Advertisement

Localization and Function of Lipases and their Reaction Products in Rat Heart

  • W. C. Hülsmann
  • H. Stam
  • J. M. J. Lamers

Abstract

Lipoprotein lipase is involved in catabolism of circulating triglycerides. Its function is exerted at the vascular endothelial surface, where the enzyme is bound and from which the enzyme is released by heparin perfusion (1–3). Natural substrates that may be used include chylomicrons and very low density lipoproteins, while artificial substrates include triglyceride-filled liposomes with phospholipid and apolipoprotein C-II on the surface. The enzyme is an -lipase that also hydrolyzes 1-acylglycerol esters of partial glycerides and phospholipids. In perfused hearts of fed rats, only about 25% of the tissue lipoprotein lipase is removed by heparin perfusion while the ability of the heart to catabolize chylomicrons is largely lost (2, 4). The study of Schotz et al. (5), who perfused rat hearts with an antibody against heart lipoprotein lipase, led to the observation that subsequent perfusion with 14C-labelled chylomicron triglyceride no longer resulted in 14CO2 formation, suggesting also that endothelial surface lipoprotein lipase, accessible to the antibody, is the functionally active fraction of the enzyme.

Keywords

Free Fatty Acid Lipoprotein Lipase Erucic Acid Lipoprotein Lipase Activity Partial Glyceride 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

Preview

Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.

