Alpha-5 beta-1

α5β1 is an integrin that binds to matrix macromolecules and proteinases and thereby stimulates angiogenesis.[1] It is composed of α5 (ITGA5/CD49e) and β1 (ITGB1/CD29) subunits. It is the primary receptor for fibronectin. The interaction of VLA-5 with fibronectin plays an important role in regulating inflammatory cytokine production by human articular chondrocytes (From the Cell Migration Gateway ITGA5 ITGB1).

α5β1-integrin is transported inside the cell by the kinesin KIF1C,[2] a kinesin-3 organelle transporter that walks along microtubules.

References

  1. Boudreau NJ, Varner JA (February 2004). "The homeobox transcription factor Hox D3 promotes integrin alpha5beta1 expression and function during angiogenesis". J. Biol. Chem. 279 (6): 4862–8. doi:10.1074/jbc.M305190200. PMID 14610084.
  2. Theisen, U; Straube, E; Straube, A (Dec 11, 2012). "Directional persistence of migrating cells requires Kif1C-mediated stabilization of trailing adhesions.". Developmental Cell. 23 (6): 1153–66. doi:10.1016/j.devcel.2012.11.005. PMID 23237952.

External links


This article is issued from Wikipedia - version of the 2/12/2016. The text is available under the Creative Commons Attribution/Share Alike but additional terms may apply for the media files.