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Angptl3 regulates lipid metabolism in mice

Koishi, Ryuta, Ando, Yosuke, Ono, Mitsuru, Shimamura, Mitsuru, Yasumo, Hiroaki, Fujiwara, Toshihiko, Horikoshi, Hiroyoshi, Furukawa, Hidehiko·2002·Nature Genetics
DOI 10.1038/ng814
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Abstract

The KK obese mouse is moderately obese and has abnormally high levels of plasma insulin (hyperinsulinemia), glucose (hyperglycemia) and lipids (hyperlipidemia). In one strain (KK/San), we observed abnormally low plasma lipid levels (hypolipidemia). This mutant phenotype is inherited recessively as a mendelian trait. Here we report the mapping of the hypolipidemia (hypl) locus to the middle of chromosome 4 and positional cloning of the autosomal recessive mutation responsible for the hypolipidemia. The hypl locus encodes a unique angiopoietin-like lipoprotein modulator, which we named Allm1. It is identical to angiopoietin-like protein 3, encoded by Angptl3, and has a highly conserved counterpart in humans. Overexpression of Angptl3 or intravenous injection of the purified protein in KK/San mice elicited an increase in circulating plasma lipid levels. This increase was also observed in C57BL/6J normal mice. Taken together, these data suggest that Angptl3 regulates lipid metabolism in animals.

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  • The KK/San substrain presented with strikingly lower levels of plasma triglycerides.

    “Although KK mice manifest obesity, insulin resistance, and hyperlipidemia (104), this substrain (KK/San) presented with strikingly lower levels of plasma triglycerides (15).”

    From Regulation of lipoprotein metabolism by ANGPTL3, ANGPTL4, and ANGPTL8 (2021) · cites this paper as [15]

  • Koishi et al. identified a homozygous loss of function mutation in ANGPTL3 as the causal factor for lower plasma triglycerides in KK/San mice.

    “Koishi et al. (15) identified a homozygous loss of function mutation in ANGPTL3 as the causal factor.”

    From Regulation of lipoprotein metabolism by ANGPTL3, ANGPTL4, and ANGPTL8 (2021) · cites this paper as [15]

  • Overexpression of wild-type ANGPTL3 could increase plasma triglycerides in these mice.

    “They further showed that overexpression of wild-type ANGPTL3 could increase plasma triglycerides in these mice (15).”

    From Regulation of lipoprotein metabolism by ANGPTL3, ANGPTL4, and ANGPTL8 (2021) · cites this paper as [15]

  • ANGPTL3 is expressed in and secreted from the liver and circulates in the bloodstream.

    “ANGPTL3 is expressed in and secreted from the liver and circulates in the bloodstream (15, 40, 72, 103).”

    From Regulation of lipoprotein metabolism by ANGPTL3, ANGPTL4, and ANGPTL8 (2021) · cites this paper as [15]

  • Overexpression or injection of ANGPTL3 into mice increases plasma triglycerides.

    “Overexpression or injection of ANGPTL3 into mice increases plasma triglycerides (15, 107).”

    From Regulation of lipoprotein metabolism by ANGPTL3, ANGPTL4, and ANGPTL8 (2021) · cites this paper as [15]

Citations

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Research works printed but not linked: 37

