A1 Refereed original research article in a scientific journal
TPA primes alpha 2 beta 1 integrins for cell adhesion
Authors: Tulla M, Helenius J, Jokinen J, Taubenberger A, Muller DJ, Heino J
Publisher: ELSEVIER SCIENCE BV
Publication year: 2008
Journal:: FEBS Letters
Journal name in source: FEBS LETTERS
Journal acronym: FEBS LETT
Volume: 582
Issue: 23-24
First page : 3520
Last page: 3524
Number of pages: 5
ISSN: 0014-5793
DOI: https://doi.org/10.1016/j.febslet.2008.09.022
Abstract
Integrin avidity is regulated by changes in the conformation of the heterodimer and cluster formation. We measured cell adhesion by integrin alpha 2 beta 1 (CHO-alpha 2) to collagen at short contact times (0.5-60 s) 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.
Integrin avidity is regulated by changes in the conformation of the heterodimer and cluster formation. We measured cell adhesion by integrin alpha 2 beta 1 (CHO-alpha 2) to collagen at short contact times (0.5-60 s) 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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