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Vol. 273, Issue 3, 1832-1837, January 16, 1998
From the In renal cells, hypertonicity induces genes for
heat shock proteins (HSP70,
p38 Kinase Activity Is Essential for Osmotic Induction of
mRNAs for HSP70 and Transporter for Organic Solute Betaine in
Madin-Darby Canine Kidney Cells
,,
Renal Division, Department of Medicine,
Baylor College of Medicine, Houston, Texas 77030 and the
¶ Renal Division, Department of Medicine, University of Texas
Medical Branch, Galveston, Texas 77555
B-crystallin), as well as enzymes and
transporters directly involved in the metabolism and transport of
protective organic osmolytes. While heat shock proteins are induced by
many stresses including osmotic stress, the induction of the osmolytes genes appears to be specific to osmotic stress. These two adaptive mechanisms allow kidney cells to survive and function in the hypertonic environment that exists on routine basis in kidney medulla. In mammalian cells, hypertonicity induces three mitogen-activated protein
kinase pathways: ERK (extracellular regulated kinase), JNK (Jun
N-terminal kinase), and p38. ERK activation by osmotic stress is a
consistent finding in many cells, but it is not essential for
transcriptional regulation of mRNA for transporter of organic osmolyte betaine. While the growth of yeast cells on NaCl-supplemented medium is dependent on HOG1 pathway, it is still unclear which pathway
mediates the adaptation to osmotic stress in mammalian cells. Here, we
show that inhibition of p38 kinase activity, using the specific
inhibitor SB203580
(4-(fluorophenyl)-2-(4-methylsulfonylphenyl)-5-(4-pyridyl) imidazole),
abolishes the hypertonicity-mediated induction of mRNAs for HSP70
and betaine transporter in Madin-Darby canine kidney cells. The
inhibition is dose-dependent and correlates with the
in situ activity of native p38 kinase, determined as MAPKAPK-2 activity in cell extracts. As reported previously, the activities of ERK-1 and -2 were not affected by SB203580, but surprisingly, inhibition of native p38 kinase activity correlates with
up-regulation of native JNK-1 activity in osmotically stressed cells.
p38 mRNA is induced by hypertonic stress and is attenuated with p38
kinase inhibition. We also find that thermal induction of HSP70
mRNA is not affected by p38 kinase inhibition. Such findings suggest that p38 kinase activity is essential for the induction of
genes involved in the adaptation of mammalian cells to osmotic stress
and that the increased activity of JNK-1 during p38 kinase inhibition
is consistent with regulation of JNK-1 by p38 kinase in osmotically
stressed cells. In addition, the transduction pathways mediating HSP70
mRNA induction by different stresses appear to be divergent;
osmotic induction of HSP70 is p38 kinase-dependent, while
thermal induction is not.
Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.
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