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Blood, Vol. 95 No. 6 (March 15), 2000:
pp. 2044-2051
Engagement of the  2 1 integrin inhibits Fas ligand expression
and activation-induced cell death in T cells in a focal adhesion
kinase-dependent manner
Fawzi Aoudjit and
Kristiina Vuori
From the Cancer Research Center, The Burnham Institute, La Jolla,
CA.
T-cell receptor (TCR)-mediated apoptosis, also known as
activation-induced cell death (AICD), plays an important role in the control of immune response and in the development of T-cell repertoire. Mechanistically, AICD has been largely attributed to the interaction of
Fas ligand (Fas-L) with its cell surface receptor Fas in activated T
cells. Signal transduction mediated by the integrin family of cell
adhesion receptors has been previously shown to modulate apoptosis in a
number of different cell types; in T cells, integrin signaling is known
to be important in cellular response to antigenic challenge by
providing a co-stimulatory signal for TCR. In this study we demonstrate
that signaling via the collagen receptor  2 1 integrin specifically
inhibits AICD by inhibiting Fas-L expression in activated Jurkat T
cells. Engagement of the 21 integrin with monoclonal antibodies
or with type I collagen, a cognate ligand for 21, reduced
anti-CD3 and PMA/ionomycin-induced cell death by 30% and 40%,
respectively, and the expression of Fas-L mRNA by 50%. Further studies
indicated that the 21-mediated inhibition of AICD and Fas-L
expression required the focal adhesion kinase FAK, a known component in
the integrin signaling pathways. These results suggest a role for the
21 integrin in the control of homeostasis of immune response and
T-cell development.
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