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Vol. 273, Issue 2, 800-804, January 9, 1998
From the Department of Medicine, University of Colorado School of
Medicine, Denver, Colorado 80262
The c-Jun NH2-terminal protein
kinases (JNKs), as well as the extracellular signal-regulated protein
kinases (ERKs) and p38 mitogen-activated protein kinase, are activated
in renal cells in response to extracellular hypertonicity. To determine
whether activation of JNKs by hypertonicity is isoform-specific, renal inner medullary collecting duct cells were stably transfected with
cDNA's encoding hemagglutinin (HA)-tagged JNK1 and JNK2 isoforms, and the expressed kinases were immunoprecipitated with an anti-HA antibody. Whereas both recombinant kinases were equivalently expressed, only immunoprecipitates from the HA-JNK2 cells displayed
hypertonicity-inducible JNK activity. Furthermore, expression of
dominant-negative JNK2 (HA-JNK2-APF) in stable clones inhibited
hypertonicity-induced JNK activation by 40-70%, whereas expression of
dominant-negative JNK1 (HA-JNK1-APF) had no significant inhibitory
effect. Independent HA-JNK2-APF (but not HA-JNK1-APF) clones displayed
greatly reduced viability relative to neomycin controls after 16 h
of exposure to 600 mosM/kg hypertonic medium with percent
survival of 20.5 ± 2.7 and 31.5 ± 7.3 for two independent
HA-JNK2-APF clones compared with 80.1 ± 1.0 for neomycin controls
(p < 0.001, n = 5, mean ± S.E.). However, neither JNK mutant blocked either regulatory volume
increase or hypertonicity-induced enhancement of uptake of inositol, an
organic osmolyte putatively involved in long term adaptation to
hypertonicity. These results define JNK2 as the primary
hypertonicity-activated JNK isoform in IMCD-3 cells and demonstrate its
central importance in cellular survival in a hypertonic environment by
a mechanism independent of acute regulatory volume increase as well as
regulation of organic osmolyte uptake.
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