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GPIHBP1 Is Responsible for the Entry of Lipoprotein Lipase into Capillaries
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LPL is secreted by parenchymal cells of fat-consuming or fat-storing tissues and transported across capillary endothelial cells by GPIHBP1.
“LPL is secreted by the parenchymal cells of these tissues, i.e., the adipocytes, cardiomyocytes, and myocytes (6) and then transported across capillary endothelial cells by the endothelial cell protein glycosylphosphatidylinositol-anchored high-density lipoprotein-binding protein 1 (GPIHBP1) (7).”
From Regulation of lipoprotein metabolism by ANGPTL3, ANGPTL4, and ANGPTL8 (2021) · cites this paper as [7]
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Cites
Mutation of conserved cysteines in the Ly6 domain of GPIHBP1 in familial chylomicronemia.
Olivecrona, G., Ehrenborg, E., Semb, H., Makoveichuk, E., Lindberg, A., Hayden, M. R., Gin, P., Davies, B. S. J., Weinstein, M. M., Fong, L. G., et al. (2010) · Journal of Lipid Research · doi:10.1194/jlr.m002717 · Cited by 118 · cited 1×
“Very recently, mutations in GPIHBP1 have been identified in humans with severe hypertriglyceridemia (Beigneux et al., 2009a; Franssen et al., 2010; Olivecrona et al., 2010; Wang and Hegele, 2007).”
Self-citationThe acidic domain of GPIHBP1 is important for the binding of lipoprotein lipase and chylomicrons.
Gin, P., Yin, L., Davies, B. S. J., Weinstein, M. M., Ryan, R. O., Bensadoun, A., Fong, L. G., Young, S. G., & Beigneux, A. P. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m802579200 · Cited by 85 · cited 3×
“Because expression of GPIHBP1 in Chinese hamster ovary (CHO) cells confers the ability to bind LPL (Beigneux et al., 2007, 2009a, 2009b; Gin et al., 2008), we hypothesized that at least some of the LPL in mouse tissues might colocalize with GPIHBP1 in capillaries.”
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Research works printed but not linked: 20
- Anderson, 1993, Plasmalemmal caveolae and GPI-anchored membrane proteins, Curr. Opin. Cell Biol., 5, 647, 10.1016/0955-0674(93)90135-D · DOI
- Beigneux, 2007, Glycosylphosphatidylinositol-anchored high-density lipoprotein-binding protein 1 plays a critical role in the lipolytic processing of chylomicrons, Cell Metab., 5, 279, 10.1016/j.cmet.2007.02.002 · DOI · Paper page
- Beigneux, 2009, Chylomicronemia with a mutant GPIHBP1 (Q115P) that cannot bind lipoprotein lipase, Arterioscler. Thromb. Vasc. Biol., 29, 956, 10.1161/ATVBAHA.109.186577 · DOI
- Beigneux, 2009, Highly conserved cysteines within the Ly6 domain of GPIHBP1 are crucial for the binding of lipoprotein lipase, J. Biol. Chem., 284, 30240, 10.1074/jbc.M109.046391 · DOI
- Brown, 1992, Sorting of GPI-anchored proteins to glycolipid-enriched membrane subdomains during transport to the apical cell surface, Cell, 68, 533, 10.1016/0092-8674(92)90189-J · DOI · Paper page
- Cryer, 1976, Effect of nutritional status on rat adipose tissue, muscle and post-heparin plasma clearing factor lipase activities: their relationship to triglyceride fatty acid uptake by fat-cells and to plasma insulin concentrations, Clin. Sci. Mol. Med., 50, 213
- Davies, 2008, The expression of GPIHBP1, an endothelial cell binding site for lipoprotein lipase and chylomicrons, is induced by peroxisome proliferator-activated receptor-gamma, Mol. Endocrinol., 22, 2496, 10.1210/me.2008-0146 · DOI
- Franssen, 2010, Chylomicronemia with low postheparin lipoprotein lipase levels in the setting of GPIHBP1 defects, Circ Cardiovasc Genet, 3, 169, 10.1161/CIRCGENETICS.109.908905 · DOI
- Frykman, 1995, Normal plasma lipoproteins and fertility in gene-targeted mice homozygous for a disruption in the gene encoding very low density lipoprotein receptor, Proc. Natl. Acad. Sci. USA, 92, 8453, 10.1073/pnas.92.18.8453 · DOI · Paper page
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- Varma, 1998, GPI-anchored proteins are organized in submicron domains at the cell surface, Nature, 394, 798, 10.1038/29563 · DOI · Paper page
- Wang, 2009, Lipoprotein lipase: from gene to obesity, Am. J. Physiol. Endocrinol. Metab., 297, E271, 10.1152/ajpendo.90920.2008 · DOI · Paper page
- Wang, 2007, Homozygous missense mutation (G56R) in glycosylphosphatidylinositol-anchored high-density lipoprotein-binding protein 1 (GPI-HBP1) in two siblings with fasting chylomicronemia (MIM 144650), Lipids Health Dis., 6, 23, 10.1186/1476-511X-6-23 · DOI
- Weinstein, 2008, Abnormal patterns of lipoprotein lipase release into the plasma in GPIHBP1-deficient mice, J. Biol. Chem., 283, 34511, 10.1074/jbc.M806067200 · DOI · Paper page
- Weinstock, 1997, Lipoprotein lipase controls fatty acid entry into adipose tissue, but fat mass is preserved by endogenous synthesis in mice deficient in adipose tissue lipoprotein lipase, Proc. Natl. Acad. Sci. USA, 94, 10261, 10.1073/pnas.94.19.10261 · DOI
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“LPL serves as the docking station for chylomicrons and VLDL for adherence to the endothelium via glycosyl-phosphatidylinositol-anchored high-density-binding protein 1 (GPIHBP1), which is present on the luminal side of the endothelium [14–16].”
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Metadata
- Authors
- Davies, B. S. J., Beigneux, A. P., Barnes, R. H., Tu, Y., Gin, P., Weinstein, M. M., Nobumori, C., Nyrén, R., Goldberg, I., Olivecrona, G., Bensadoun, A., Young, S. G., & Fong, L. G.
- Venue
- Cell Metabolism
- Publisher
- Elsevier BV
- Published
- 2010-07
- Volume
- 12
- Issue
- 1
- Pages
- 42-52
- ISSN
- 1550-4131
- PMC
- PMC2913606
- Cited by
- 342
- References
- 2
- Language
- en
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