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B, Activator Protein-1, c-Jun N-Terminal Kinase, and Apoptosis1
Cytokine Research Section, Department of Bioimmunotherapy, University of Texas M. D. Anderson Cancer Center, Houston, TX 77030
HIV-tat protein, like TNF, activates a wide variety of cellular
responses, including NF-
B, AP-1, c-Jun N-terminal kinase (JNK), and
apoptosis. Whether HIV-tat transduces these signals through the same
mechanism as TNF is not known. In the present study we investigated the
role of the T cell-specific tyrosine kinase
p56lck in HIV-tat and TNF-mediated cellular
responses by comparing the responses of Jurkat T cells with JCaM1
cells, an isogeneic lck-deficient T cell line. Treatment
with HIV-tat protein activated NF-B, degraded IB
, and induced
NF-B-dependent reporter gene expression in a time-dependent manner
in Jurkat cells but not in JCaM1 cells, suggesting the critical role of
p56lck kinase. These effects were specific to
HIV-tat, as activation of NF-B by PMA, LPS,
H2O2, and TNF was minimally affected.
p56lck was also found to be required for
HIV-tat-induced but not TNF-induced AP-1 activation. Similarly, HIV-tat
activated the protein kinases JNK and mitogen-activated protein kinase
kinase in Jurkat cells but not in JCaM1 cells. HIV-tat also induced
cytotoxicity, activated caspases, and reactive oxygen intermediates in
Jurkat cells, but not in JCaM1 cells. HIV-tat activated
p56lck activity in Jurkat cells. Moreover, the
reconstitution of JCaM1 cells with p56lck
tyrosine kinase reversed the HIV-tat-induced NF-B activation and
cytotoxicity. Overall, our results demonstrate that
p56lck plays a critical role in the activation
of NF-B, AP-1, JNK, and apoptosis by HIV-tat protein but has minimal
or no role in activation of these responses by
TNF.
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