Alpha-5 beta-1

α5β1, also known as the fibronectin receptor,[1] is an integrin that binds to matrix macromolecules and proteinases and thereby stimulates angiogenesis.[2] 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,[3] a kinesin-3 organelle transporter that walks along microtubules.

References

  1. ^ Schaffner, F.; Ray, A.; Dontenwill, M. (2013). "Integrin α5β1, the Fibronectin Receptor, as a Pertinent Therapeutic Target in Solid Tumors". Cancers. 5 (4): 27–47. doi:10.3390/cancers5010027. PMC 3730317.
  2. ^ 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.
  3. ^ 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.


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