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

AGRN  -  agrin

Gallus gallus

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 AGRN


High impact information on AGRN


Chemical compound and disease context of AGRN

  • The early appearance of agrin mRNA coincides with the period during which acetylcholine receptors are being organized on ciliary ganglion neurons, consistent with the possibility that agrin contributes to neuron-neuron synapse formation in this pathway [5].

Biological context of AGRN


Anatomical context of AGRN


Associations of AGRN with chemical compounds


Regulatory relationships of AGRN

  • However, a time course of agrin-induced clustering that focused on filamin revealed that most of the early AChR clusters (3-6 h) were not associated with detectable amounts of cytoskeletal material [12].

Other interactions of AGRN

  • Even a muscle form of agrin that lacks intrinsic clustering activities by itself, significantly enhances neuregulin-induced clustering and insertion of AChRs [13].
  • Agrin is a proteoglycan that can inhibit neurite outgrowth from multiple neuronal types when present as a substrate [10].
  • Thus, our studies demonstrate that chick agrin is a HSPG that is prominent in the embryonic chick brain [14].
  • Laminin, nidogen, agrin, collagen IV, and XVIII are major constituents of the retinal basal lamina [15].

Analytical, diagnostic and therapeutic context of AGRN

  • Here, electron microscopy was used to determine the structure of agrin and to localize its binding site in laminin-1 [11].
  • The cellular origin of the agrin-like molecules at synapses was examined in cross-species cocultures in which the neurons and muscle cells were obtained from embryos of Xenopus laevis and Rana pipiens [16].
  • Immunocytochemistry demonstrated that agrin is expressed in developing brain, and is especially abundant in developing axonal tracts, in a distribution identical to the staining of the brain HSPG with monoclonal antibodies [14].
  • Reverse transcription-polymerase chain reaction (RT-PCR) of E9 chick brain mRNA confirmed the existence of this agrin isoform in brain, although the novel splice variant represents a minor fraction of agrin mRNA in brain [17].
  • The amino acid sequence of agrin encodes a protein with a molecular size of 220 kDa, whereas SDS-PAGE shows a diffuse band around 400 kDa [18].


  1. Developmental expression and alternative splicing of chick agrin RNA. Thomas, W.S., O'Dowd, D.K., Smith, M.A. Dev. Biol. (1993) [Pubmed]
  2. Agrin-deficient myotube retains its acetylcholine receptor aggregation ability when challenged with agrin. Pun, S., Ng, Y.P., Yang, J.F., Ip, N.Y., Tsim, K.W. J. Neurochem. (1997) [Pubmed]
  3. Agrin is a differentiation-inducing "stop signal" for motoneurons in vitro. Campagna, J.A., Rüegg, M.A., Bixby, J.L. Neuron (1995) [Pubmed]
  4. Cell-specific regulation of agrin RNA splicing in the chick ciliary ganglion. Smith, M.A., O'Dowd, D.K. Neuron (1994) [Pubmed]
  5. Agrin mRNA expression in the developing chick Edinger-Westphal nucleus. McAvoy, M., Smith, M.A., Fujii, J.T. Vis. Neurosci. (1996) [Pubmed]
  6. cDNA that encodes active agrin. Tsim, K.W., Ruegg, M.A., Escher, G., Kröger, S., McMahan, U.J. Neuron (1992) [Pubmed]
  7. Agrin induces phosphorylation of the nicotinic acetylcholine receptor. Wallace, B.G., Qu, Z., Huganir, R.L. Neuron (1991) [Pubmed]
  8. The agrin gene codes for a family of basal lamina proteins that differ in function and distribution. Ruegg, M.A., Tsim, K.W., Horton, S.E., Kröger, S., Escher, G., Gensch, E.M., McMahan, U.J. Neuron (1992) [Pubmed]
  9. Agrin-induced AChR aggregate formation requires cGMP and aggregate maturation requires activation of cGMP-dependent protein kinase. Jones, M.A., Werle, M.J. Mol. Cell. Neurosci. (2004) [Pubmed]
  10. Glycosaminoglycan-dependent and -independent inhibition of neurite outgrowth by agrin. Baerwald-de la Torre, K., Winzen, U., Halfter, W., Bixby, J.L. J. Neurochem. (2004) [Pubmed]
  11. Electron microscopic structure of agrin and mapping of its binding site in laminin-1. Denzer, A.J., Schulthess, T., Fauser, C., Schumacher, B., Kammerer, R.A., Engel, J., Ruegg, M.A. EMBO J. (1998) [Pubmed]
  12. Agrin induces alpha-actinin, filamin, and vinculin to co-localize with AChR clusters on cultured chick myotubes. Shadiack, A.M., Nitkin, R.M. J. Neurobiol. (1991) [Pubmed]
  13. Synergistic effects of neuregulin and agrin on muscle acetylcholine receptor expression. Li, Q., Esper, R.M., Loeb, J.A. Mol. Cell. Neurosci. (2004) [Pubmed]
  14. Agrin is a heparan sulfate proteoglycan. Tsen, G., Halfter, W., Kröger, S., Cole, G.J. J. Biol. Chem. (1995) [Pubmed]
  15. Composition, synthesis, and assembly of the embryonic chick retinal basal lamina. Halfter, W., Dong, S., Schurer, B., Osanger, A., Schneider, W., Ruegg, M., Cole, G.J. Dev. Biol. (2000) [Pubmed]
  16. Early appearance of and neuronal contribution to agrin-like molecules at embryonic frog nerve-muscle synapses formed in culture. Cohen, M.W., Godfrey, E.W. J. Neurosci. (1992) [Pubmed]
  17. Identification of a novel alternatively spliced agrin mRNA that is preferentially expressed in non-neuronal cells. Tsen, G., Napier, A., Halfter, W., Cole, G.J. J. Biol. Chem. (1995) [Pubmed]
  18. Agrin is a chimeric proteoglycan with the attachment sites for heparan sulfate/chondroitin sulfate located in two multiple serine-glycine clusters. Winzen, U., Cole, G.J., Halfter, W. J. Biol. Chem. (2003) [Pubmed]
WikiGenes - Universities