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Department of Immunology, Roswell Park Cancer Institute, Buffalo, NY 14263
Regional inflammation and systemic fever are hallmarks of host
immune responses to pathogenic stimuli. Although the thermal element of
fever is thought to enhance the activity of immune effector cells, it
is unclear what the precise role of increased body temperatures is on
the activation state and effector functions of lymphocytes. We report
here that mild, fever-like whole body hyperthermia (WBH) treatment of
mice results in a distinct increase in the numbers of tissue
lymphocytes with polarized spectrin cytoskeletons and uropods, as
visualized in situ. WBH also induces a coincident reorganization of
protein kinase C (PKC) isozymes and increased PKC activity within T
cells. These hyperthermia-induced cellular alterations are nearly
identical with the previously described effects of Ag- and
mitogen-induced activation on lymphocyte spectrin and PKC.
Immunoprecipitation studies combined with dual staining and protein
overlay assays confirmed the association of PKCß and PKC
with
spectrin following its reorganization. The receptor for activated C
kinase-1 was also found to associate with the spectrin-based
cytoskeleton. Furthermore, all these molecules (spectrin, PKCß,
PKC, and receptor for activated C kinase-1) cotranslocate to the
uropod. Enhanced intracellular spectrin phosphorylation upon WBH
treatment of lymphocytes was also found and could be blocked by the PKC
inhibitor bisindolylmaleimide I (GF109203X). These data suggest that
the thermal element of fever, as mimicked by these studies, can
modulate critical steps in the signal transduction pathways necessary
for effective lymphocyte activation and function. Further work is
needed to determine the cellular target(s) that transduces the
signaling pathway(s) induced by hyperthermia.
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