Literature DB >> 18804470

TPA primes alpha2beta1 integrins for cell adhesion.

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.

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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


  9 in total

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