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Gene Review

Fzd1  -  frizzled homolog 1 (Drosophila)

Mus musculus

Synonyms: AW227548, FZ-1, Frizzled-1, Fz-1, Fz1, ...
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Disease relevance of Fzd1


High impact information on Fzd1

  • G protein signaling from activated rat frizzled-1 to the beta-catenin-Lef-Tcf pathway [4].
  • The central effector of the Wnt pathway is beta-catenin, which undergoes stabilization upon binding of Wnt ligands to frizzled receptors [5].
  • Biochemical analysis demonstrates that Wnt7b can bind to Fzd1 and -10 on the cell surface and cooperatively activate canonical Wnt signaling with these receptors in the presence of LRP5 [6].
  • Fzd1, -4, and -7 are expressed primarily in the developing lung mesenchyme, and Fzd10 is expressed in airway epithelium [6].
  • Identification and cloning of a secreted protein related to the cysteine-rich domain of frizzled. Evidence for a role in endothelial cell growth control [7].

Biological context of Fzd1

  • In the course of the analysis of genes regulated by bone morphogenetic protein 2 in mesenchymal cells we found a significant induction of murine Frizzled-1 (mFz1) gene expression [8].
  • Asymmetric localization of Vangl2 and Fz3 indicate novel mechanisms for planar cell polarity in mammals [9].
  • WNT factors represent key mediators of many processes in animal development and homeostasis and act through a receptor complex comprised of members of the Frizzled and low density lipoprotein-related receptors (LRP) [10].
  • Our results indicated that activated Fz1 increases stability of beta-catenin, inhibits apoptosis, induces osteoblastogenesis, and inhibits adipogenesis [11].
  • The expression of eight murine Frizzled (1,3-9) genes was studied during mouse somitogenesis, in order to correlate the Wnt-dependent activation of myogenesis with the expression of specific Frizzled putative receptors [12].

Anatomical context of Fzd1

  • We report comprehensive analysis of Wnt and Fz expression in whole liver as well as individual cell types: freshly isolated and plated hepatocytes, biliary epithelial cells, normal and activated stellate and Kupffer cells, and sinusoidal endothelial cells (SECs) [13].
  • The same 14 Wnt and 7 Fz genes were expressed in both activated and normal stellate and Kupffer cells; only Fzb was expressed in their activated state [13].
  • Although only 6 Wnt and 5 Fz genes were expressed in freshly isolated hepatocytes, 8 Wnt genes, 7 Fz genes, and Fzb were expressed in plated hepatocytes [13].
  • We found that sFRP3 unexpectedly increased osteoblast differentiation, suggesting it may act through other mechanisms besides acting as a decoy receptor for Wnt's. INTRODUCTION: Secreted frizzled-related proteins (sFRPs) are a truncated form of frizzled receptor, missing both the transmembrane and cytosolic domains [14].
  • Collectively these findings suggest (1) a functional role for Wnt-producing thymic epithelium in determining TCF/LEF-mediated transcriptional regulation in Fz-bearing thymocytes, and (2) a role for defined Wnt-Fz interactions at successive stages of thymocyte maturation [15].

Associations of Fzd1 with chemical compounds

  • By using chimeric constructs in which N- and C-terminal segments of mFz1 were replaced by the corresponding parts of Xfz3 we demonstrated that the antagonistic activity resides in the cysteine-rich domain of the N-terminal part [8].
  • Wnt signaling, Ca2+, and cyclic GMP: visualizing Frizzled functions [16].
  • The results show that the main families in the human genome, Glutamate, Rhodopsin, Adhesion, Frizzled, and Secretin, arose before the split of nematodes from the chordate lineage [17].

Physical interactions of Fzd1

  • Our results in combination with work from Xenopus laevis (not shown) lead us to believe that Wnt-4 binds both canonical and noncanonical Frizzled receptors, thereby activating Wnt signaling pathways that may each contribute to kidney tubulogenesis [18].