References

  1. 1.
    Robinson, D.S. (1970): Comprehensive Biochem. 18: 51.Google Scholar
  2. 2.
    Fielding, C.J., & Havel, R.J. (1977): Arch. Pathol. Lab. Med. 101: 225.PubMedGoogle Scholar
  3. 3.
    Nilsson-Ehle, P., Garfinkel, A.S., & Schotz, M.C. (1980): Ann. Rev, Biochem. 49: 667.CrossRefGoogle Scholar
  4. 4.
    Fielding, C.J., & Higgins, J.M. (1974): Biochemistry 13: 4324.PubMedCrossRefGoogle Scholar
  5. 5.
    Schotz, M.C., Twu, J.-S., Pedersen, M.E., Chen, C.-II., Garfinkel, A.S., & Borensztajn, J. (1977): Biochim. Biophys. Acta 489: 214.PubMedGoogle Scholar
  6. 6.
    Stoke, K.T., Fjeld, N.B., Kluge, T.H., & Skrede, S. (1974): Scand. J. Clin. Lab. Invest. 33: 199.CrossRefGoogle Scholar
  7. 7.
    Roy, P.-E. (1975): IN Recent Advances in Studies on Cardiac Structure and Metabolism. Vol. 10. (eds) P.-E. Roy, & G. Rona, University Park Press, Baltimore, p. 17.Google Scholar
  8. 8.
    Stam, H., Jansen, H., & Hülsmann, W.C (1980): Biochem. Biophys. Res. Commun. 96: 899.PubMedCrossRefGoogle Scholar
  9. 9.
    Julien, P., Downar, E., & Angel, A. (1981): Circ. Res. 49: 48.Google Scholar
  10. 10.
    Julien, P., & Angel, A. (1981): Can. J. Biochem. 59: 709.PubMedCrossRefGoogle Scholar
  11. 11.
    Jansen, H., Stam, H., Kalkman, C., & Hülsmann, W.C. (1980): Biochem. Biophys. Res. Commun. 92: 411.PubMedCrossRefGoogle Scholar
  12. 12.
    Külsmann, W.C., Stam, H., & Breeman, W.A.P. (1982): Biochem. Biophys. Res. Commun. 108: 371.CrossRefGoogle Scholar
  13. 13.
    Hülsmann, W.C., & Stam, H. (1978): Biochem. Biophys. Res. Commun. 82: 53.PubMedCrossRefGoogle Scholar
  14. 14.
    Jansen, H., Hülsmann, W.C., van Zuylen-Van, Wiggen, A., Struijk, C.B., & Houtsmuller, U.M.T. (1975): Biochem. Biophys. Res. Commun. 64: 747.PubMedCrossRefGoogle Scholar
  15. 15.
    Hülsmann, W.C., Geelhoed-Mieras, M.M., Jansen, H., & Houtsmuller, U.M.T. (1979): Biochim. Biophys. Acta 572: 183.PubMedGoogle Scholar
  16. 16.
    Christopherson, B.O., & Bremer, J. (1972): Biochim. Biophys. Acta 280: 506.Google Scholar
  17. 17.
    Idell-Wenger, J.A., Grotyohann, L.W., & Neely, J.R. (1978): J. Biol. Chem. 253: 4310.PubMedGoogle Scholar
  18. 18.
    Shug, A.L., Tomsen, J.H., Folts, J.D., Bittar, N., Klein, M.I., Koker, J.R., & Huth, P.J. (1978): Arch. Biochem. Biophys. 187: 25.PubMedCrossRefGoogle Scholar
  19. 19.
    van der Vusse, G.J., Roemen, T.M., Prinzen, F.W., & Reneman, R.S. (1981): Basic Res. Cardiol. 76: 389.PubMedCrossRefGoogle Scholar
  20. 20.
    Stam, H., & Hülsmann, W.C. (1981): Biochem. Int. 2: 477.Google Scholar
  21. 21.
    De Deckere, E.A.M., & Ten Hoor, F. (1975): Pflugers Archiv. 370: 103.Google Scholar
  22. 22.
    Crass, M.F. III, Shipp, J.C., & Pieper, G.M. (1975): Am. J. Physiol. 228: 618.PubMedGoogle Scholar
  23. 23.
    Hron, W.T., Jesmok, G.J., Lombardo, Y.B., Menahan, L.A., & Lech, J.J. (1977): J. Mol. Cell. Cardiol. 9: 733.PubMedCrossRefGoogle Scholar
  24. 24.
    Stam, H., Geelhoed-Mieras, M.M., & Hülsmann, W.C. (1980): Lipids 15: 242.PubMedCrossRefGoogle Scholar
  25. 25.
    Hülsmann, W.C., & Stam, H. (1983): Basic Res. Cardiol. In press.Google Scholar
  26. 26.
    Hülsmann, W.C., & Stam, H. (1980): Biochem. Biophys. Res. Commun. 88: 867.CrossRefGoogle Scholar
  27. 27.
    Hülsmann, W.C., Stam, H., & Geelhoed-Mieras, M.M. (1979): IN Obesitas. Cellular and Molecular Aspects, Vol. 87 (ed) G. Ailhaud, INSERM, Paris, p. 179.Google Scholar
  28. 28.
    Stam, H., & Hülsmann, W.C. (1982): IN Advances in Myocardiology, Vol. 3 (eds) E. Chazov, V. Smirnov, & N.S. Dhalla, Plenum Publishing Corp., New York, p. 499.Google Scholar
  29. 29.
    Bundgaard, M., Hagman, P., & Crone, C. (1983): Microvascular Res. 25: 358.CrossRefGoogle Scholar
  30. 30.
    Henson, L.C., Schotz, M.C., & Harary, I. (1977): Biochim. Biophys. Acta 487: 212.PubMedGoogle Scholar
  31. 31.
    Chajek-Shaul, T., Friedman, G., Stein, O., Olivecrona, T., & Stein, Y. (1982): Biochim. Biophys. Acta 712: 200.PubMedGoogle Scholar
  32. 32.
    Hülsmann, W.C., Stam, H., & Maccari, F. (1982): Biochim. Biophys. Acta 713: 39.PubMedGoogle Scholar
  33. 33.
    Morgan, H.E., Regen, D.M., & Park, C.R. (1964): J. Biol. Chem. 239: 369.PubMedGoogle Scholar
  34. 34.
    Owens, K., Kennett, F.F., & Weglicki, W.B. (1982): Am. J. Physiol. 242: H456.PubMedGoogle Scholar
  35. 35.
    Harmsen, E., De Tombe, P.Ph., & De Jong, J.W. (1982): J. Chromatography 230: 131.CrossRefGoogle Scholar
  36. 36.
    Pearson, D.J., Chase, J.F.A., & Tubbs, P.K. (1969): IN Methods in Enzymology, Vol. 14 (eds) S.P. Colowick, N.O. Kaplan, & J.M. Lowenstein, Academic Press, New York, p. 612.Google Scholar
  37. 37.
    Christiansen, R.Z., & Bremer, J. (1978): FEBS Lett. 86: 99.PubMedCrossRefGoogle Scholar
  38. 38.
    Reeves, J.P., & Sutko, J.L. (1979): Proc. Natl. Acad. Sci. USA 76: 590.PubMedCrossRefGoogle Scholar
  39. 39.
    Cross, R.W., & Sobel, B.E. (1983): J. Biol. Chem. 258: 5221.Google Scholar
  40. 40.
    Lamers, J.M.J., & Hülsmann, W.C. (1977): J. Mol. Cell. Cardiol. 9: 343.PubMedCrossRefGoogle Scholar
  41. 41.
    McMi11in-Wood, J., Bush, B., Pitts, B.J.R., & Schwartz, A. (1977): Biochem. Biophys. Res. Commun. 74: 677.CrossRefGoogle Scholar
  42. 42.
    Hülsmann, W.C. (1976): Basic Res. Cardiol. 71: 179.PubMedCrossRefGoogle Scholar
  43. 43.
    Stam, H., & Kulsmann, W.C. (1978): Biochem. Biophys. Res. Commun. 82: 609.PubMedCrossRefGoogle Scholar
  44. 44.
    Rhoads, D.E., Ockner, R.K., Peterson, N.A., & Raghupathy, E. (1983): Biochemistry 22: 1965.PubMedCrossRefGoogle Scholar
  45. 45.
    Dhalla, N.S. (1976): J. Mol. Cell. Cardiol. 9: 661.CrossRefGoogle Scholar
  46. 46.
    Farber, J.L. (1982): Lab. Invest. 47: 114.PubMedGoogle Scholar
  47. 47.
    Clusin, W.T., Buchbinder, M., & Harrison, D.C. (1983): Lancet i: 272.CrossRefGoogle Scholar

Copyright information

© Plenum Press, New York 1984

Authors and Affiliations

  • W. C. Hülsmann
    • 1
  • H. Stam
    • 1
  • J. M. J. Lamers
    • 1
  1. 1.Department of Biochemistry IErasmus UniversityRotterdamThe Netherlands

Personalised recommendations