Glycosylphosphatidylinositol-anchored high density lipoprotein-binding protein 1

Definition:

Mediates the transport of lipoprotein lipase LPL from the basolateral to the apical surface of endothelial cells in capillaries (By similarity). Anchors LPL on the surface of endothelial cells in the lumen of blood capillaries (By similarity). Protects LPL against loss of activity, and against ANGPTL4-mediated unfolding. Thereby, plays an important role in lipolytic processing of chylomicrons by LPL, triglyceride metabolism and lipid homeostasis. Binds chylomicrons and phospholipid particles that contain APOA5. Binds high-density lipoprotein (HDL) and plays a role in the uptake of lipids from HDL (By similarity).

References:

[1]. Anne P Beigneux, et al. Chylomicronemia with a mutant GPIHBP1 (Q115P) that cannot bind lipoprotein lipase. Arterioscler Thromb Vasc Biol. 2009 Jun;29(6):956-62. [Content Brief]

[2]. Peter Gin, et al. Normal binding of lipoprotein lipase, chylomicrons, and apo-AV to GPIHBP1 containing a G56R amino acid substitution. Biochim Biophys Acta. 2007 Dec;1771(12):1464-8. [Content Brief]

[3]. Kristian K Kristensen, et al. A disordered acidic domain in GPIHBP1 harboring a sulfated tyrosine regulates lipoprotein lipase. Proc Natl Acad Sci U S A. 2018 Jun 26;115(26):E6020-E6029. [Content Brief]

[4]. I Coca-Prieto, et al. Childhood-onset chylomicronaemia with reduced plasma lipoprotein lipase activity and mass: identification of a novel GPIHBP1 mutation. J Intern Med. 2011 Sep;270(3):224-8. [Content Brief]

[5]. Simon Mysling, et al. The angiopoietin-like protein ANGPTL4 catalyzes unfolding of the hydrolase domain in lipoprotein lipase and the endothelial membrane protein GPIHBP1 counteracts this unfolding. Elife. 2016 Dec 8;5:e20958. [Content Brief]

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