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

Wnt2  -  wingless-type MMTV integration site family...

Mus musculus

Synonyms: 2610510E18Rik, INT-1-related protein, IRP, Int1l1, Irp, ...
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 Wnt2

  • Wnt2, 3 and 5a mRNAs were also lower in endometrial carcinoma compared with normal endometrium [1].
  • We have developed a novel monoclonal antibody against the NH(2) terminus of the human Wnt-2 ligand that induces apoptosis in human melanoma cells overexpressing Wnt-2 [2].
  • Iron-repressible outer membrane proteins (Irp) and siderophore production of Yersinia enterocolitica, serotype 08, were subjected to analysis [3].

High impact information on Wnt2

  • Expression of multiple novel Wnt-1/int-1-related genes during fetal and adult mouse development [4].
  • IRP induction by H2O2 appears to involve the disassembly of its cubane 4Fe-4S cluster and occurs even in the presence of the protein synthesis inhibitor cycloheximide [5].
  • In this study, we establish the function of NO as a signaling molecule to IRP and as a regulator of mRNA translation and stabilization [6].
  • Iron-regulatory protein (IRP) is a master regulator of cellular iron homeostasis [6].
  • Recent work revealed that nitric oxide (NO) can mimic the effect of iron chelation on IRP and on ferritin mRNA translation, whereas the stabilization of transferrin receptor mRNA following NO-mediated IRP activation could not be observed in gamma-interferon/lipopolysaccharide-stimulated murine macrophages [6].

Chemical compound and disease context of Wnt2


Biological context of Wnt2


Anatomical context of Wnt2


Associations of Wnt2 with chemical compounds

  • At the amino acid level, m-irp and h-irp share 97% of amino acids including all 24 cysteine residues, which are highly conserved among members of the int-1 family [9].
  • Twenty-four Cys residues were conserved among vertebrate Wnt2b and Wnt2 orthologs [13].
  • Moreover, we show that 3-morpholinosydnonimine (SIN-1), a chemical which releases both NO and O2-. enhanced IRE binding activity of IRP only in the presence of superoxide dismutase (SOD) [14].
  • The IRE/IRP regulatory system receives additional input by oxidative stress in the form of H(2)O(2) that leads to rapid activation of IRP1 [15].
  • We show that in vitro RNA-binding can be inhibited for each IRP by the alkylation of free sulfhydryl groups with N-ethylmaleimide, or by oxidation with diamide [16].

Other interactions of Wnt2

  • No difference could be observed between transgenic and control lungs in either the level or distribution of Bmp4, Wnt2 and Fgf7 RNA [17].
  • Finally, Wnt-2, Wnt-4 and Wnt-5b were shown to be regulated by ovarian hormones [18].
  • These results suggest that Wnt2 is required for the proper vascularisation of the mouse placenta and the placental defects in Wnt2-deficient mice result in a reduction in birthweight and perinatal lethality [7].
  • Characterization of Wnt-1 and Wnt-2 induced growth alterations and signaling pathways in NIH3T3 fibroblasts [12].
  • We show that early cardiac expression of one of these genes, Wnt2, mirrors that of GATA6 in vitro and in vivo [19].

Analytical, diagnostic and therapeutic context of Wnt2

  • Mice deficient in Wnt2, generated by gene targeting, displayed runting and approximately 50% died perinatally [7].
  • The spatial and temporal expression of Wnt-2 in the developing mouse mammary gland was studied by in situ hybridization, quantitative RT-PCR, and Northern analysis [20].
  • Gel retardation assays performed on cytoplasmic extracts of transfected cells using an iron-responsive element (IRE) as a probe revealed that in overexpressing cells, the iron-regulatory protein (IRP) had a conformation with a high RNA-binding affinity, thus leading to translational repression of the endogenous L-ferritin synthesis [21].
  • Both vaccines induced significant anti-IRP antibodies as measured by enzyme immunoassay and by Western immunoblot with both M986 and 44/76 outer membranes [22].
  • Although IRP binding activity is predominantly located in the cytosol (90%), there was increased IRP/IRE binding activity in both cytosolic and membrane fractions when the cells were treated with deferoxamine, and decreased binding activity after treatment with iron [23].


