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GPIHBP1 and lipolysis: an update Beigneux AP; Weinstein MM; Davies BS; Gin P; Bensadoun A; Fong LG; Young SGCurr Opin Lipidol 2009[Jun]; 20 (3): 211-6PURPOSE OF REVIEW: This review will provide an update on the structure of GPIHBP1, a 28-kDa glycosylphosphatidylinositol-anchored glycoprotein, and its role in the lipolytic processing of triglyceride-rich lipoproteins. RECENT FINDINGS: Gpihbp1 knockout mice on a chow diet have milky plasma and plasma triglyceride levels of more than 3000 mg/dl. GPIHBP1 is located on the luminal surface of endothelial cells in tissues where lipolysis occurs: heart, skeletal muscle, and adipose tissue. The pattern of lipoprotein lipase (LPL) release into the plasma after an intravenous injection of heparin is abnormal in Gpihbp1-deficient mice, suggesting that GPIHBP1 plays a direct role in binding LPL within the tissues of mice. Transfection of CHO cells with a GPIHBP1 expression vector confers on cells the ability to bind both LPL and chylomicrons. Two regions of GPIHBP1 are required for the binding of LPL - an amino-terminal acidic domain and the cysteine-rich Ly6 domain. GPIHBP1 expression in mice changes with fasting and refeeding and is regulated in part by peroxisome proliferator-activated receptor-gamma. SUMMARY: GPIHBP1, an endothelial cell-surface glycoprotein, binds LPL and is required for the lipolytic processing of triglyceride-rich lipoproteins.|*Lipolysis[MESH]|Animals[MESH]|Gene Expression Regulation[MESH]|Glycoproteins/chemistry/deficiency/genetics/*metabolism[MESH]|Humans[MESH]|Hyperlipidemias/metabolism[MESH]|Lipoprotein Lipase/metabolism[MESH]|Protein Structure, Tertiary[MESH]|Receptors, Lipoprotein/chemistry/deficiency/genetics/metabolism[MESH] |
