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J. Biol. Chem., Vol. 269, Issue 42, 26396-26401, Oct, 1994
JK Westwick, C Weitzel, A Minden, M Karin and DA Brenner
Tumor necrosis factor alpha (TNF alpha) has multiple biological functions
including the prolonged activation of the collagenase and c- jun genes,
which are regulated via their AP-1 binding sites. We show that incubating
human fibroblasts with TNF alpha induces prolonged activation of JNK, the
c-Jun kinase, which phosphorylates the transactivation domain of c-Jun.
Furthermore, an immune complex kinase assay specifically demonstrates that
TNF alpha stimulates the activity of JNK1, the recently described
predominant form of JNK. TNF alpha also produces a small and transient
increase in extracellular signal- regulated kinase (ERK) activity and no
measured increase in Raf-1 kinase activity. On the other hand, epidermal
growth factor causes a prolonged activation of Raf-1 kinase and ERK
activity and a smaller, more transient activation of JNK, whereas the
phorbol ester phorbol 12- myristate 13-acetate causes a small stimulation
of Raf-1 kinase and a pronounced stimulation of ERK activity. The
activation of JNK by TNF alpha does not correlate with Raf-1 or ERK
activity. The kinetics of Raf-1, ERK, and JNK induction by epidermal growth
factor, phorbol 12- myristate 13-acetate, or TNF alpha indicate distinct
mechanisms of activation in human fibroblasts.
Tumor necrosis factor alpha stimulates AP-1 activity through prolonged activation of the c-Jun kinase
Department of Medicine, University of North Carolina, Chapel Hill 27599.
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