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
- ^ 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.
{{cite journal}}: CS1 maint: unflagged free DOI (link) - ^ Theisen, U (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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External links
- Integrin+alpha5beta1 at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
- ITGA5 ITGB1 Info with links in the Cell Migration Gateway
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