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GPIHBP1: an endothelial cell molecule important for the lipolytic processing of chylomicrons Young SG; Davies BS; Fong LG; Gin P; Weinstein MM; Bensadoun A; Beigneux APCurr Opin Lipidol 2007[Aug]; 18 (4): 389-96PURPOSE OF REVIEW: To summarize recent data indicating that glycosylphosphatidylinositol-anchored high density lipoprotein-binding protein 1 (GPIHBP1) plays a key role in the lipolytic processing of chylomicrons. RECENT FINDINGS: Lipoprotein lipase hydrolyses triglycerides in chylomicrons at the luminal surface of the capillaries in heart, adipose tissue, and skeletal muscle. The endothelial cell molecule that facilitates the lipolytic processing of chylomicrons has never been clearly defined. Mice lacking GPIHBP1 manifest chylomicronemia, with plasma triglyceride levels as high as 5000 mg/dl. In wild-type mice, GPIHBP1 is expressed on the luminal surface of capillaries in heart, adipose tissue, and skeletal muscle. Cells transfected with GPIHBP1 bind both chylomicrons and lipoprotein lipase avidly. SUMMARY: The chylomicronemia in Gpihbp1-deficient mice, the fact that GPIHBP1 is located within the lumen of capillaries, and the fact that GPIHBP1 binds lipoprotein lipase and chylomicrons suggest that GPIHBP1 is a key platform for the lipolytic processing of triglyceride-rich lipoproteins.|*Lipolysis[MESH]|Amino Acid Sequence[MESH]|Animals[MESH]|Carrier Proteins/*physiology[MESH]|Chylomicrons/*metabolism[MESH]|Endothelial Cells/*metabolism[MESH]|Humans[MESH]|Lipoproteins/chemistry[MESH]|Mice[MESH]|Models, Biological[MESH]|Molecular Sequence Data[MESH]|Phenotype[MESH]|Receptors, Lipoprotein/*physiology[MESH]|Sequence Homology, Amino Acid[MESH]|Tissue Distribution[MESH]|Triglycerides/metabolism[MESH] |