  1. Stanbury, J.B., Wyngaarden, J.B., Goldstein, J.L. & Brown, M.S. in The Metabolic Basis of Inherited Disease 5th edn (eds Herbert, P.N., Assmann, G., Gotto, A.M. Jr & Fredrickson, D.S.) 589–621 (McGraw-Hill, New York, 1983).
  2. Wetterau, J.R. et al. Absence of microsomal triglyceride transfer protein in individuals with abetalipoproteinemia. Science 258, 999–1001 (1992). · DOI
  3. Shoulders, C.C. et al. Abetalipoproteinemia is caused by defects of the gene encoding the 97 kDa subunit of a microsomal triglyceride transfer protein. Hum. Mol. Genet. 2, 2109–2116 (1993). · DOI
  4. Sharp, D. et al. Cloning and gene defects in microsomal triglyceride transfer protein associated with abetalipoproteinemia. Nature 365, 65–69 (1993). · DOI · Paper page
  5. Rehberg, E.F. et al. A novel abetalipoproteinemia genotype. Identification of a missense mutation in the 97-kDa subunit of the microsomal triglyceride transfer protein that prevents complex formation with protein disulfide isomerase. J. Biol. Chem. 271, 29945–29952 (1996). · DOI
  6. Narcisi, T.M. et al. Mutations of the microsomal triglyceride transfer-protein gene in abetalipoproteinemia. Am. J. Hum. Genet. 57, 1298–1310 (1995).
  7. Farese, R.V., Linton, M.F. & Young, S.G. Apolipoprotein-B gene mutations affecting cholesterol levels. J. Int. Med. 231, 643–652 (1992). · DOI
  8. Schonfeld, G. The hypobetalipoproteinemias. Annu. Rev. Nutr. 15, 23–34 (1995). · DOI
  9. Talmud, P.J. et al. Donor splice mutation generates a lipid-associated apolipoprotein B-27.6 in a patient with homozygous hypobetalipoproteinemia. J. Lipid Res. 35, 468–477 (1994). · DOI
  10. Welty, F.K., Ordovas, J., Schaefer, E.J., Wilson, P.W.F. & Young, S.G. Identification and molecular analysis of two apoB gene mutations causing low plasma cholesterol levels. Circulation 92, 2036–2040 (1995). · DOI
  11. Parhofer, K.G., Barrett, P.H.R., Bier, D.M. & Schonfeld, G. Positive linear correlations between the length of truncated apolipoprotein B and its secretion rate: in vivo studies in apoB-89, apoB-75, apoB-54.8, and apoB-31 heterozygotes. J. Lipid Res. 37, 844–852 (1996). · DOI
  12. Brooks-Wilson, A. et al. Mutations in ABC1 in Tangier disease and familial high-density lipoprotein deficiency. Nature Genet. 22, 336–345 (1999). · DOI · Paper page
  13. Bodzioch, M. et al. The gene encoding ATP-binding cassette transporter 1 is mutated in Tangier disease. Nature Genet. 22, 347–351 (1999). · DOI · Paper page
  14. Rust, S. et al. Tangier disease is caused by mutations in the gene encoding ATP-binding cassette transporter 1. Nature Genet. 22, 352–355 (1999). · DOI · Paper page
  15. Reue, K. & Doolittle, M.H. Naturally occurring mutations in mice affecting lipid transport and metabolism. J. Lipid Res. 37, 1387–1405 (1996). · DOI
  16. Welsh, C.L. et al. Genetic regulation of cholesterol homeostasis: chromosomal organization of candidate genes. J. Lipid Res. 37, 1406–1421 (1996). · DOI
  17. Purcell-Huynh, D.A. et al. Genetic factors in lipoprotein metabolism. Analysis of a genetic cross between inbred mouse strains NZB/BINJ and SM/J using a complete linkage map approach. J. Clin. Invest. 96, 1845–1858 (1995). · DOI
  18. Kondo, K., Nozawa, K., Tomita, T. & Ezaki, K. Inbred strains resulting from Japanese mice. Bulletin of the Experimental Animals 6, 107–112 (1957). · DOI
  19. Nakamura, M. & Yamada, K. Studies on a diabetic (KK) strain of mice. Diabetologia 3, 212–221 (1967). · DOI
  20. Nakamura, M. A diabetic strain of the mouse. Proc. Jpn. Acad. 38, 348–352 (1962). · DOI