Regulatory relationships of Fzd1


Other interactions of Fzd1

  • Wnts are extracellular ligands that bind to frizzled (Fz) receptors at the membrane, canonically inducing beta-catenin nuclear translocation and activation [13].
  • Although 12 Wnt and 7 Fz genes were expressed in biliary tree, additional Fz9 and Fzb were only expressed in cultured biliary epithelial cells [13].
  • Oligonucleotides for the 19 Wnt, 10 frizzled receptors genes, and secreted Frizzled-related protein-1 (sFRP or Fzb) were synthesized based on the available sequences [13].
  • Thus, casein kinase 2 is shown to be regulated by Wnt3a and essential to stimulation of the Frizzled-1/beta-catenin/Lef-Tcf pathway [19].
  • We ectopically expressed constitutively active chimeras between Wnt8 and Fz1 or Fz2 in preadipocytes and mesenchymal precursor cells [11].

Analytical, diagnostic and therapeutic context of Fzd1


  1. Activation of the beta-catenin/Lef-Tcf pathway is obligate for formation of primitive endoderm by mouse F9 totipotent teratocarcinoma cells in response to retinoic acid. Liu, T., Lee, Y.N., Malbon, C.C., Wang, H.Y. J. Biol. Chem. (2002) [Pubmed]
  2. Activation of rat frizzled-1 promotes Wnt signaling and differentiation of mouse F9 teratocarcinoma cells via pathways that require Galpha(q) and Galpha(o) function. Liu, T., Liu, X., Wang, H., Moon, R.T., Malbon, C.C. J. Biol. Chem. (1999) [Pubmed]
  3. Frizzled A, a novel angiogenic factor: promises for cardiac repair. Barandon, L., Couffinhal, T., Dufourcq, P., Ezan, J., Costet, P., Daret, D., Deville, C., Duplàa, C. European journal of cardio-thoracic surgery : official journal of the European Association for Cardio-thoracic Surgery. (2004) [Pubmed]
  4. G protein signaling from activated rat frizzled-1 to the beta-catenin-Lef-Tcf pathway. Liu, T., DeCostanzo, A.J., Liu, X., Wang Hy, n.u.l.l., Hallagan, S., Moon, R.T., Malbon, C.C. Science (2001) [Pubmed]
  5. Somatic activation of beta-catenin bypasses pre-TCR signaling and TCR selection in thymocyte development. Gounari, F., Aifantis, I., Khazaie, K., Hoeflinger, S., Harada, N., Taketo, M.M., von Boehmer, H. Nat. Immunol. (2001) [Pubmed]
  6. Wnt7b activates canonical signaling in epithelial and vascular smooth muscle cells through interactions with Fzd1, Fzd10, and LRP5. Wang, Z., Shu, W., Lu, M.M., Morrisey, E.E. Mol. Cell. Biol. (2005) [Pubmed]
  7. Identification and cloning of a secreted protein related to the cysteine-rich domain of frizzled. Evidence for a role in endothelial cell growth control. Duplàa, C., Jaspard, B., Moreau, C., D'Amore, P.A. Circ. Res. (1999) [Pubmed]
  8. Murine Frizzled-1 behaves as an antagonist of the canonical Wnt/beta-catenin signaling. Roman-Roman, S., Shi, D.L., Stiot, V., Haÿ, E., Vayssière, B., Garcia, T., Baron, R., Rawadi, G. J. Biol. Chem. (2004) [Pubmed]
  9. Asymmetric localization of Vangl2 and Fz3 indicate novel mechanisms for planar cell polarity in mammals. Montcouquiol, M., Sans, N., Huss, D., Kach, J., Dickman, J.D., Forge, A., Rachel, R.A., Copeland, N.G., Jenkins, N.A., Bogani, D., Murdoch, J., Warchol, M.E., Wenthold, R.J., Kelley, M.W. J. Neurosci. (2006) [Pubmed]
