期刊
CELL METABOLISM
卷 5, 期 4, 页码 279-291出版社
CELL PRESS
DOI: 10.1016/j.cmet.2007.02.002
关键词
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资金
- NCI NIH HHS [R01 CA099506, R01 CA099506-05, R01 CA099506-04] Funding Source: Medline
- NHLBI NIH HHS [U01 HL066600, U01 HL066621-04, U01 HL066621-05, R01 HL073061, HL073061, HL087228-01, HL66621, U01 HL066621, HL66600] Funding Source: Medline
- NIAMS NIH HHS [R01 AR050200-05, R01 AR050200-04, R01 AR050200] Funding Source: Medline
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-nnediated processing of chylomicrons in capillaries.
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