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TPA primes α2β1 integrins for cell adhesion
Author(s) -
Tulla Mira,
Helenius Jonne,
Jokinen Johanna,
Taubenberger Anna,
Müller Daniel J.,
Heino Jyrki
Publication year - 2008
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2008.09.022
Subject(s) - integrin , avidity , cell adhesion , cytoskeleton , microbiology and biotechnology , chemistry , adhesion , collagen receptor , cell adhesion molecule , cell , biochemistry , biology , immunology , antigen , organic chemistry
Integrin avidity is regulated by changes in the conformation of the heterodimer and cluster formation. We measured cell adhesion by integrin α2β1 (CHO‐α2) 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.