The DOI matches its Crossref record; 2 of the 2 references it cites were found in a registry or an index.
GPIHBP1 stabilizes lipoprotein lipase and prevents its inhibition by angiopoietin-like 3 and angiopoietin-like 4
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
Targeting ANGPTL3, ANGPTL4, or ANGPTL8 with antibodies or antisense oligos can lower plasma triglycerides in preclinical studies.
“Preclinical studies using antibodies or antisense oligos showed that targeting ANGPTL3, ANGPTL4, or ANGPTL8 can lower plasma triglycerides (29, 56, 60, 165, 168–172).”
From Regulation of lipoprotein metabolism by ANGPTL3, ANGPTL4, and ANGPTL8 (2021) · cites this paper as [60]
In the section “Neutralizing mAbs to ANGPTL3 and ANGPTL4 lower TG levels in Gpihbp1−/− mice” (page unavailable), the paper reports lower serum triglycerides after antibody treatment targeting ANGPTL4 or ANGPTL3. It does not report antibody targeting of ANGPTL8 or triglyceride lowering with antisense oligos, so it supports only part of the citing sentence. (LLM, conf=0.88)
Experimental — accuracy not yet measuredSeveral studies have reported that ANGPTL3 is a less potent inhibitor than ANGPTL4.
“In fact, several studies have reported that ANGPTL3 is a less potent inhibitor than ANGPTL4 (54, 55, 60, 133, 136),”
From Regulation of lipoprotein metabolism by ANGPTL3, ANGPTL4, and ANGPTL8 (2021) · cites this paper as [60]
Most studies showing ANGPTL3-mediated LPL inhibition in vitro required supraphysiological concentrations of ANGPTL3 to achieve significant inhibition.
“and most of the studies showing that ANGPTL3-mediated LPL inhibition in vitro required supraphysiological concentrations of ANGPTL3 to achieve significant inhibition (60, 105, 107, 115).”
From Regulation of lipoprotein metabolism by ANGPTL3, ANGPTL4, and ANGPTL8 (2021) · cites this paper as [60]
GPIHBP1 protects LPL from ANGPTL3 inhibition as does heparin.
“LPL’s endothelial cell receptor GPIHBP1 protects LPL from ANGPTL3 inhibition as does heparin (60, 115).”
From Regulation of lipoprotein metabolism by ANGPTL3, ANGPTL4, and ANGPTL8 (2021) · cites this paper as [60]
Vascular LPL, bound to its receptor GPIHBP1, is protected from ANGPTL4 inhibition.
“In fact, several studies have found that vascular LPL, bound to its receptor GPIHBP1, is protected from ANGPTL4 inhibition (51, 52, 60).”
From Regulation of lipoprotein metabolism by ANGPTL3, ANGPTL4, and ANGPTL8 (2021) · cites this paper as [60]
LPL bound to GPIHBP1 is largely protected from ANGPTL4.
“LPL bound to GPIHBP1 is largely protected from ANGPTL4 (51, 52, 60, 98).”
From Regulation of lipoprotein metabolism by ANGPTL3, ANGPTL4, and ANGPTL8 (2021) · cites this paper as [60]
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
Köster, A., Chao, Y. B., Mosior, M., Ford, A., Gonzalez-DeWhitt, P. A., Hale, J. E., Li, D., Qiu, Y., Fraser, C. C., Yang, D. D., et al. (2005) · Endocrinology · doi:10.1210/en.2005-0476 · Cited by 427
The 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
Flagged first, then by citations
Research works printed but not linked: 39
- Wang, 2008, Polygenic determinants of severe hypertriglyceridemia, Hum. Mol. Genet., 17, 2894, 10.1093/hmg/ddn188 · DOI
- Lusis, 2008, A treasure trove for lipoprotein biology, Nat. Genet., 40, 129, 10.1038/ng0208-129 · DOI
- Mead, 2002, Lipoprotein lipase: structure, function, regulation, and role in disease, J. Mol. Med., 80, 753, 10.1007/s00109-002-0384-9 · DOI
- Merkel, 2002, Lipoprotein lipase: genetics, lipid uptake, and regulation, J. Lipid Res., 43, 1997, 10.1194/jlr.R200015-JLR200 · DOI
- Li, 2006, Genetics and regulation of angiopoietin-like proteins 3 and 4, Curr. Opin. Lipidol., 17, 152, 10.1097/01.mol.0000217896.67444.05 · DOI
- Dorfmeister, 2008, Effects of six APOA5 variants, identified in patients with severe hypertriglyceridemia, on in vitro lipoprotein lipase activity and receptor binding, Arterioscler. Thromb. Vasc. Biol., 28, 1866, 10.1161/ATVBAHA.108.172866 · DOI
- Jong, 1999, Role of ApoCs in lipoprotein metabolism: functional differences between ApoC1, ApoC2, and ApoC3, Arterioscler. Thromb. Vasc. Biol., 19, 472, 10.1161/01.ATV.19.3.472 · DOI · Paper page
- Merkel, 2005, Apolipoprotein AV accelerates plasma hydrolysis of triglyceride-rich lipoproteins by interaction with proteoglycan-bound lipoprotein lipase, J. Biol. Chem., 280, 21553, 10.1074/jbc.M411412200 · DOI
