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J. Biol. Chem., Vol. 269, Issue 42, 26546-26551, 10, 1994
CM Pombo, JV Bonventre, J Avruch, JR Woodgett, JM Kyriakis and T Force
The signal transduction pathways that mediate activation of trans acting
factors controlling an organ's response to ischemia are unknown. The
stress-activated protein kinases (SAPKs), a subfamily of the extracellular
signal-regulated kinases (ERKs), phosphorylate c-Jun within the
amino-terminal transactivation domain and are activated in response to a
variety of cellular stresses. We determined whether SAPKs are activated in
response to ischemia, an extreme, albeit common, pathophysiologic stress.
Rats underwent 40 min of renal ischemia followed by reperfusion for 0, 5,
20, or 90 min. SAPKs were immunoprecipitated from kidney lysates and kinase
activity assayed with recombinant GST-c-Jun(1-135), containing the
amino-terminal transactivation domain of c-Jun as substrate. SAPKs were not
activated by ischemia alone, but reperfusion for as little as 5 min was
associated with a 4.6-fold increase in kinase activity. Kinase activity was
increased 7.6-fold at 20 min following reperfusion and remained elevated at
90 min of reperfusion (4.9-fold). In contrast, activity of the related
ERK-1 and -2 was increased only 1.3-fold and only at the 5- min reperfusion
time point. When SAPKs were immunodepleted from kidney extracts prior to
incubation of the extracts with agarose-coupled GST-c- Jun(1-135), it was
found that SAPKs accounted for the majority of the amino-terminal c-Jun
kinase activity of kidney at 5 min following reperfusion. In Madin-Darby
canine kidney epithelial cells, ATP repletion, following ATP depletion
induced by chemical anoxia, was associated with a 9-15-fold activation of
SAPKs with a similar time course of activation to that seen in the kidney
after ischemia and reperfusion. In conclusion, the SAPKs are markedly
activated very early after reperfusion of ischemic kidney and following ATP
repletion of anoxic cells in culture. We propose that this activation of
SAPKs may trigger part of the kidney's early genetic response to ischemia,
possibly by enhancing trans acting activity of c-Jun.
The stress-activated protein kinases are major c-Jun amino-terminal kinases activated by ischemia and reperfusion
Cardiac Unit, Massachusetts General Hospital 02129.
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