组织型纤溶酶原激活剂（TPA）使α2β1整合素做好细胞黏附的准备。
TPA primes alpha2beta1 integrins for cell adhesion.
作者信息
Tulla Mira, Helenius Jonne, Jokinen Johanna, Taubenberger Anna, Müller Daniel J, Heino Jyrki
机构信息
Biotechnology Center, University of Technology Dresden, Germany.
出版信息
FEBS Lett. 2008 Oct 15;582(23-24):3520-4. doi: 10.1016/j.febslet.2008.09.022. Epub 2008 Sep 18.
Integrin avidity is regulated by changes in the conformation of the heterodimer and cluster formation. We measured cell adhesion by integrin alpha2beta1 (CHO-alpha2) to collagen at short contact times (0.5-60s) by single cell force spectroscopy (SCFS). The adhesion increased rapidly with contact time and was further strengthened by the addition of 12-O-tetradecanoylphorbol-13-acetate (TPA), a protein kinase C (PKC) and integrin activator. TPA also improved the strength of adhesive units. Furthermore, changes in membrane nanotube properties indicated better coupling of integrins to the cell cytoskeleton. We conclude that in addition to increasing integrin avidity TPA strengthens integrin-cytoskeletal linkage.
整合素亲和力受异二聚体构象变化和聚集体形成的调节。我们通过单细胞力谱（SCFS）在短接触时间（0.5 - 60秒）下测量了整合素α2β1（CHO - α2）与胶原蛋白的细胞黏附。黏附力随接触时间迅速增加，并通过添加12 - O - 十四烷酰佛波醇 - 13 - 乙酸酯（TPA）进一步增强，TPA是一种蛋白激酶C（PKC）和整合素激活剂。TPA还提高了黏附单元的强度。此外，膜纳米管特性的变化表明整合素与细胞细胞骨架的耦合更好。我们得出结论，除了增加整合素亲和力外，TPA还增强了整合素 - 细胞骨架连接。
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