- Priore Oliva, 2005, Inherited apolipoprotein A-V deficiency in severe hypertriglyceridemia, Arterioscler. Thromb. Vasc. Biol., 25, 411, 10.1161/01.ATV.0000153087.36428.dd · DOI
- McIlhargey, 2003, Identification of a lipoprotein lipase cofactor-binding site by chemical cross-linking and transfer of apolipoprotein C–II-responsive lipolysis from lipoprotein lipase to hepatic lipase, J. Biol. Chem., 278, 23027, 10.1074/jbc.M300315200 · DOI
- Olivecrona, 1997, Lipid binding of apolipoprotein CII is required for stimulation of lipoprotein lipase activity against apolipoprotein CII-deficient chylomicrons, Arterioscler. Thromb. Vasc. Biol., 17, 1545, 10.1161/01.ATV.17.8.1545 · DOI
- Wang, 1985, Modulation of lipoprotein lipase activity by apolipoproteins. Effect of apolipoprotein C–III, J. Clin. Invest., 75, 384, 10.1172/JCI111711 · DOI
- Zhang, 2005, Calcium triggers folding of lipoprotein lipase into active dimers, J. Biol. Chem., 280, 42580, 10.1074/jbc.M507252200 · DOI
- Kobayashi, 2002, Molecular modeling of the dimeric structure of human lipoprotein lipase and functional studies of the carboxyl-terminal domain, Eur. J. Biochem., 269, 4701, 10.1046/j.1432-1033.2002.03179.x · DOI
- Lookene, 2004, Rapid subunit exchange in dimeric lipoprotein lipase and properties of the inactive monomer, J. Biol. Chem., 279, 49964, 10.1074/jbc.M407419200 · DOI
- Wong, 1997, A molecular biology-based approach to resolve the subunit orientation of lipoprotein lipase, Proc. Natl. Acad. Sci. USA., 94, 5594, 10.1073/pnas.94.11.5594 · DOI
- Lutz, 2001, Heparin-binding defective lipoprotein lipase is unstable and causes abnormalities in lipid delivery to tissues, J. Clin. Invest., 107, 1183, 10.1172/JCI11774 · DOI · Paper page
- Desai, 2007, Lipid-lowering effects of anti-angiopoietin-like 4 antibody recapitulate the lipid phenotype found in angiopoietin-like 4 knockout mice, Proc. Natl. Acad. Sci. USA., 104, 11766, 10.1073/pnas.0705041104 · DOI · Paper page
- Kathiresan, 2008, Six new loci associated with blood low-density lipoprotein cholesterol, high-density lipoprotein cholesterol or triglycerides in humans, Nat. Genet., 40, 189, 10.1038/ng.75 · DOI · Paper page
- Kersten, 2005, Regulation of lipid metabolism via angiopoietin-like proteins, Biochem. Soc. Trans., 33, 1059, 10.1042/BST0331059 · DOI
- Oike, 2005, Angiopoietin-like proteins: potential new targets for metabolic syndrome therapy, Trends Mol. Med., 11, 473, 10.1016/j.molmed.2005.08.002 · DOI
- Romeo, 2007, Population-based resequencing of ANGPTL4 uncovers variations that reduce triglycerides and increase HDL, Nat. Genet., 39, 513, 10.1038/ng1984 · DOI · Paper page
- Willer, 2008, Newly identified loci that influence lipid concentrations and risk of coronary artery disease, Nat. Genet., 40, 161, 10.1038/ng.76 · DOI · Paper page
- Sukonina, 2006, Angiopoietin-like protein 4 converts lipoprotein lipase to inactive monomers and modulates lipase activity in adipose tissue, Proc. Natl. Acad. Sci. USA., 103, 17450, 10.1073/pnas.0604026103 · DOI · Paper page
- 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
- Young, 2007, GPIHBP1: an endothelial cell molecule important for the lipolytic processing of chylomicrons, Curr. Opin. Lipidol., 18, 389, 10.1097/MOL.0b013e3281527914 · DOI
- Ioka, 2003, Expression cloning and characterization of a novel glycosylphosphatidylinositol-anchored high density lipoprotein-binding protein, GPI-HBP1, J. Biol. Chem., 278, 7344, 10.1074/jbc.M211932200 · DOI
- 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
- Ausubel, 1998, Current Protocols in Molecular Biology, John Wiley & Sons New York, NY
- Lee, 2009, Identification of a new functional domain in angiopoietin-like 3 (ANGPTL3) and angiopoietin-like 4 (ANGPTL4) involved in binding and inhibition of lipoprotein lipase (LPL), J. Biol. Chem., 284, 13735, 10.1074/jbc.M807899200 · DOI · Paper page
- Panteghini, 2001, Measurement of pancreatic lipase activity in serum by a kinetic colorimetric assay using a new chromogenic substrate, Ann. Clin. Biochem., 38, 365, 10.1258/0004563011900876 · DOI
- Institute of Laboratory Animal Research. C. o. L. S., National Research Council. 1996. Guide for the Care and Use of Laboratory Animals The National Academic Press, Washington, D.C.
