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)
 

Links

 

Gene Review

Efna5  -  ephrin A5

Rattus norvegicus

Synonyms: AL-1, EPH-related receptor tyrosine kinase ligand 7, Ephrin-A5, Eplg7, LERK-7, ...
 
 
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 Efna5

  • Previous experiments identified AL-1 as a glycosylphosphatidylinositol (GPI)-linked ligand for the Eph-related receptor, REK7, and showed that a REK7-IgG fusion protein blocks axon bundling in co-cultures of cortical neurons on astrocytes, suggesting a role for REK7 and AL-1 in axon fasciculation [1].
 

High impact information on Efna5

  • Three putative receptors for ephrin-A5 -- EphA3, EphA4 and EphA5 -- showed distinct expression patterns in the developing thalamus [2].
  • The graded distributions of ephrin-A5 in the developing subplate and cortex and the expression of its receptors in the thalamus are consistent with the notion that the Eph ligands and their receptors may function in the topographic mapping of thalamic axons to specific cortical areas [2].
  • Regional differences in the developing cerebral cortex revealed by ephrin-A5 expression [2].
  • The Eph ligand ephrin-A5 was expressed in three distinct gradients during the development of the telencephalon [2].
  • Analysis of the effects of Lerk2 on both the morphology and the cytoskeleton of cortical neurons suggests a mechanism of action different from that of AL-1, a GPI-linked Eph ligand having similar repellant activity [3].
 

Biological context of Efna5

 

Anatomical context of Efna5

  • Development of inhibition by ephrin-A5 on outgrowth of embryonic spinal motor neurites [5].
  • Subsequent identification of RAGS, the chick homologue of AL-1, as a repellent axon guidance molecule in the developing chick visual system led to speculation that AL-1, expressed on astrocytes, provides a repellent stimulus for cortical axons, inducing them to bundle as an avoidance mechanism [1].
  • AL-1-induced growth cone collapse of rat cortical neurons is correlated with REK7 expression and rearrangement of the actin cytoskeleton [1].
  • These results demonstrate a progressive development of sensitivity to ephrin-A5, and suggest a divergence in this sensitivity between rostral and caudal spinal cord neurites [5].
  • These data suggest a role for REK7 and AL-1 in the patterning of axonal connections in the developing cortex, hippocampus and visual system [1].
 

Associations of Efna5 with chemical compounds

 

Other interactions of Efna5

  • The developmentally associated growth inhibitors ephrin-A5, ephB1, semaphorin IIIa, and neuropilin 1 are also induced in the early phases of the sprouting response [7].
 

Analytical, diagnostic and therapeutic context of Efna5

  • Three monoclonal antibodies (AL-1 to AL-3) that bound to intact laminin in a solid-phase radioimmunoassay were chosen for further analysis [8].

References

  1. AL-1-induced growth cone collapse of rat cortical neurons is correlated with REK7 expression and rearrangement of the actin cytoskeleton. Meima, L., Kljavin, I.J., Moran, P., Shih, A., Winslow, J.W., Caras, I.W. Eur. J. Neurosci. (1997) [Pubmed]
  2. Regional differences in the developing cerebral cortex revealed by ephrin-A5 expression. Mackarehtschian, K., Lau, C.K., Caras, I., McConnell, S.K. Cereb. Cortex (1999) [Pubmed]
  3. Lerk2 (ephrin-B1) is a collapsing factor for a subset of cortical growth cones and acts by a mechanism different from AL-1 (ephrin-A5). Meima, L., Moran, P., Matthews, W., Caras, I.W. Mol. Cell. Neurosci. (1997) [Pubmed]
  4. Differential effects of overexpression of two forms of ephrin-A5 on neonatal rat cardiomyocytes. Li, Y.Y., Mi, Z., Feng, Y., McTiernan, C.F., Zhou, R., Robbins, P.D., Watkins, S.C., Feldman, A.M. Am. J. Physiol. Heart Circ. Physiol. (2001) [Pubmed]
  5. Development of inhibition by ephrin-A5 on outgrowth of embryonic spinal motor neurites. Wang, H., Chadaram, S.R., Norton, A.S., Laskowski, M.B. J. Neurobiol. (2001) [Pubmed]
  6. Alteration of pharmacokinetics and nephrotoxicity of cisplatin by alginates. Imai, T., Fujii, K., Shiraishi, S., Otagiri, M. Journal of pharmaceutical sciences. (1997) [Pubmed]
  7. Growth-associated gene expression after stroke: evidence for a growth-promoting region in peri-infarct cortex. Carmichael, S.T., Archibeque, I., Luke, L., Nolan, T., Momiy, J., Li, S. Exp. Neurol. (2005) [Pubmed]
  8. Localization of a tumor cell adhesion domain of laminin by a monoclonal antibody. Skubitz, A.P., Charonis, A.S., Tsilibary, E.C., Furcht, L.T. Exp. Cell Res. (1987) [Pubmed]
 
WikiGenes - Universities