| Literature DB >> 18804470 |
Mira Tulla1, Jonne Helenius, Johanna Jokinen, Anna Taubenberger, Daniel J Müller, Jyrki Heino.
Abstract
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.Entities:
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Year: 2008 PMID: 18804470 DOI: 10.1016/j.febslet.2008.09.022
Source DB: PubMed Journal: FEBS Lett ISSN: 0014-5793 Impact factor: 4.124