Glycosylphosphatidylinositol-anchored high-density lipoprotein-binding protein 1 plays a critical role in the lipolytic processing of chylomicrons.
نویسندگان
چکیده
The triglycerides in chylomicrons are hydrolyzed by lipoprotein lipase (LpL) along the luminal surface of the capillaries. However, the endothelial cell molecule that facilitates chylomicron processing by LpL has not yet been defined. Here, we show that glycosylphosphatidylinositol-anchored high-density lipoprotein-binding protein 1 (GPIHBP1) plays a critical role in the lipolytic processing of chylomicrons. Gpihbp1-deficient mice exhibit a striking accumulation of chylomicrons in the plasma, even on a low-fat diet, resulting in milky plasma and plasma triglyceride levels as high as 5000 mg/dl. Normally, Gpihbp1 is expressed highly in heart and adipose tissue, the same tissues that express high levels of LpL. In these tissues, GPIHBP1 is located on the luminal face of the capillary endothelium. Expression of GPIHBP1 in cultured cells confers the ability to bind both LpL and chylomicrons. These studies strongly suggest that GPIHBP1 is an important platform for the LpL-mediated processing of chylomicrons in capillaries.
منابع مشابه
The lipolytic processing of triglyceride-rich lipoproteins (e.g., chylomicrons, very low density lipoproteins) by lipo- protein lipase (LPL) is the central event in plasma triglyc- eride metabolism and plays a crucial role in the delivery of lipid nutrients to parenchymal cells
This article is available online at http://www.jlr.org The lipolytic processing of triglyceride-rich lipoproteins (e.g., chylomicrons, very low density lipoproteins) by lipoprotein lipase (LPL) is the central event in plasma triglyceride metabolism and plays a crucial role in the delivery of lipid nutrients to parenchymal cells (e.g., adipocytes, myocytes) ( 1–4 ). LPL is synthesized by parench...
متن کاملThe lipolytic processing of triglyceride-rich lipoproteins (e.g., chylomicrons, very low density lipoproteins) by lipo- protein lipase (LPL) is the central event in plasma triglyc-
This article is available online at http://www.jlr.org The lipolytic processing of triglyceride-rich lipoproteins (e.g., chylomicrons, very low density lipoproteins) by lipoprotein lipase (LPL) is the central event in plasma triglyceride metabolism and plays a crucial role in the delivery of lipid nutrients to parenchymal cells (e.g., adipocytes, myocytes) ( 1–4 ). LPL is synthesized by parench...
متن کاملGlycosylation of Asn-76 in mouse GPIHBP1 is critical for its appearance on the cell surface and the binding of chylomicrons and lipoprotein lipase.
GPIHBP1 is a glycosylphosphatidylinositol-anchored protein in the lymphocyte antigen 6 (Ly-6) family that recently was identified as a platform for the lipolytic processing of triglyceride-rich lipoproteins. GPIHBP1 binds both LPL and chylomicrons and is expressed on the luminal face of microvascular endothelial cells. Here, we show that mouse GPIHBP1 is N-glycosylated at Asn-76 within the Ly-6...
متن کاملBinding preferences for GPIHBP1, a glycosylphosphatidylinositol-anchored protein of capillary endothelial cells.
OBJECTIVE To define the ability of GPIHBP1 to bind other lipase family members and other apolipoproteins (apos) and lipoproteins. METHODS AND RESULTS GPIHBP1, a GPI-anchored lymphocyte antigen (Ly)6 protein of capillary endothelial cells, binds lipoprotein lipase (LPL) avidly, but its ability to bind related lipase family members has never been evaluated. As judged by cell-based and cell-free...
متن کاملRecent advances in physiological lipoprotein metabolism.
Research into lipoprotein metabolism has developed because understanding lipoprotein metabolism has important clinical indications. Lipoproteins are risk factors for cardiovascular disease. Recent advances include the identification of factors in the synthesis and secretion of triglyceride rich lipoproteins, chylomicrons (CM) and very low density lipoproteins (VLDL). These included the identifi...
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ورودعنوان ژورنال:
- Cell metabolism
دوره 5 4 شماره
صفحات -
تاریخ انتشار 2007