Primary Lipoprotein Lipase Deficiency

  • John D. Brunzell
  • Per-Henrik Iverius
  • Mark S. Scheibel
  • Wilfred Y. Fujimoto
  • Michael R. Hayden
  • Roger McLeod
  • Jiri Frolich
Part of the Advances in Experimetal Medicine and Biology book series (AEMB, volume 201)


The enzyme lipoprotein lipase (LPL) is a glycoprotein located on the luminal surface of capillary endothelial cells (see reviews: 1–4). It is bound to a glycosaminoglycan on the endothelium, can be displaced into plasma by intravenous heparin or other polyanions, and binds to heparin-Sepharose gels. The enzyme has an apparent monomeric molecular weight on SDS gel of over 60,000 and 48,300 by sedimentation-equilibrium ultracentrifugation, and probably functions as a dimer in vivo. It has binding sites for heparin, for the cofactor apolipoprotein CII, and for lipid, and has a separate catalytic site for triglyceride hydrolysis. It is inhibited by serine proteases inhibitors, by protamine, and by high ionic strength. The enzyme appears to be synthesized in a number of different parenchymal cells including monocyte-derived macrophages, Kupfer cells, adipocytes, and cells in cardiac and skeletal muscle. The enzyme is secreted from the adipocyte and transported in an unknown fashion to the plasma surface of the capillary endothelial cell, where it has several functions in humans.


Lipoprotein Lipase Lipoprotein Lipase Activity High Density Lipopro Postheparin Plasma Adipose Tissue Lipoprotein Lipase 
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Copyright information

© Springer Science+Business Media New York 1986

Authors and Affiliations

  • John D. Brunzell
    • 1
  • Per-Henrik Iverius
    • 1
  • Mark S. Scheibel
    • 1
  • Wilfred Y. Fujimoto
    • 1
  • Michael R. Hayden
    • 2
  • Roger McLeod
    • 2
  • Jiri Frolich
    • 2
  1. 1.University of WashingtonSeattleUSA
  2. 2.University of British ColumbiaVancouverCanada

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