Chylomicrons and lipoprotein lipase at the endothelial surface: bound and GAG-ged?
- PMID: 17403366
- DOI: 10.1016/j.cmet.2007.03.003
Chylomicrons and lipoprotein lipase at the endothelial surface: bound and GAG-ged?
Abstract
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.
Comment on
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Glycosylphosphatidylinositol-anchored high-density lipoprotein-binding protein 1 plays a critical role in the lipolytic processing of chylomicrons.Cell Metab. 2007 Apr;5(4):279-91. doi: 10.1016/j.cmet.2007.02.002. Cell Metab. 2007. PMID: 17403372 Free PMC article.
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