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Production in a Manner Distinct from LPS Activation of Monocytes
Drug Discovery Research, R. W. Johnson Pharmaceutical Research Institute, Raritan, NJ, 08869
p38 mitogen-activated protein kinase (MAPK) (p38) is involved in
various cellular responses, including LPS stimulation of monocytes,
resulting in production of proinflammatory cytokines such as TNF-
.
However, the function of p38 during antigenic stimulation of T cells is
largely unknown. Stimulation of the human Th cell clone HA-1.70 with
either the superantigen staphylococcal enterotoxin B (SEB) or with a
specific antigenic peptide resulted in p38 activation and the release
of TNF-. MAPK-activated protein kinase-2 (MAPKAPK-2), an in vivo
substrate for p38, was also activated by T cell signaling. SB 203580, a
selective inhibitor of p38, blocked p38 and MAPKAPK-2 activation in the
T cell clone but did not completely inhibit TNF- release. PD 098059,
a selective inhibitor of MAPK kinase 1 (MEK1), blocked activation of
extracellular signal-regulated kinase (ERK) and partially blocked
TNF- production by the clone. In human peripheral T cells, p38 was
not activated by SEB, but rather by CD28 cross-linking, whereas in the
human leukemic T cell line Jurkat, p38 was activated by CD3 and CD28
cross-linking in an additive fashion. TNF- production by peripheral
T cells in response to SEB and anti-CD28 mAb correlated more
closely with ERK activity than with p38 activity. Therefore, various
forms of T cell stimulation can activate the p38 pathway depending on
the cells examined. Furthermore, unlike LPS-stimulated monocytes,
TNF- production by T cells is only partially
p38-dependent.
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