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Division of Allergy and Clinical Immunology, and
Division of Nephrology, Departments of Medicine and Immunology, University of Colorado Health Sciences Center, Denver, CO 80262
Ten isoforms of c-jun N-terminal kinase (JNK) have been described
that arise by differential mRNA splicing of three genes. In that the
relative expression and function of these different JNK proteins in
human monocytic cells is not known, we have examined the JNK isoforms
in THP-1 monocyte/macrophage cells. Differentiation of THP-1 cells by
exposure to 10-8 M PMA for 42–48 h enhances cellular
responses to LPS, including enhanced activation of total JNK activity
and increased phosphorylation of p54 JNK as well as p46 JNK.
Examination of JNK proteins on Western blots reveals a predominance of
p46 JNK1 and p54 JNK2 proteins. Clearing of lysates by
immunoprecipitation of JNK1(99% effective) removes 46% of the JNK
enzymatic activity (p < 0.01), whereas clearing of
JNK1 plus JNK2 (70% effective) depletes the sample of 72% of the JNK
activity (p < 0.01). Further analysis, undertaken
with real-time RT-PCR, revealed that 98% of the JNK messages code for
three isoforms: JNK1
1, JNK2
1, and JNK22. The p54 JNK that is
phosphorylated in LPS-stimulated, PMA-differentiated THP-1 cells is
most likely JNK22 because 97% of the p54 JNK-encoding messages code
for JNK22. By analogous reasoning, the p46 JNKs that are not heavily
phosphorylated, but account for approximately half of the N-terminal
c-jun kinase enzymatic activity, are most likely either JNK11 or
JNK21 because they account for 98% of the messages that can code
for 46kDa JNKs.
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