Blocked Signal Transduction to the ERK and JNK Protein Kinases in Anergic CD4+ T Cells
W Li, CD Whaley, A Mondino, DL Mueller - Science, 1996 - science.org
W Li, CD Whaley, A Mondino, DL Mueller
Science, 1996•science.orgT cells activated by antigen receptor stimulation in the absence of accessory cell-derived
costimulatory signals lose the capacity to synthesize the growth factor interleukin-2 (IL-2), a
state called clonal anergy. An analysis of CD3-and CD28-induced signal transduction
revealed reduced ERK and JNK enzyme activities in murine anergic T cells. The amounts of
ERK and JNK proteins were unchanged, and the kinases could be fully activated in the
presence of phorbol 12-myristate 13-acetate. Dephosphorylation of the calcineurin substrate …
costimulatory signals lose the capacity to synthesize the growth factor interleukin-2 (IL-2), a
state called clonal anergy. An analysis of CD3-and CD28-induced signal transduction
revealed reduced ERK and JNK enzyme activities in murine anergic T cells. The amounts of
ERK and JNK proteins were unchanged, and the kinases could be fully activated in the
presence of phorbol 12-myristate 13-acetate. Dephosphorylation of the calcineurin substrate …
T cells activated by antigen receptor stimulation in the absence of accessory cell-derived costimulatory signals lose the capacity to synthesize the growth factor interleukin-2 (IL-2), a state called clonal anergy. An analysis of CD3- and CD28-induced signal transduction revealed reduced ERK and JNK enzyme activities in murine anergic T cells. The amounts of ERK and JNK proteins were unchanged, and the kinases could be fully activated in the presence of phorbol 12-myristate 13-acetate. Dephosphorylation of the calcineurin substrate NFATp (preexisting nuclear factor of activated T cells) also remained inducible. These results suggest that a specific block in the activation of ERK and JNK contributes to defective IL-2 production in clonal anergy.
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