Hepatic lipase may act as a ligand in the uptake of artificial chylomicron remnant-like particles by isolated rat hepatocytes.
Active and heat-inactivated hepatic lipase stimulated to a statistically comparable extent the uptake of chylomicron remnant-like particles by isolated rat hepatocytes by 3-fold and 2.3-fold respectively and, likewise, their binding to hepatic plasma membranes by 5-fold and 4-fold respectively. Hepatic lipase may facilitate uptake of these particles, not only as a lipolytic enzyme, but also as a ligand anchored to extracellular glycosaminoglycans.
Diard
P
P
Laboratoire de Physiopathologie de la Nutrition, Inserm U177, Institut des Cordeliers, Paris, France.
Malewiak
M I
MI
Lagrange
D
D
Griglio
S
S
D000818:Animals; D001057:Apolipoproteins E / Q000378:metabolism; D002462:Cell Membrane / Q000378:metabolism; D002914:Chylomicrons / Q000378:metabolism*; D019763:Heparin Lyase; D006358:Hot Temperature; D008024:Ligands; D008049:Lipase / Q000037:antagonists & inhibitors / Q000378:metabolism*; D008099:Liver / Q000166:cytology / Q000187:drug effects / Q000201:enzymology*; D008297:Male; D011133:Polysaccharide-Lyases / Q000378:metabolism; D051381:Rats; D011924:Rats, Zucker; D013498:Suramin / Q000494:pharmacology
D001057:Apolipoproteins E; D002914:Chylomicrons; D008024:Ligands; D013498:Suramin; D008049:Lipase; D011133:Polysaccharide-Lyases; D019763:Heparin Lyase