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Cooperates with Calcineurin to Induce Fas Ligand Expression During Activation-Induced T Cell Death1
Divisions of
*
Cell Biology and
Cellular Immunolgy, La Jolla Institute for Allergy and Immunology, San Diego, CA 92121
Activation-induced cell death is mediated by the TCR-induced
expression of the Fas ligand (FasL) on the surface of T cells, followed
by binding to its receptor Fas. FasL expression is induced by
stimulating T cells with a combination of phorbol ester and
Ca2+ ionophore, implicating a role for protein kinase C
(PKC) in this process. However, the precise mechanisms that regulate
FasL expression, including the contribution of distinct T
cell-expressed PKC isoforms, are poorly understood. Herein, we report
that PKC
, a Ca2+-independent PKC isoform that we have
previously isolated as a PKC enzyme selectively expressed in T cells,
plays an important role in these processes. A constitutively active
PKC mutant preferentially induced FasL expression and activated the
corresponding gene promoter; conversely, a dominant-negative PKC
mutant blocked FasL expression induced by anti-CD3 or PMA plus
ionomycin stimulation. Furthermore, PKC synergized with calcineurin
to provide a potent stimulus for FasL promoter activation. Full
activation of the promoter required its binding sites for the
transcription factors NF-AT, AP-1, and NF-
B. The biological
significance of these findings is implicated by the finding that
rottlerin, a selective PKC inhibitor, blocked FasL induction by
anti-CD3 or PMA plus ionomycin stimulation and, consequently,
protected human Jurkat T cells and the mouse T cell hybridoma A1.1 from
activation-induced cell death.
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M. Villalba, K. Bi, J. Hu, Y. Altman, P. Bushway, E. Reits, J. Neefjes, G. Baier, R. T. Abraham, and A. Altman Translocation of PKC{theta} in T cells is mediated by a nonconventional, PI3-K- and Vav-dependent pathway, but does not absolutely require phospholipase C J. Cell Biol., April 15, 2002; 157(2): 253 - 263. [Abstract] [Full Text] [PDF]
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