Apoprotein S Versus SAA Protein

  • C. L. Malmendier
  • J. P. Ameryckx


Intravenous glucose infusions into neurological patients and post-surgery patients increased dramatically the amount of new polypeptides associated with high density lipoproteins, reaching up to 40% of total apoproteins whereas plasmas of normal subjects fed a regular diet contained only traces of these peptides (0.1%). This increase was observed in HDL2 as well as in HDL3 and also in very low density lipoproteins. Eight polymorphic forms of these new apoproteins named S (sugar induced) were isolated and defined by successive gel chromatography, ion-exchange chromatography, polyacrylamide gel electrophoresis and isoelectric focusing. Apoprotein S did not react with antisera prepared to apo B, apo C, apo A-I and apo A-II, but S4 and S5 gave a positive reaction with anti SAA.

Polypeptides S4 and S5 were recognized to have a high affinity for artificial lipid complexes. The change in the microviscosity of the apoprotein S-dimyristosyl-phosphatidylcholine and apo S-DMPC-cholesterol complexes with temperature, was similar to that observed for apo A-II and a stable complex might be isolated by sepharose 4B chromatography.

The simultaneous appearance of radioactivity into apoproteins S and other apoproteins of HDL (A-I, A-II and C) after the intravenous injection of l-14 C-leucine suggests a common hepatic origin.

Aminoacid composition and partial sequence of apoprotein S were almost identical to those of SAA protein. Similarities and differences between apoprotein S and SAA protein are discussed. The putative precursor role played by apoprotein S in the formation of amyloid may build a link between glucose supply in the diet and tissue deposits observed in atherosclerosis.


High Density Lipoprotein Glucose Infusion Partial Amino Acid Sequence Lipid Research Clinic Program Human High Density 
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Abbreviations and Nomenclature


very low density lipoproteins (d < 1.006 g/ml)


high density lipoproteins (d=l.063-1.210 g/ml)

HDL2 and HDL3

respectively d=l.063-1.125 and 1.125-1.210 g/ml

Apoprotein Sx

replaces SV-Dx and means Subfraction x of DEAE cellulose chromatography of Fraction V obtained from Sephacryl S-200 chromatography of HDL apoproteins