  1. Expression and hormone regulation of Wnt2, 3, 4, 5a, 7a, 7b and 10b in normal human endometrium and endometrial carcinoma. Bui, T.D., Zhang, L., Rees, M.C., Bicknell, R., Harris, A.L. Br. J. Cancer (1997) [Pubmed]
  2. An anti-Wnt-2 monoclonal antibody induces apoptosis in malignant melanoma cells and inhibits tumor growth. You, L., He, B., Xu, Z., Uematsu, K., Mazieres, J., Fujii, N., Mikami, I., Reguart, N., McIntosh, J.K., Kashani-Sabet, M., McCormick, F., Jablons, D.M. Cancer Res. (2004) [Pubmed]
  3. Virulence of Yersinia enterocolitica is closely associated with siderophore production, expression of an iron-repressible outer membrane polypeptide of 65,000 Da and pesticin sensitivity. Heesemann, J., Hantke, K., Vocke, T., Saken, E., Rakin, A., Stojiljkovic, I., Berner, R. Mol. Microbiol. (1993) [Pubmed]
  4. Expression of multiple novel Wnt-1/int-1-related genes during fetal and adult mouse development. Gavin, B.J., McMahon, J.A., McMahon, A.P. Genes Dev. (1990) [Pubmed]
  5. Rapid responses to oxidative stress mediated by iron regulatory protein. Pantopoulos, K., Hentze, M.W. EMBO J. (1995) [Pubmed]
  6. Nitric oxide signaling to iron-regulatory protein: direct control of ferritin mRNA translation and transferrin receptor mRNA stability in transfected fibroblasts. Pantopoulos, K., Hentze, M.W. Proc. Natl. Acad. Sci. U.S.A. (1995) [Pubmed]
  7. Targeted disruption of the Wnt2 gene results in placentation defects. Monkley, S.J., Delaney, S.J., Pennisi, D.J., Christiansen, J.H., Wainwright, B.J. Development (1996) [Pubmed]
  8. Use of transgenic mice model for understanding the placentation: towards clinical applications in human obstetrical pathologies? Sapin, V., Blanchon, L., Serre, A.F., Lémery, D., Dastugue, B., Ward, S.J. Transgenic Res. (2001) [Pubmed]
  9. Nucleotide sequence, chromosomal localization and developmental expression of the mouse int-1-related gene. McMahon, J.A., McMahon, A.P. Development (1989) [Pubmed]
  10. Evidence from normal expression and targeted misexpression that bone morphogenetic protein (Bmp-4) plays a role in mouse embryonic lung morphogenesis. Bellusci, S., Henderson, R., Winnier, G., Oikawa, T., Hogan, B.L. Development (1996) [Pubmed]
  11. Classical genotropic versus kinase-initiated regulation of gene transcription by the estrogen receptor alpha. Almeida, M., Han, L., O'brien, C.A., Kousteni, S., Manolagas, S.C. Endocrinology (2006) [Pubmed]
  12. Characterization of Wnt-1 and Wnt-2 induced growth alterations and signaling pathways in NIH3T3 fibroblasts. Bafico, A., Gazit, A., Wu-Morgan, S.S., Yaniv, A., Aaronson, S.A. Oncogene (1998) [Pubmed]
  13. Molecular evolution of Wnt2b orthologs. Katoh, M. Int. J. Oncol. (2005) [Pubmed]
  14. Modulation of iron regulatory protein functions. Further insights into the role of nitrogen- and oxygen-derived reactive species. Bouton, C., Raveau, M., Drapier, J.C. J. Biol. Chem. (1996) [Pubmed]
  15. Modulation of cellular iron metabolism by hydrogen peroxide. Effects of H2O2 on the expression and function of iron-responsive element-containing mRNAs in B6 fibroblasts. Caltagirone, A., Weiss, G., Pantopoulos, K. J. Biol. Chem. (2001) [Pubmed]
  16. Differential modulation of the RNA-binding proteins IRP-1 and IRP-2 in response to iron. IRP-2 inactivation requires translation of another protein. Henderson, B.R., Kühn, L.C. J. Biol. Chem. (1995) [Pubmed]
  17. Involvement of Sonic hedgehog (Shh) in mouse embryonic lung growth and morphogenesis. Bellusci, S., Furuta, Y., Rush, M.G., Henderson, R., Winnier, G., Hogan, B.L. Development (1997) [Pubmed]
  18. Developmental and hormonal regulation of Wnt gene expression in the mouse mammary gland. Weber-Hall, S.J., Phippard, D.J., Niemeyer, C.C., Dale, T.C. Differentiation (1994) [Pubmed]
  19. Wnt2 is a direct downstream target of GATA6 during early cardiogenesis. Alexandrovich, A., Arno, M., Patient, R.K., Shah, A.M., Pizzey, J.A., Brewer, A.C. Mech. Dev. (2006) [Pubmed]
  20. Localization and quantification of Wnt-2 gene expression in mouse mammary development. Bühler, T.A., Dale, T.C., Kieback, C., Humphreys, R.C., Rosen, J.M. Dev. Biol. (1993) [Pubmed]
  21. Overexpression of the ferritin H subunit in cultured erythroid cells changes the intracellular iron distribution. Picard, V., Renaudie, F., Porcher, C., Hentze, M.W., Grandchamp, B., Beaumont, C. Blood (1996) [Pubmed]
  22. Expression of Neisseria meningitidis iron-regulated outer membrane proteins, including a 70-kilodalton transferrin receptor, and their potential for use as vaccines. Banerjee-Bhatnagar, N., Frasch, C.E. Infect. Immun. (1990) [Pubmed]
  23. The intracellular location of iron regulatory proteins is altered as a function of iron status in cell cultures and rat brain. Piñero, D.J., Li, N., Hu, J., Beard, J.L., Connor, J.R. J. Nutr. (2001) [Pubmed]
WikiGenes - Universities