Cited by 339

The DOI matches its Crossref record.

ANGPTL3 Decreases Very Low Density Lipoprotein Triglyceride Clearance by Inhibition of Lipoprotein Lipase

Shimizugawa, Tetsuya, Ono, Mitsuru, Shimamura, Mitsuru, Yoshida, Kenichi, Ando, Yosuke, Koishi, Ryuta, Ueda, Kenjiro, Inaba, Toshimori, Minekura, Hiroyuki, Kohama, Takafumi, Furukawa, Hidehiko·2002·Journal of Biological Chemistry

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.

A few free checks a day · papers already verified open instantly · results are public

Integrity signals

Registry

Crossref · 10.1074/jbc.m203215200

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.

A few free checks a day · papers already verified open instantly · results are public

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?

  • 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 [105]

    The Results report substantial in-vitro LPL inhibition at 10 µg/ml. But the Discussion explicitly says that the estimated ANGPTL3 concentration in normal humans is close to the dose required for in-vitro inhibition and suggests that ANGPTL3 may act physiologically. That contradicts attributing to this paper the conclusion that supraphysiological concentrations were required. (LLM, conf=0.82)

    Checked by a reasoning model — may be wrong.

    Experimental — accuracy not yet measured
  • ANGPTL3 reduces the activity of LPL and EL in vitro.

    “ANGPTL3 is mainly expressed in the liver and has been shown to reduce the activity of LPL (lipoprotein lipase)4 and EL (endothelial lipase) in vitro,5 which is widely considered to explain the observed low triglyceride and HDL-C levels, respectively, in carriers of LOF variants in ANGPTL3.”
  • The low triglyceride and HDL-C levels in carriers of LOF variants in ANGPTL3 are widely considered to be explained by ANGPTL3's inhibition of LPL and EL.

    “ANGPTL3 is mainly expressed in the liver and has been shown to reduce the activity of LPL (lipoprotein lipase)4 and EL (endothelial lipase) in vitro,5 which is widely considered to explain the observed low triglyceride and HDL-C levels, respectively, in carriers of LOF variants in ANGPTL3.”
  • KK/San mice had increased clearance of triglyceride-rich lipoproteins and ANGPTL3 could inhibit LPL in vitro.

    “Soon after, Shimizugawa et al. (105) made a direct connection between ANGPTL3 and LPL, finding that the KK/San mice had increased clearance of triglyceride-rich lipoproteins and showing that ANGPTL3 could inhibit LPL in vitro.”

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

No references could be resolved yet.

Research works printed but not linked: 35

  1. Rice, 1991, Hum. Hered., 41, 107, 10.1159/000153987 · DOI
  2. Perusse, 1989, Arteriosclerosis, 9, 308, 10.1161/01.ATV.9.3.308 · DOI
  3. Bucher, 1988, Genet. Epidemiol., 5, 17, 10.1002/gepi.1370050103 · DOI
  4. Austin, 1987, Am. J. Epidemiol., 125, 308, 10.1093/oxfordjournals.aje.a114531 · DOI
  5. Reue, 1996, J. Lipid Res., 37, 1387, 10.1016/S0022-2275(20)39126-4 · DOI
  6. Welch, 1996, J. Lipid Res., 37, 1406, 10.1016/S0022-2275(20)39145-8 · DOI
  7. Purcell-Huynh, 1995, J. Clin. Invest., 96, 1845, 10.1172/JCI118230 · DOI
  8. Kondo, 1957, Bull. Exp. Anim., 6, 107, 10.1538/expanim1957.6.4_107 · DOI
  9. Nakamura, 1967, Diabetologia, 3, 212, 10.1007/BF01222198 · DOI
  10. Nakamura, 1962, Proc. Jpn. Acad., 38, 348, 10.2183/pjab1945.38.348 · DOI
  11. Shiraki, 1993, Diabetes Frontier, 4, 641
  12. Koishi, 2002, Nat. Genet., 30, 151, 10.1038/ng814 · DOI · Paper page
  13. Davis, 1996, Cell, 87, 1161, 10.1016/S0092-8674(00)81812-7 · DOI · Paper page
  14. Maisonpierre, 1997, Science, 277, 55, 10.1126/science.277.5322.55 · DOI · Paper page
  15. Valenzuela, 1999, Proc. Natl. Acad. Sci. U. S. A., 96, 1904, 10.1073/pnas.96.5.1904 · DOI
  16. Procopio, 1999, J. Biol. Chem., 274, 30196, 10.1074/jbc.274.42.30196 · DOI
  17. Okazaki, 1998, J. Chromatogr. B Biomed. Sci. Appl., 709, 179, 10.1016/S0378-4347(98)00064-4 · DOI
  18. Miyake, 1996, Proc. Natl. Acad. Sci. U. S. A., 93, 1320, 10.1073/pnas.93.3.1320 · DOI
  19. Kanegae, 1994, Jpn. J. Med. Sci. Biol., 47, 157, 10.7883/yoken1952.47.157 · DOI
  20. Otway, 1967, J. Physiol., 190, 321, 10.1113/jphysiol.1967.sp008211 · DOI
  21. Jong, 1996, J. Clin. Invest., 98, 2259, 10.1172/JCI119036 · DOI
  22. Bilheimer, 1972, Biochim. Biophys. Acta, 260, 212, 10.1016/0005-2760(72)90034-3 · DOI
  23. Holmquist, 1978, Anal. Biochem., 88, 457, 10.1016/0003-2697(78)90444-X · DOI
  24. Kita, 1982, Proc. Natl. Acad. Sci. U. S. A., 79, 5693, 10.1073/pnas.79.18.5693 · DOI
  25. Nilsson-Ehle, 1976, J. Lipid Res., 17, 536, 10.1016/S0022-2275(20)41752-3 · DOI
  26. Maeda, 1994, J. Biol. Chem., 269, 23610, 10.1016/S0021-9258(17)31559-4 · DOI
  27. Wang, 1985, J. Clin. Invest., 75, 384, 10.1172/JCI111711 · DOI
  28. McConathy, 1992, J. Lipid Res., 33, 995, 10.1016/S0022-2275(20)41415-4 · DOI
  29. Kinnunen, 1976, FEBS Lett., 65, 354, 10.1016/0014-5793(76)80145-7 · DOI
  30. Rossetti, 2002, Nat. Med., 8, 112, 10.1038/nm0202-112 · DOI
  31. Naoumova, 2002, Lancet, 359, 2215, 10.1016/S0140-6736(02)09315-7 · DOI
  32. Amar, 1998, J. Lipid Res., 39, 2436, 10.1016/S0022-2275(20)33323-X · DOI · Paper page
  33. Levak-Frank, 1995, J. Clin. Invest., 96, 976, 10.1172/JCI118145 · DOI
  34. Crawford, 1981, Clin Sci (Lond.), 60, 73, 10.1042/cs0600073 · DOI
  35. Murase, 1975, Metabolism, 24, 1279, 10.1016/0026-0495(75)90066-9 · DOI

Cited by

Sorted by citations

Metadata

Authors
Shimizugawa, T., Ono, M., Shimamura, M., Yoshida, K., Ando, Y., Koishi, R., Ueda, K., Inaba, T., Minekura, H., Kohama, T., & Furukawa, H.
Venue
Journal of Biological Chemistry
Publisher
Elsevier BV
Published
2002-09
Volume
277
Issue
37
Pages
33742-33748
ISSN
0021-9258
Cited by
339
References
0
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