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J Biol Chem, Vol. 273, Issue 21, 12901-12908, May 22, 1998
SEK1/MKK4 p38 Mitogen-activated Protein Kinase Pathway
,,
From the The mitogen-activated protein kinase (MAPK)
cascade is believed to function as an important regulator of
prostaglandin biosynthesis. Previously we reported that
interleukin-1 Department of Molecular Biology and
Pharmacology and Medicine, Washington University School of Medicine,
St. Louis, Missouri 63110, the § Department of Medicine,
Rochester University School of Medicine, Rochester, New York 14642, and
the ¶ Institute of Pathology and Program in Cell Biology, Case
Western Reserve University School of Medicine,
Cleveland, Ohio 44106
induces activation of JNK/SAPK and p38 MAPK with
concomitant up-regulation of cyclooxygenase (Cox)-2 expression and
prostaglandin E2 (PGE2) synthesis. Our experiments demonstrate that overexpression of 
MEKK1 (a
constitutively active truncation mutant of MEKK1 containing the
C-terminal 324 amino acids) increases Cox-2 expression and
PGE2 production which is completely blocked by SC68376, a
pharmacologic inhibitor of p38 MAPK. MEKK1 overexpression results in
activation of both c-Jun N-terminal kinases/extracellular
signal-regulated kinases (JNK/SAPK) and p38 MAPK. Furthermore,
activation of MEKK1 increases SEK1/MKK4 but not MKK3 or MKK6 activity.
These findings suggest that MEKK1 
SEK1/MKK4 may function as an
upstream kinase capable of activating both p38 MAPK and JNK/SAPK with
subsequent induction of Cox-2 expression and PGE2
production. We also found that overexpression of the constitutively
active form of SEK1 (SEK1-ED) increases both p38 MAPK and JNK/SAPK
phosphorylation, and increases PGE2 production and Cox-2
expression. By comparison, overexpression of the dominant negative form
of SEK1 (SEK1-AL) decreases the phosphorylation of both p38 MAPK and
JNK/SAPK and reduces Cox-2 expression. Together, this data suggests a
potential role for the MEKK1 SEK1/MKK4 p38 MAPK Cox-2
cascade linking members of the MAPK pathway with prostaglandin
biosynthesis.
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