The world's first wiki where authorship really matters (Nature Genetics, 2008). Due credit and reputation for authors. Imagine a global collaborative knowledge base for original thoughts. Search thousands of articles and collaborate with scientists around the globe.

wikigene or wiki gene protein drug chemical gene disease author authorship tracking collaborative publishing evolutionary knowledge reputation system wiki2.0 global collaboration genes proteins drugs chemicals diseases compound
Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)



Gene Review

ANGPTL3  -  angiopoietin-like 3

Homo sapiens

Synonyms: ANG-5, ANGPT5, ANL3, Angiopoietin-5, Angiopoietin-like protein 3, ...
Welcome! If you are familiar with the subject of this article, you can contribute to this open access knowledge base by deleting incorrect information, restructuring or completely rewriting any text. Read more.

Disease relevance of ANGPTL3

  • METHODS AND RESULTS: Angptl3-deficient mice showed low plasma HDL cholesterol and HDL phospholipid (PL), and which were increased by ANGPTL3 supplementation via adenovirus [1].

High impact information on ANGPTL3

  • Furthermore, a cleavage-resistant mutant of ANGPTL3 was determined to be less active than wild-type ANGPTL3 in increasing mouse plasma triglyceride levels but not in inhibiting lipoprotein lipase activity [2].
  • Protein region important for regulation of lipid metabolism in angiopoietin-like 3 (ANGPTL3): ANGPTL3 is cleaved and activated in vivo [2].
  • Angiopoietin-like 3 (ANGPTL3) is a secreted protein that is mainly expressed in the liver and regulates lipid metabolism by inhibiting the lipolysis of triglyceriderich lipoproteins [2].
  • Serial deletion and point mutation of Angptl3 promoter identified an LXR response element (LXRE) [3].
  • By screening expressed sequence tag data bases for homologies to a consensus FBN-like motive, we have identified ANGPTL3, a liver-specific, secreted factor consisting of an N-terminal coiled-coil domain and the C-terminal FBN-like domain [4].

Biological context of ANGPTL3


Anatomical context of ANGPTL3

  • We conclude that ANGPTL3 is a liver-derived lipolytic factor targeting on adipocyte [8].
  • Furthermore, the mRNA level of ANGPTL3 and -4 in liver and the mRNA level of ANGPTL4 in white adipose tissue were significantly higher in genetically obese pigs than in their lean counterparts [6].
  • We evaluated the possible association between plasma ANGPTL3 level and carotid artery intima-media thickness (CA-IMT) and femoral artery intima-media thickness (FA-IMT) in healthy human subjects [9].

Associations of ANGPTL3 with chemical compounds

  • Using deletion mutants of human ANGPTL3, we demonstrated that the N-terminal coiled-coil domain-containing fragment-(17-207) and not the C-terminal fibrinogen-like domain-containing fragment-(207-460) increased the plasma triglyceride levels in mice [2].
  • Furthermore, ANGPTL3 activated the lipolysis to stimulate the release of FFA and glycerol from adipocytes [8].
  • Taken together, our data demonstrate that ANGPTL3 is the first member of the angiopoietin-like family of secreted factors binding to integrin alpha(v)beta(3) and suggest a possible role in the regulation of angiogenesis [4].
  • The level of ANGPTL3 mRNA was increased approximately 2.2-fold in the livers of streptozotocin (STZ) diabetic mice, and this effect was reversed by administration of insulin [7].
  • The positive association between ANGPTL3 and CA-IMT remained significant after adjustment for age, sex, smoking, body mass index, systolic blood pressure, plasma glucose, insulin resistance index, triglyceride, and high-density and low-density lipoprotein cholesterol levels [9].

Regulatory relationships of ANGPTL3

  • To elucidate the mechanism by which PPARbeta represses angptl3 promoter activity, reporter constructs were prepared and transfection analysis carried out [10].

Other interactions of ANGPTL3


Analytical, diagnostic and therapeutic context of ANGPTL3


  1. Angiopoietin-like protein3 regulates plasma HDL cholesterol through suppression of endothelial lipase. Shimamura, M., Matsuda, M., Yasumo, H., Okazaki, M., Fujimoto, K., Kono, K., Shimizugawa, T., Ando, Y., Koishi, R., Kohama, T., Sakai, N., Kotani, K., Komuro, R., Ishida, T., Hirata, K., Yamashita, S., Furukawa, H., Shimomura, I. Arterioscler. Thromb. Vasc. Biol. (2007) [Pubmed]
  2. Protein region important for regulation of lipid metabolism in angiopoietin-like 3 (ANGPTL3): ANGPTL3 is cleaved and activated in vivo. Ono, M., Shimizugawa, T., Shimamura, M., Yoshida, K., Noji-Sakikawa, C., Ando, Y., Koishi, R., Furukawa, H. J. Biol. Chem. (2003) [Pubmed]
  3. Angiopoietin-like protein 3 mediates hypertriglyceridemia induced by the liver X receptor. Inaba, T., Matsuda, M., Shimamura, M., Takei, N., Terasaka, N., Ando, Y., Yasumo, H., Koishi, R., Makishima, M., Shimomura, I. J. Biol. Chem. (2003) [Pubmed]
  4. ANGPTL3 stimulates endothelial cell adhesion and migration via integrin alpha vbeta 3 and induces blood vessel formation in vivo. Camenisch, G., Pisabarro, M.T., Sherman, D., Kowalski, J., Nagel, M., Hass, P., Xie, M.H., Gurney, A., Bodary, S., Liang, X.H., Clark, K., Beresini, M., Ferrara, N., Gerber, H.P. J. Biol. Chem. (2002) [Pubmed]
  5. Identification of a mammalian angiopoietin-related protein expressed specifically in liver. Conklin, D., Gilbertson, D., Taft, D.W., Maurer, M.F., Whitmore, T.E., Smith, D.L., Walker, K.M., Chen, L.H., Wattler, S., Nehls, M., Lewis, K.B. Genomics (1999) [Pubmed]
  6. Cloning, chromosome mapping and expression characteristics of porcine ANGPTL3 and -4. Feng, S.Q., Chen, X.D., Xia, T., Gan, L., Qiu, H., Dai, M.H., Zhou, L., Peng, Y., Yang, Z.Q. Cytogenet. Genome Res. (2006) [Pubmed]
  7. ANGPTL3 is increased in both insulin-deficient and -resistant diabetic states. Inukai, K., Nakashima, Y., Watanabe, M., Kurihara, S., Awata, T., Katagiri, H., Oka, Y., Katayama, S. Biochem. Biophys. Res. Commun. (2004) [Pubmed]
  8. Angiopoietin-like protein 3, a hepatic secretory factor, activates lipolysis in adipocytes. Shimamura, M., Matsuda, M., Kobayashi, S., Ando, Y., Ono, M., Koishi, R., Furukawa, H., Makishima, M., Shimomura, I. Biochem. Biophys. Res. Commun. (2003) [Pubmed]
  9. Association between plasma angiopoietin-like protein 3 and arterial wall thickness in healthy subjects. Hatsuda, S., Shoji, T., Shinohara, K., Kimoto, E., Mori, K., Fukumoto, S., Koyama, H., Emoto, M., Nishizawa, Y. J. Vasc. Res. (2007) [Pubmed]
  10. Ligand-activated PPARbeta efficiently represses the induction of LXR-dependent promoter activity through competition with RXR. Matsusue, K., Miyoshi, A., Yamano, S., Gonzalez, F.J. Mol. Cell. Endocrinol. (2006) [Pubmed]
WikiGenes - Universities