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Beta 2-integrin, LFA-1-mediated p125FAK activation.

F H Tabassam1, H Umehara, N Domae

  • 1Department of Internal Medicine, Osaka Dental University.

Journal of Osaka Dental University
|June 23, 2000
PubMed
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Lymphocyte function-associated antigen (LFA)-1 engagement triggers focal adhesion kinase (FAK) phosphorylation in T cells. This LFA-1 costimulation enhances T cell proliferation, suggesting a role for FAK in T cell activation.

Area of Science:

  • Immunology
  • Cellular Biology
  • Biochemistry

Background:

  • T cell accumulation is characteristic of inflammatory diseases.
  • T cell activation requires MHC/Ag-TCR binding and costimulatory signals (e.g., CD2, CD28, integrins).
  • Focal adhesion kinase (FAK) is involved in integrin-mediated fibroblast activation, but its role in T cell activation via LFA-1 was unknown.

Purpose of the Study:

  • To investigate whether lymphocyte function-associated antigen (LFA)-1 activation involves focal adhesion kinase (FAK) in T cells.
  • To determine if LFA-1 costimulation influences FAK phosphorylation and T cell proliferation.

Main Methods:

  • Crosslinking of LFA-1 on PHA-activated T cells.
  • Co-crosslinking of LFA-1 with suboptimal anti-CD3 monoclonal antibody (mAb).

Related Experiment Videos

  • Analysis of FAK tyrosine phosphorylation and T cell proliferation.

    • Main Results:

    • Crosslinking LFA-1 induced tyrosine phosphorylation of FAK in PHA-activated T cells.
    • Co-crosslinking LFA-1 and CD3 significantly increased FAK phosphorylation in an antibody- and time-dependent manner compared to CD3 stimulation alone.
    • Enhanced FAK phosphorylation correlated with increased T cell proliferation.

    Conclusions:

    • Signals mediated by LFA-1 can regulate FAK activity in T cells.
    • LFA-1-mediated T cell costimulation likely contributes to T cell activation, at least partially, through FAK.