- Poisson, 2007, FragAnchor: a large-scale predictor of glycosylphosphatidylinositol anchors in eukaryote protein sequences by qualitative scoring, Genomics Proteomics Bioinformatics., 5, 121, 10.1016/S1672-0229(07)60022-9 · DOI
- Beigneux, 2008, Glycosylation of Asn-76 in mouse GPIHBP1 is critical for its appearance on the cell surface and the binding of chylomicrons and lipoprotein lipase, J. Lipid Res., 49, 1312, 10.1194/jlr.M700593-JLR200 · 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
- Kieffer, 1994, Three-dimensional solution structure of the extracellular region of the complement regulatory protein CD59, a new cell-surface protein domain related to snake venom neurotoxins, Biochemistry., 33, 4471, 10.1021/bi00181a006 · DOI
- Ploug, 1994, Structure-function relationships in the receptor for urokinase-type plasminogen activator. Comparison to other members of the Ly-6 family and snake venom alpha-neurotoxins, FEBS Lett., 349, 163, 10.1016/0014-5793(94)00674-1 · DOI
- Blasiole, 2007, The physiological and molecular regulation of lipoprotein assembly and secretion, Mol. Biosyst., 3, 608, 10.1039/b700706j · DOI
- 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
Cited by
Sorted by citations
Angiopoietin-like 3 in lipoprotein metabolism
Kersten, S. (2017) · Nature Reviews Endocrinology · doi:10.1038/nrendo.2017.119 · Cited by 220
Gusarova, V., Alexa, C. A., Wang, Y., Rafique, A., Kim, J. H., Buckler, D., Mintah, I. J., Shihanian, L. M., Cohen, J. C., Hobbs, H. H., et al. (2015) · Journal of Lipid Research · doi:10.1194/jlr.m054890 · Cited by 210
Inactivation of ANGPTL3 reduces hepatic VLDL-triglyceride secretion
Wang, Y., Gusarova, V., Banfi, S., Gromada, J., Cohen, J. C., & Hobbs, H. H. (2015) · Journal of Lipid Research · doi:10.1194/jlr.m054882 · Cited by 189
Regulation of lipoprotein metabolism by ANGPTL3, ANGPTL4, and ANGPTL8
Sylvers-Davie, K. L., & Davies, B. S. J. (2021) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00195.2021 · Cited by 154
Angiopoietin-like Protein 4 Inhibition of Lipoprotein Lipase
Lafferty, M. J., Bradford, K. C., Erie, D. A., & Neher, S. B. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.497602 · Cited by 88
Angiopoietin-like 4 directs uptake of dietary fat away from adipose during fasting
Cushing, E. M., Chi, X., Sylvers, K. L., Shetty, S. K., Potthoff, M. J., & Davies, B. S. J. (2017) · Molecular Metabolism · doi:10.1016/j.molmet.2017.06.007 · Cited by 88
Metadata
- Authors
- Sonnenburg, W. K., Yu, D., Lee, E.-C., Xiong, W., Gololobov, G., Key, B., Gay, J., Wilganowski, N., Hu, Y., Zhao, S., Schneider, M., Ding, Z.-M., Zambrowicz, B. P., Landes, G., Powell, D. R., & Desai, U.
- Venue
- Journal of Lipid Research
- Publisher
- Elsevier BV
- Published
- 2009-12
- Volume
- 50
- Issue
- 12
- Pages
- 2421-2429
- ISSN
- 0022-2275
- Cited by
- 115
- References
- 2
- Language
- en
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review