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The DOI matches its Crossref record; 3 of the 3 references it cites were found in a registry or an index.

ANGPTL8 requires ANGPTL3 to inhibit lipoprotein lipase and plasma triglyceride clearance

Haller, Jorge F., Mintah, Ivory J., Shihanian, Lisa M., Stevis, Panayiotis, Buckler, David, Alexa-Braun, Corey A., Kleiner, Sandra, Banfi, Serena, Cohen, Jonathan C., Hobbs, Helen H., Yancopoulos, George D., Murphy, Andrew J., Gusarova, Viktoria, Gromada, Jesper·2017·Journal of Lipid Research
DOI 10.1194/jlr.m075689
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Crossref · 10.1194/jlr.m075689

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  • In vitro, ANGPTL3-ANGPTL8 complexes inhibit LPL orders of magnitude better than either ANGPTL3 or ANGPTL8 alone.

    “in vitro several studies have found that the ability of ANGPTL3-ANGPTL8 complexes to inhibit LPL is orders of magnitude better than that of either ANGPTL3 or ANGPTL8 alone (54, 115, 137, 138)”

    From Regulation of lipoprotein metabolism by ANGPTL3, ANGPTL4, and ANGPTL8 (2021) · cites this paper as [137]

    The Results section (page unavailable) reports that ANGPTL8 alone failed to inhibit LPL in vitro, while ANGPTL3 alone and ANGPTL3–ANGPTL8 coexpression both strongly inhibited it. This supports the comparison with ANGPTL8 alone, but the paper does not show that the combination inhibits LPL orders of magnitude better than ANGPTL3 alone. (LLM, conf=0.87)

    Experimental — accuracy not yet measured

  • Overexpression of ANGPTL8 in the absence of ANGPTL3, or vice versa, has limited ability to increase plasma triglycerides.

    “overexpression of ANGPTL8 in the absence of ANGPTL3, or vice versa, has limited ability to increase plasma triglycerides (19, 115, 137)”

    From Regulation of lipoprotein metabolism by ANGPTL3, ANGPTL4, and ANGPTL8 (2021) · cites this paper as [137]

    The Results (Fig. 1E; page unavailable) show that ANGPTL8 expression had no effect on triglycerides in mice lacking ANGPTL3. The converse is overstated: the Results say ANGPTL3 independently promoted hypertriglyceridemia, although coexpression with ANGPTL8 raised triglycerides further. (LLM, conf=0.88)

    Experimental — accuracy not yet measured

  • More recent studies have shown that ANGPTL3 forms a complex with ANGPTL8 and that this complex is most likely the physiologically relevant LPL inhibitor.

    “As discussed below, more recent studies have shown that ANGPTL3 forms of complex with ANGPTL8 and that this complex is most likely the physiologically relevant LPL inhibitor (19, 54, 115, 137, 138).”

    From Regulation of lipoprotein metabolism by ANGPTL3, ANGPTL4, and ANGPTL8 (2021) · cites this paper as [137]

    The Abstract and Results show that ANGPTL3 and ANGPTL8 form an inhibitory complex: ANGPTL8 inhibits LPL in the presence of ANGPTL3, and coexpression raises triglycerides in mice more than ANGPTL3 alone. The paper does not establish that the complex is the predominant physiologically relevant LPL inhibitor; it also reports that ANGPTL3 inhibits LPL independently of ANGPTL8. Page numbers are unavailable in our copy. (LLM, conf=0.82)

    Experimental — accuracy not yet measured

  • ANGPTL8 does not inhibit LPL on its own.

    “Although ANGPTL8 was initially reported to inhibit LPL on its own (35), later studies found that this not to be the case (115, 137, 138).”

    From Regulation of lipoprotein metabolism by ANGPTL3, ANGPTL4, and ANGPTL8 (2021) · cites this paper as [137]

  • ANGPTL8 has a domain homologous to the lipase inhibitory domain of ANGPTL3 and ANGPTL4.

    “ANGPTL8 has a domain homologous to the lipase inhibitory domain of ANGPTL3 and ANGPTL4 (137).”

    From Regulation of lipoprotein metabolism by ANGPTL3, ANGPTL4, and ANGPTL8 (2021) · cites this paper as [137]

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Citations

Cites

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Research works printed but not linked: 11

  1. Romeo, 2009, Rare loss-of-function mutations in ANGPTL family members contribute to plasma triglyceride levels in humans, J. Clin. Invest., 119, 70
  2. Zhang, 2012, Lipasin, a novel nutritionally-regulated liver-enriched factor that regulates serum triglyceride levels, Biochem. Biophys. Res. Commun., 424, 786, 10.1016/j.bbrc.2012.07.038 · DOI · Paper page
  3. Quagliarini, 2012, Atypical angiopoietin-like protein that regulates ANGPTL3, Proc. Natl. Acad. Sci. USA., 109, 19751, 10.1073/pnas.1217552109 · DOI · Paper page
  4. Wang, 2015, Hepatic ANGPTL3 regulates adipose tissue energy homeostasis, Proc. Natl. Acad. Sci. USA., 112, 11630, 10.1073/pnas.1515374112 · DOI · Paper page
  5. Yau, 2009, A highly conserved motif within the NH2-terminal coiled-coil domain of angiopoietin-like protein 4 confers its inhibitory effects on lipoprotein lipase by disrupting the enzyme dimerization, J. Biol. Chem., 284, 11942, 10.1074/jbc.M809802200 · DOI · Paper page
  6. Basu, 2011, Determination of lipoprotein lipase activity using a novel fluorescent lipase assay, J. Lipid Res., 52, 826, 10.1194/jlr.D010744 · DOI
  7. Fairhead, 2015, Site-specific biotinylation of purified proteins using BirA. Methods in molecular biology, 1266, 171
  8. Gusarova, 2015, ANGPTL3 blockade with a human monoclonal antibody reduces plasma lipids in dyslipidemic mice and monkeys, J. Lipid Res., 56, 1308, 10.1194/jlr.M054890 · DOI · Paper page
  9. Gusarova, V., S. Banfi, C. A. Alexa-Braun, L. M. Shihanian, I. J. Mintah, J. S. Lee, Y. Xin, Q. Su, V. Kamat, J. C. Cohen, . ANGPTL8 blockade with a monoclonal antibody promotes triglyceride clearance, energy expenditure and weight loss in mice. Endocrinology. Epub ahead of print. February 15, 2017. · DOI
  10. Siddiqa, 2016, Structural characterization of ANGPTL8 (betatrophin) with its interacting partner lipoprotein lipase, Comput. Biol. Chem., 61, 210, 10.1016/j.compbiolchem.2016.01.009 · DOI
  11. Wang, 2013, Mice lacking ANGPTL8 (Betatrophin) manifest disrupted triglyceride metabolism without impaired glucose homeostasis, Proc. Natl. Acad. Sci. USA., 110, 16109, 10.1073/pnas.1315292110 · DOI · Paper page

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Metadata

Authors
Haller, J. F., Mintah, I. J., Shihanian, L. M., Stevis, P., Buckler, D., Alexa-Braun, C. A., Kleiner, S., Banfi, S., Cohen, J. C., Hobbs, H. H., Yancopoulos, G. D., Murphy, A. J., Gusarova, V., & Gromada, J.
Venue
Journal of Lipid Research
Publisher
Elsevier BV
Published
2017-06
Volume
58
Issue
6
Pages
1166-1173
ISSN
0022-2275
DOI
10.1194/jlr.m075689
Cited by
199
References
3
Language
en
Licence

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