A novel NanoBiT-based assay monitors the interaction between lipoprotein lipase and GPIHBP1 in real time [S]
The hydrolysis of triglycerides in triglyceride-rich lipoproteins by LPL is critical for the
delivery of triglyceride-derived fatty acids to tissues, including heart, skeletal muscle, and
adipose tissues. Physiologically active LPL is normally bound to the endothelial cell protein
glycosylphosphatidylinositol-anchored high-density lipoprotein binding protein 1
(GPIHBP1), which transports LPL across endothelial cells, anchors LPL to the vascular wall,
and stabilizes LPL activity. Disruption of LPL-GPIHBP1 binding significantly alters …
delivery of triglyceride-derived fatty acids to tissues, including heart, skeletal muscle, and
adipose tissues. Physiologically active LPL is normally bound to the endothelial cell protein
glycosylphosphatidylinositol-anchored high-density lipoprotein binding protein 1
(GPIHBP1), which transports LPL across endothelial cells, anchors LPL to the vascular wall,
and stabilizes LPL activity. Disruption of LPL-GPIHBP1 binding significantly alters …