  21. Shiraki, T., Yoshioka, S. & Horikoshi, H. Difference of triglyceride metabolism between two colonies of diabetic KK-mice. Diabetes Frontier 4, 641 (1993).
  22. Fujiwara, T. et al. Identification and chromosomal assignment of USP1, a novel gene encoding a human ubiquitin-specific protease. Genomics 54, 155–158 (1998). · DOI
  23. Reaven, G.M. Non-insulin-dependent diabetes mellitus, abnormal lipoprotein metabolism, and atherosclerosis. Metabolism 36, 1–8 (1987). · DOI
  24. Greenfield, M., Kolterman, O., Olesfsky, J. & Reaven, G.M. Mechanism of hypertriglyceridaemia in diabetic patients with fasting hyperglycaemia. Diabetologia 18, 441–446 (1980). · DOI
  25. Greenfield, M.S., Doberne, L., Rosenthal, M., Vreman, H.J. & Reaven, G.M. Lipid metabolism in non-insulin-dependent diabetes mellitus: effect of glipizide therapy. Arch. Intern. Med. 142, 1498–1500 (1982). · DOI
  26. Davis, S. et al. Isolation of angiopoietin-1, a ligand for the Tie2 receptor, by secretion-trap expression cloning. Cell 87, 1161–1169 (1996). · DOI · Paper page
  27. Maisonpierre, P.C. et al. Angiopoietin-2, a natural antagonist for Tie2 that disrupts in vivo angiogenesis. Science 277, 55–60 (1997). · DOI · Paper page
  28. Valenzuela, D.M. et al. Angiopoietin 3 and 4: diverging gene counterparts in mice and humans. Proc. Natl Acad. Sci. USA 96, 1904–1909 (1999). · DOI
  29. Procopio, W.N., Pelavin, P.I., Lee, W.M.F. & Yeilding, N.M. Angiopoietin-1 and –2 coiled coil domains mediate distinct homo-oligomerization patterns, but fibrinogen-like domains mediate ligand activity. J. Biol. Chem. 274, 30196–30201 (1999). · DOI
  30. Brunzell, J.D., Schrott, H.G., Motulsky, A.G. & Bierman, E.L. Myocardial infarction in the familial forms of hypertriglyceridemia. Metabolism 25, 313–320 (1976). · DOI
  31. Goldstein, J.L., Schrott, H.G., Hazzard, W.R., Bierman, E.L. & Motulsky, A.G. Hyperlipidemia in coronary heart disease. II. Genetic analysis of lipid levels in 176 families and delineation of a new inherited disorder, combined hyperlipidemia. J.Clin. Invest. 52, 1544–1568 (1973). · DOI
  32. Genest, J.J. Jr et al. Familial lipoprotein disorders in patients with premature coronary artery disease. Circulation 85, 2025–2033 (1992). · DOI
  33. Schaefer, E.J., Genest, J.J. Jr, Ordovas, J.M., Salem, D.N. & Wilson, P.W. Familial lipoprotein disorders and premature coronary artery disease. Atherosclerosis 108, S41–S54 (1994). · DOI
  34. Lander, E.S. et al. MAPMAKER: an interactive computer package for constructing primary genetic linkage maps of experimental and natural populations. Genomics 1, 174–181 (1987). · DOI
  35. Miyake, S. et al. Efficient generation of recombinant adenoviruses using adenovirus DNA-terminal protein complex and a cosmid bearing the full-length virus genome. Proc. Natl Acad. Sci. USA 93, 1320–1324 (1996). · DOI
  36. Kanegae, Y., Makimura, M. & Saito, I. A simple and efficient method for purification of infectious recombinant adenovirus. Jpn. J. Med. Sci. Biol. 47, 157–166 (1994). · DOI
  37. Laemmli, U.K. Cleavage of structure proteins during the assembly of the head of bacteriophage T4. Nature 227, 680–685 (1970). · DOI · Paper page

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Metadata

Authors
Koishi, R., Ando, Y., Ono, M., Shimamura, M., Yasumo, H., Fujiwara, T., Horikoshi, H., & Furukawa, H.
Venue
Nature Genetics
Publisher
Springer Science and Business Media LLC
Published
2002-01-14
Volume
30
Issue
2
Pages
151-157
ISSN
  • 1061-4036
  • 1546-1718
DOI
10.1038/ng814
Cited by
379
References
1
Language
en
Licence
www.springer.com/tdm (tdm)

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