polyacrylamide gel electrophoresis


serum amyloid A protein


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  1. 1.
    Malmendier, C.L., Christophe, J. and Amerychx, J.P. Separation and partial characterization of new apoproteins from human plasma high density lipoproteins. Clin. Chim. Acta 99: 167–176, 1979PubMedCrossRefGoogle Scholar
  2. 2.
    Malmendier, L., Paroutaud, P. and Amerychx, J.P. Partial amino acid sequence of three new apolipoproteins isolated from high density lipoproteins. FEBS lett. 109: 43–44, 1980PubMedCrossRefGoogle Scholar
  3. 3.
    Malmendier, C.L. and Amerychx, J.P.S-peptides. New apoproteins of human high density lipoproteins induced by glucose infusions. Short communication. Clin. Chim. Acta, 111: 267–270, 1981.PubMedCrossRefGoogle Scholar
  4. 4.
    Schacterle, G.R. and Pollack, R.L.A simplified method for the quantitative assay of small amounts of protein in biologic material. Anal. Biochem. 51 654–655, 1973PubMedCrossRefGoogle Scholar
  5. Manual of Laboratory Operations, Lipid Research Clinics Program, Vol. 1 “Lipid and lipoprotein analysis” DHEW Publ. No. (NIH) 75–628, 1974Google Scholar
  6. 6.
    SchonfeTd, G. and Pfleger, B. The structure of human high density lipoprotein and the levels of apolipoprotein A-I in plasma as determined by radioimunoassay. J. Clin. Invest. 54: 236–246, 1974PubMedCrossRefGoogle Scholar
  7. 7.
    Schonfeld, G.,Lees, R. S., George, P.K. and Prieger, B. Assay of total plasma apolipoprotein B concentration in human subjects. J. Clin. Invest. 53: 1458–1467, 1974PubMedCrossRefGoogle Scholar
  8. 8.
    Rosseneu, M., van Tornout, P., Lievens, M-J., Amerychx,J.P and Malmendier, C.L. Lipid binding properties of apo S5 protein. Kinetics of association and complex isolation. Eur. J. Biochem. 1981. Submitted.Google Scholar
  9. 9.
    Anker, H.S. A solubilizable acrylamide gel for electrophoresis. FEBS Lett: 293, 1970Google Scholar
  10. 10.
    Albers, J.J., Warnick, G.R. and Chenng, M.C. Quantitation of high density lipoproteins. Lipids 13: 926–923, 1978PubMedCrossRefGoogle Scholar
  11. 11.
    Schonfeld, G., Bailey, A. and Steelman, R. Plasma apolipoprotein A-i and A-II levels in hyperlipidemia Lipids 13: 951–959, 1978Google Scholar
  12. 12.
    Scanu, A.M. In: The biochemistry of atherosclerosis ( Scanu, A.M. ed.), Dekker, New York, 1979Google Scholar
  13. 13.
    Alaupovic, P., Curry, M., McConathy, W. and Fesmi re, J. Electroimmunoassay of apolipoproteins occurring in high density lipoproteins of human plasma. Report of the high density lipoprotein methodology worshop. US Department of Health, NIH Publication No. 79–1661, 1979Google Scholar
  14. 14.
    Blum, c:b., Levy, R.I., Eisenberg, S., Hall, M., Goebel, R.H. and Berman, M. High density lipoprotein metabolism in man. J. Clin.Invest. 60:795–807, 1977Google Scholar
  15. 15.
    Malmendier, C.L., Amerychx, J.P. and van den Bergen, C.J. Sequence of 1–14 C-leucine and 9,10-3H-palmitate incorporation into lipoprotein apoproteins and triglycerides in man. Proc. of 25 th colloquium on protides of the biological fluids (H. Peeters, ed.). Pergamon Press Oxford and New York, 1978, pp. 167–170Google Scholar
  16. 16.
    Segrest, J.P., Pownall, H. J., Jackson, R.L., Glenner, G.G. and Pollack, P.S. Amyloid A: Amphipathic helixes and lipid binding, Biochemistry 15: 3187–3191, 1976PubMedCrossRefGoogle Scholar
  17. 17.
    Malmendier, C.L. and Ameryckx, J.P. L’apoprotéine S. Sa structure, son origine, sa fonction, sa destinée, ses implicatioris possibles en pathologie. Exposés annuels de biochimie médicale. Paris, 1981. InPress.Google Scholar
  18. 18.
    Shore, V.G., Shore, B. and Lewis, S.B. Isolation and characterization of two threonine-poor apolipoproteins of human plasma high density lipoproteins. Biochemistry 17: 2174–2179, 1978PubMedCrossRefGoogle Scholar
  19. 19.
    Levin, M., Franklin, E.C., Frangione, B. and Pras, M. The amino acid sequence of a malor non immunoglubin component of some amyloid fibrils. J. Clin. Invest. 51: 2773–2776, 1972PubMedCrossRefGoogle Scholar
  20. 20.
    Benditt, E.P., Eriksen, N. and Hoffman, J.S. Origin of protein AA. Symposium on amyloidosis. Portugal, 23–28 September 1979Google Scholar
  21. 21.
    Segrest, J.P., Jackson, R.L., Morrisett, J.D. and Gotto, A.M. A molecular theory of lipid-protein interactions in the plasma!ipoproteins. FEBS Lett. 38: 247–253, 1974PubMedCrossRefGoogle Scholar

Copyright information

© Plenum Press, New York 1985

Authors and Affiliations

  • C. L. Malmendier
    • 1
  • J. P. Ameryckx
    • 1
  1. 1.Research Unit on Atherosclerosis, Laboratory of Chemical PathologyFree University of BrusselsBrusselsBelgium

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