Chylomicrons and lipoprotein lipase at the endothelial surface: bound and GAG-ged?
At the endothelial cell surface, binding of chylomicrons and lipoprotein lipase (LpL), the major enzyme involved in the processing of these triglyceride-rich lipoproteins, is thought to involve electrostatic interactions with glycosaminoglycans. A new study published in this issue of Cell Metabolism (Beigneux et al., 2007) provides evidence for a specific chylomicron/LpL receptor, which may serve as a platform for LpL-mediated processing of chylomicrons on the capillary endothelium.
Ory
Daniel S
DS
Department of Medicine, Washington University School of Medicine, 660 South Euclid Avenue, St. Louis, MO 63110, USA. dory@wustl.edu
D000818:Animals; D002478:Cells, Cultured; D002914:Chylomicrons / Q000378:metabolism*; D004730:Endothelium, Vascular / Q000378:metabolism*; D006025:Glycosaminoglycans / Q000378:metabolism*; D008071:Lipoprotein Lipase / Q000378:metabolism*; D051379:Mice; D018345:Mice, Knockout; D008954:Models, Biological; D011485:Protein Binding; D011499:Protein Processing, Post-Translational; D011956:Receptors, Cell Surface / Q000378:metabolism; D018110:Receptors, Lipoprotein / Q000235:genetics / Q000378:metabolism / Q000502:physiology
D002914:Chylomicrons; C472779:GPI-HBP1 protein, mouse; D006025:Glycosaminoglycans; D011956:Receptors, Cell Surface; D018110:Receptors, Lipoprotein; D008071:Lipoprotein Lipase