fielding, A protein co-factor of lecithin : cholesterol Acyltransferase, Biochem. Biophys. Res. Commun. 47:1493 (1972).CrossRefGoogle Scholar
  3. 3.
    J.C. Larosa, R.I. Levy, P.N. Herbert, S.E. Lux, and D.S. Fredrickson, A specific apoprotein activator for lipoprotein lipase, Biochem. Biophys. Res. Commun. 41:57 (1970).PubMedCrossRefGoogle Scholar
  4. 4.
    J.L. Goldstein, M.S. Brown, The low density lipoprotein pathway and its relation to atherosclerosis, Ann. Rev. Biochem. 46:897(1977).Google Scholar
  5. 5.
    R.W. Mahley, D.Y. Hui, T.L. Innerarity, and K.H. Weisgraber, Two independent lipoprotein receptors on hepatic membranes of dog, swine and man. Apo-B, E and Apo : E receptors, J. Clin. Invest. 68:1197(1981).PubMedCrossRefGoogle Scholar
  6. 6.
    R. Biesbroeck, J.R. Oram, J.J. Albers, and E.L. Bierman, Specific high affinity binding of high density lipoproteins to cultured human skin fibroblasts and arterial smooth muscle cells, J. Clin. Invest.71: 525 (1983).PubMedCrossRefGoogle Scholar
  7. 7.
    N.M. Fidge, and P.J. Nestel, Identification of apolipoproteins involved in the interaction of human high density lipoprotein 3 with receptors on cultured cells, J. Biol. Chem. 260:3570 (1985).PubMedGoogle Scholar
  8. 8.
    J.P. Segrest, R.L. Jackson, J.D. Morrisett, and A.M. Gotto, Jr., A molecular theory of lipid-protein interactions in the plasma lipoproteins, FEBS Lett. 38:247 (1974).PubMedCrossRefGoogle Scholar
  9. 9.
    H.J. Pownall, J.B. Massey, S.K. Kusserow, and A.M. Gotto Jr., Kinetics of lipid-protein interactions. Interaction of apolipoprotein A-I from human plasma high density lipoproteins with phosphatidylcholines, Biochemistry 17:1183 (1978).PubMedCrossRefGoogle Scholar
  10. 10.
    H.J. Pownall, D. Hickson, and A.M. Gotto, Jr., The free energy of association of lecithin with reduced and carboxymethylated apolipoprotein A-II from human plasma high density lipoprotein, J. Biol. Chem. 256:9849 (1981).PubMedGoogle Scholar
  11. 11.
    S. Yokoyama, D. Fukushima, J.P. Kupferberg F.J. Kezdy, and E.T. Kaiser, The mechanism of activation of lecithin:cholesterol acyltransferase by apolipoprotein A-I and an amphiphilic peptide, J. Biol Chem. 255:7333 (1980).PubMedGoogle Scholar
  12. 12.
    H.J. Pownall, A.M. Gotto Jr., and J.T. Sparrow, Thermodynamics of lipid-protein association and the activation of lecithin:cholesterol acyltransferase by synthetic model apolipopeptides, Biochim. Biophys. Acta 763:149 (1984).Google Scholar
  13. 13.
    G. Ponsin, K. Strong, A.M. Gotto, Jr., J.T. Sparrow, H.J. Pownall, In vitro binding of synthetic acylated lipid associating peptides to high density lipoproteins. Effects of hydrophobicity, Biochemistry 23: 5337 (1984).PubMedCrossRefGoogle Scholar
  14. 14.
    G. Ponsin, L. Hester, A.M. Gotto, Jr., H.J. Pownall, and J.T. Sparrow, Lipid-peptide association and activation of lecithin:cholesterol acyltransferase : effect of helicity, J. Biol. Chem. 261:9202 (1986).PubMedGoogle Scholar
  15. 15.
    P. Kanellis, A.Y. Romans, B.J. Johnson, H. Kercret, R. Chiovetti Jr., T.M. Allen, and J.P. Segrest, Studies of synthetic peptide analogs of the amphipathic helix. Effect of charged amino-acid residue topography on lipid affinity, J. Biol. Chem. 255:11464 (1980).PubMedGoogle Scholar
  16. 16.