  10. Functional characterization of WNT7A signaling in PC12 cells: interaction with A FZD5 x LRP6 receptor complex and modulation by Dickkopf proteins. Caricasole, A., Ferraro, T., Iacovelli, L., Barletta, E., Caruso, A., Melchiorri, D., Terstappen, G.C., Nicoletti, F. J. Biol. Chem. (2003) [Pubmed]
  11. Wnt signaling inhibits adipogenesis through beta-catenin-dependent and -independent mechanisms. Kennell, J.A., MacDougald, O.A. J. Biol. Chem. (2005) [Pubmed]
  12. Differential expression of the Wnt putative receptors Frizzled during mouse somitogenesis. Borello, U., Buffa, V., Sonnino, C., Melchionna, R., Vivarelli, E., Cossu, G. Mech. Dev. (1999) [Pubmed]
  13. Wnt'er in liver: Expression of Wnt and frizzled genes in mouse. Zeng, G., Awan, F., Otruba, W., Muller, P., Apte, U., Tan, X., Gandhi, C., Demetris, A.J., Monga, S.P. Hepatology (2007) [Pubmed]
  14. Effects of secreted frizzled-related protein 3 on osteoblasts in vitro. Chung, Y.S., Baylink, D.J., Srivastava, A.K., Amaar, Y., Tapia, B., Kasukawa, Y., Mohan, S. J. Bone Miner. Res. (2004) [Pubmed]
  15. Thymic epithelial cells provide WNT signals to developing thymocytes. Pongracz, J., Hare, K., Harman, B., Anderson, G., Jenkinson, E.J. Eur. J. Immunol. (2003) [Pubmed]
  16. Wnt signaling, Ca2+, and cyclic GMP: visualizing Frizzled functions. Wang, H.Y., Malbon, C.C. Science (2003) [Pubmed]
  17. The repertoire of G-protein-coupled receptors in fully sequenced genomes. Fredriksson, R., Schiöth, H.B. Mol. Pharmacol. (2005) [Pubmed]
  18. Wnt-4 activates the canonical beta-catenin-mediated Wnt pathway and binds Frizzled-6 CRD: functional implications of Wnt/beta-catenin activity in kidney epithelial cells. Lyons, J.P., Mueller, U.W., Ji, H., Everett, C., Fang, X., Hsieh, J.C., Barth, A.M., McCrea, P.D. Exp. Cell Res. (2004) [Pubmed]
  19. Casein kinase 2 Is activated and essential for Wnt/beta-catenin signaling. Gao, Y., Wang, H.Y. J. Biol. Chem. (2006) [Pubmed]
  20. A possible role for the canonical Wnt pathway in endocrine cell development in chicks. Pedersen, A.H., Heller, R.S. Biochem. Biophys. Res. Commun. (2005) [Pubmed]
  21. Expression of Frizzled genes in developing and postnatal hair follicles. Reddy, S.T., Andl, T., Lu, M.M., Morrisey, E.E., Millar, S.E. J. Invest. Dermatol. (2004) [Pubmed]
  22. Expression of frizzled genes in mouse costochondral chondrocytes. Xu, L., Tan, L., Goldring, M.B., Olsen, B.R., Li, Y. Matrix Biol. (2001) [Pubmed]
  23. Identification of a Wnt-responsive signal transduction pathway in primary endothelial cells. Wright, M., Aikawa, M., Szeto, W., Papkoff, J. Biochem. Biophys. Res. Commun. (1999) [Pubmed]
  24. Involvement of FrzA/sFRP-1 and the Wnt/frizzled pathway in ischemic preconditioning. Barandon, L., Dufourcq, P., Costet, P., Moreau, C., Allières, C., Daret, D., Dos Santos, P., Daniel Lamazière, J.M., Couffinhal, T., Duplàa, C. Circ. Res. (2005) [Pubmed]
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