Primary lipoprotein lipase deficiency
JD Brunzell, PH Iverius, MS Scheibel… - Lipoprotein deficiency …, 1986 - Springer
Lipoprotein deficiency syndromes, 1986•Springer
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 …
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 …
Abstract
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.
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