[HTML][HTML] Angiopoietin-like 4 modifies the interactions between lipoprotein lipase and its endothelial cell transporter GPIHBP1
The release of fatty acids from plasma triglycerides for tissue uptake is critically dependent
on the enzyme lipoprotein lipase (LPL). Hydrolysis of plasma triglycerides by LPL can be
disrupted by the protein angiopoietin-like 4 (ANGPTL4), and ANGPTL4 has been shown to
inactivate LPL in vitro. However, in vivo LPL is often complexed to
glycosylphosphatidylinositol-anchored high density lipoprotein-binding protein 1 (GPIHBP1)
on the surface of capillary endothelial cells. GPIHBP1 is responsible for trafficking LPL …
on the enzyme lipoprotein lipase (LPL). Hydrolysis of plasma triglycerides by LPL can be
disrupted by the protein angiopoietin-like 4 (ANGPTL4), and ANGPTL4 has been shown to
inactivate LPL in vitro. However, in vivo LPL is often complexed to
glycosylphosphatidylinositol-anchored high density lipoprotein-binding protein 1 (GPIHBP1)
on the surface of capillary endothelial cells. GPIHBP1 is responsible for trafficking LPL …