Glycosylphosphatidylinositol-anchored high-density lipoprotein-binding protein 1 plays a critical role in the lipolytic processing of chylomicrons.

@article{Beigneux2007Glycosylphosphatidylinositolancho,
  title={Glycosylphosphatidylinositol-anchored high-density lipoprotein-binding protein 1 plays a critical role in the lipolytic processing of chylomicrons.},
  author={Anne P. Beigneux and Brandon S. J. Davies and Peter M. W. Gin and Michael S Weinstein and Emily A. Farber and Xin Qiao and Franklin Peale and Stuart Bunting and Rosemary L. Walzem and Jinny S. Wong and William S. Blaner and Z Ding and Kristan Melford and Nuttaporn Wongsiriroj and Xiao Xiao Shu and Fred de Sauvage and Robert Ryan and Loren G. Fong and Andr{\'e} Bensadoun and Stephen G. Young},
  journal={Cell metabolism},
  year={2007},
  volume={5 4},
  pages={279-91}
}
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… CONTINUE READING
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