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Department of Immunobiology, Fraunhofer Institute for Toxicology and Molecular Biology, Hannover, Germany
IL-16 has been reported as a modulator of T cell activation and was
shown to function as chemoattractant factor. The chemotactic activity
of IL-16 depends on the expression of CD4 on the surface of target
cells, but the intracellular signaling pathways are only now being
deciphered. This report describes IL-16 as an additional activator of
the stress-activated protein kinase (SAPK) pathway in
CD4+ macrophages. Treatment of these cells with
recombinant expressed IL-16 leads to the phosphorylation of SEK-1,
resulting in activation of the SAPKs p46 and p54. IL-16 stimulation
also leads to the phosphorylation of c-Jun and p38 MAPK
(mitogen-activated protein kinase), without inducing MAPK-family
members ERK-1 and ERK-2. Interestingly, the IL-16-mediated activation
of SAPKs and p38 MAPK in macrophages alone induces no detectable
apoptotic cell death. These observations suggest specific regulatory
functions of IL-16 distinct from the proinflammatory cytokines TNF-
and IL-1ß.
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