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

Chrd  -  chordin

Mus musculus

Synonyms: Chd, Chordin
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 Chrd


High impact information on Chrd

  • Extracellular levels of Sizzled and Chordin in the gastrula embryo and enzyme reaction constants were all in the 10(-8) M range, consistent with a physiological role in the regulation of dorsal-ventral patterning [2].
  • Recombinant Xenopus Chd binds to BMP-4 with high affinity (KD, 3 x 10(-10) M), binding specifically to BMPs but not to activin or TGF-beta1 [3].
  • Dorsoventral patterning in Xenopus: inhibition of ventral signals by direct binding of chordin to BMP-4 [3].
  • Chordin (Chd) is an abundant protein secreted by Spemann organizer tissue during gastrulation [3].
  • Here we show that mice double-homozygous mutants that are for chordin and noggin display severe defects in the development of the prosencephalon [4].

Biological context of Chrd

  • To elucidate roles of Chrd and Nog that are masked by the severe phenotype and early lethality of the double null, we have characterized embryos of the genotype Chrd(-/-);Nog(+/-) [5].
  • Transfection of ES cells with a pCS2/chordin expression vector or exposure to chordin-conditioned medium produced a more complex pattern of differentiation; ES cells formed neurons, mesenchymal cells as well as N-CAM-positive, nestin-positive neuroepithelial progenitors [6].
  • Spatiotemporal expression patterns of mammalian chordin during postgastrulation embryogenesis and in postnatal brain [7].
  • Expression of Chordin in the primordia of most major organs from 10.5 dpc, including the brain, lung, heart, liver, kidney, thymus, and gut, suggests multiple functions for Chordin in organogenesis, potentially by means of interactions with TGFbeta-like BMPs [7].
  • BMP binding proteins, noggin, chordin and DAN, act as antagonists and determine the bioavailability of BMPs for binding to cognate receptors to elicit the biological response [8].

Anatomical context of Chrd


Associations of Chrd with chemical compounds

  • Here, we demonstrate that mammalian Chordin binds heparin with an affinity similar to that of factors known to functionally interact with heparan sulfate proteoglycans (HSPGs) in tissues [12].
  • Furthermore, BMP-1DeltaEC3 cleaves chordin and requires Ca(2+) for activity [13].
  • Cell-surface heparan sulfate proteoglycans potentiate chordin antagonism of bone morphogenetic protein signaling and are necessary for cellular uptake of chordin [12].
  • Osteocalcin (OCN) mRNA levels decrease following both Tsg and Chd treatment [14].

Enzymatic interactions of Chrd

  • In vitro studies have shown BMP-1 and mTLL-1 capable of cleaving Chordin, an extracellular antagonist of BMP signaling, suggesting that these proteases might also serve to modulate BMP signaling and to coordinate the latter with ECM formation [15].

Regulatory relationships of Chrd

  • In the postnatal mouse brain, we demonstrate that Chordin is coexpressed with other components of the TGFbeta-like BMP signalling pathway in the cerebellum and hippocampus, sites of high synaptic plasticity, suggesting a role for Chordin in this process [7].
  • Tsg and Chd also inhibit alkaline phosphatase (ALP) activity in a dose-dependent manner [14].

Other interactions of Chrd

  • The mouse chordin and noggin genes (Chrd and Nog) are expressed in the organizer (the node) and its mesendodermal derivatives, including the prechordal plate, an organizing center for rostral development [5].
  • Further analysis revealed that cells which express Chrd activity are either absent in Hnf3beta mutant embryos or localised in heterotopic sites in Lim1 and Otx2 null mutants [16].
  • Chordin and Noggin are secreted bone morphogenetic protein (BMP) antagonists expressed in the mouse node, but not in the AVE [4].
  • Interestingly, the spatiotemporal expression patterns of CHL were distinct from those of chordin in many areas examined [11].
  • Chordin secreted by the mesendoderm is required for the correct expression of Tbx1 and other transcription factors involved in the development of the pharyngeal region [1].