    J.P. Segrest, B.H. Chung, C.G. Brouillette, P. Kanellis, and R. Mc Gahan, Studies of synthetic peptide analogs of the amphipathic helix. Competitive displacement of exchangeable apolipoproteins from native lipoproteins, J. Biol. Chem. 258:2290 (1983).PubMedGoogle Scholar
  17. 17.
    G.M. Anantharamaiah, J.L. Jones, C.G. Brouillette, C.F. Schmidt, B.H. Chung, T.A. Hughes, A.S. Bhown, and J.P. Segrest, Studies of synthetic peptide analogs of the amphipathic helix, J. Biol. Chem. 260:10248 (1985).PubMedGoogle Scholar
  18. 18.
    B.H. Chung, G.M. Anantharamaiah, C.G. Brouillette, T. Nishida, and J.P. Segrest, Studies of synthetic peptide analogs of the amphipathic helix. Correlation of structure with function, J. Biol. Chem. 260:10256 (1985).PubMedGoogle Scholar
  19. 19.
    G.M. Anantharamaiah, Synthetic peptide analogs of apolipoproteins,in: Methods in Enzymology, Plasma lipoproteins, part A, vol. 128, J.P. Segrest and J.J. Albers, eds., Academic Press, Inc. (1986).Google Scholar
  20. 20.
    H.J. Pownall, A. Hu, A.M. Gotto, Jr., J.J. Albers, and J.T. Sparrow, Activation of lecithin:cholesterol acyltransferase by a synthetic model lipid-associating peptides, Proc. Natl. Acad. Sci. USA 77:3154 (1980).PubMedCrossRefGoogle Scholar
  21. 21.
    R.M. Epand, A. Gawish, M. Iqbal, K.B. Gupta, C.H. Chen, J.P. Segrest, and G.M. Anantharamaiah, Studies of synthetic peptide analogs of the amphipathic helix. Effect of charge distribution, hydrophobicity, and secondary structure on lipid association and lecithin cholesterol acyltransferase activation, J. Biol. Chem. 262:9389 (1987).PubMedGoogle Scholar
  22. 22.
    G. Ponsin, J.T. Sparrow, A.M. Gotto Jr., and H.J. Pownall, In vivo interaction of synthetic acylated apopeptides with high density lipoproteins in rat, J. CI in. Invest. 77:559 (1986).CrossRefGoogle Scholar
  23. 23.
    G. Ponsin, and H.J. Pownall, Equilibrium of apoproteins between high density lipoprotein and the aqueous phase : modelling of in vivo metabolism, J. Theor. Biol. 112:183 (1985).PubMedCrossRefGoogle Scholar
  24. 24.
    S.J.T. Mao, J.T. Sparrow, E.B. Gilliam, A.M. Gotto Jr., and R.L. Jackson, Mechanism of lipid-protein interaction in the plasma lipoproteins lipid-binding properties of synthetic fragments of apolipoprotein A-II, Biochemistry 16:4150 (1977).PubMedCrossRefGoogle Scholar
  25. 25.
    A. Fukushima, S. Yokoyama, A.J. Kroon, F.J. Kezdy, and E.T. Kaiser, Chain length function correlation of amphiphilic peptides. Synthesis and surface properties of a tetratetracontrapeptide segment of apolipoprotein A-I, J. Biol. Chem. 255:10651 (1980).PubMedGoogle Scholar
  26. 26.
    S.C. Rail, Jr., K.H. Weisgraber, R.W. Mahley, Y. Ogama, C.J. Fielding, G. Utermann, J. Haas, A. Steinmetz, H.J. Menzel, and G. Assmann, Abnormal lecithin : cholesterol acyltransferase activation by a human apolipoprotein A-I variant in which a single lysine residue is deleted, J. Biol. Chem. 259:10063 (1984).Google Scholar
  27. 27.
    G. Ponsin, A.M. Gotto, Jr., G. Utermann, and H.J. Pownall, Abnormal interaction of the human apolipoprotein A-I variant (Lys 107→ 0) with high density lipoprotein, Biochem. Biophys. Res. Commun. 133:856 (1986).CrossRefGoogle Scholar

Copyright information

© Plenum Press, New York 1988

Authors and Affiliations

  • Gabriel Ponsin
    • 1
  1. 1.INSERM U. 197Laboratoire de Métabolisme des LipidesLyonFrance

Personalised recommendations