Glycosylphosphatidylinositol-anchored high-density lipoprotein-binding protein 1 (GPIHBP1)

Glycosylphosphatidylinositol-anchored high-density lipoprotein-binding protein 1 (GPIHBP1) is a GPI-anchored membrane protein primarily expressed on capillary endothelial cells, characterized by a Ly6/uPAR (LU) domain and an intrinsically disordered, highly acidic N-terminal domain[1][3][5]. GPIHBP1 is essential for binding, stabilizing, and transporting lipoprotein lipase (LPL) from the subendothelial space across endothelial cells to the capillary lumen, enabling efficient intravascular hydrolysis of triglyceride-rich lipoproteins[1][3][5][6]. Loss of GPIHBP1 function—whether by genetic mutation or by the development of autoantibodies—leads to severe hypertriglyceridemia (familial or acquired chylomicronemia), a life-threatening disorder[1][3][5]. GPIHBP1 has also been implicated in tumor progression and immune microenvironment regulation in colorectal cancer, where its increased expression in advanced tumors is associated with immune evasion and poorer outcomes[2]. There are currently no direct drugs targeting GPIHBP1, but its presence and function are crucial for therapies that rely on LPL-mediated lipid metabolism.

Other names

Glycosylphosphatidylinositol-anchored high-density lipoprotein-binding protein 1GPIHBP1HBP1GPI-HBP1GPI-anchored HDL-binding protein 1High density lipoprotein-binding protein 1Endothelial cell LPL transporterHYPL1DLOC338328