Analytical, diagnostic and therapeutic context of Chrd


  1. The role of chordin/Bmp signals in mammalian pharyngeal development and DiGeorge syndrome. Bachiller, D., Klingensmith, J., Shneyder, N., Tran, U., Anderson, R., Rossant, J., De Robertis, E.M. Development (2003) [Pubmed]
  2. Embryonic dorsal-ventral signaling: secreted frizzled-related proteins as inhibitors of tolloid proteinases. Lee, H.X., Ambrosio, A.L., Reversade, B., De Robertis, E.M. Cell (2006) [Pubmed]
  3. Dorsoventral patterning in Xenopus: inhibition of ventral signals by direct binding of chordin to BMP-4. Piccolo, S., Sasai, Y., Lu, B., De Robertis, E.M. Cell (1996) [Pubmed]
  4. The organizer factors Chordin and Noggin are required for mouse forebrain development. Bachiller, D., Klingensmith, J., Kemp, C., Belo, J.A., Anderson, R.M., May, S.R., McMahon, J.A., McMahon, A.P., Harland, R.M., Rossant, J., De Robertis, E.M. Nature (2000) [Pubmed]
  5. Chordin and noggin promote organizing centers of forebrain development in the mouse. Anderson, R.M., Lawrence, A.R., Stottmann, R.W., Bachiller, D., Klingensmith, J. Development (2002) [Pubmed]
  6. Noggin and chordin have distinct activities in promoting lineage commitment of mouse embryonic stem (ES) cells. Gratsch, T.E., O'Shea, K.S. Dev. Biol. (2002) [Pubmed]
  7. Spatiotemporal expression patterns of mammalian chordin during postgastrulation embryogenesis and in postnatal brain. Scott, I.C., Steiglitz, B.M., Clark, T.G., Pappano, W.N., Greenspan, D.S. Dev. Dyn. (2000) [Pubmed]
  8. Interplay between bone morphogenetic proteins and cognate binding proteins in bone and cartilage development: noggin, chordin and DAN. Reddi, A.H. Arthritis Res. (2001) [Pubmed]
  9. The organizer of the mouse gastrula is composed of a dynamic population of progenitor cells for the axial mesoderm. Kinder, S.J., Tsang, T.E., Wakamiya, M., Sasaki, H., Behringer, R.R., Nagy, A., Tam, P.P. Development (2001) [Pubmed]
  10. The BMP antagonists Chordin and Noggin have essential but redundant roles in mouse mandibular outgrowth. Stottmann, R.W., Anderson, R.M., Klingensmith, J. Dev. Biol. (2001) [Pubmed]
  11. A novel chordin-like protein inhibitor for bone morphogenetic proteins expressed preferentially in mesenchymal cell lineages. Nakayama, N., Han , C.E., Scully, S., Nishinakamura, R., He, C., Zeni, L., Yamane, H., Chang, D., Yu, D., Yokota, T., Wen, D. Dev. Biol. (2001) [Pubmed]
  12. Cell-surface heparan sulfate proteoglycans potentiate chordin antagonism of bone morphogenetic protein signaling and are necessary for cellular uptake of chordin. Jasuja, R., Allen, B.L., Pappano, W.N., Rapraeger, A.C., Greenspan, D.S. J. Biol. Chem. (2004) [Pubmed]
  13. Deletion of epidermal growth factor-like domains converts mammalian tolloid into a chordinase and effective procollagen C-proteinase. Garrigue-Antar, L., François, V., Kadler, K.E. J. Biol. Chem. (2004) [Pubmed]
  14. Twisted gastrulation and chordin inhibit differentiation and mineralization in MC3T3-E1 osteoblast-like cells. Petryk, A., Shimmi, O., Jia, X., Carlson, A.E., Tervonen, L., Jarcho, M.P., O'connor, M.B., Gopalakrishnan, R. Bone (2005) [Pubmed]
  15. Use of Bmp1/Tll1 doubly homozygous null mice and proteomics to identify and validate in vivo substrates of bone morphogenetic protein 1/tolloid-like metalloproteinases. Pappano, W.N., Steiglitz, B.M., Scott, I.C., Keene, D.R., Greenspan, D.S. Mol. Cell. Biol. (2003) [Pubmed]
  16. Defects of the body plan of mutant embryos lacking Lim1, Otx2 or Hnf3beta activity. Kinder, S.J., Tsang, T.E., Ang, S.L., Behringer, R.R., Tam, P.P. Int. J. Dev. Biol. (2001) [Pubmed]
WikiGenes - Universities