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J Biol Chem, Vol. 273, Issue 8, 4769-4775, February 20, 1998
From the Department of Environmental Health, University of
Washington, Seattle, Washington 98195
Previous investigations have indicated that
de novo protein synthesis is a critical requirement for
phenobarbital (PB) induction. We reexamined this issue in PB-responsive
primary rat hepatocyte cultures using a broader array of protein
synthesis inhibitors and experimental end points. Anisomycin,
cycloheximide, emetine, puromycin, and puromycin aminonucleoside, a
negative analog, were evaluated for their respective effects on protein
synthesis and the PB-induction process. All of the inhibitors
effectively repressed de novo protein synthesis in the
cells in a concentration-dependent manner. However,
anisomycin only minimally effected PB induction, ascertained though the
measure of CYP2B1, CYP2B2, and CYP3A1 mRNA levels. The inactive
agent, puromycin aminonucleoside, produced marked repression of the
PB-induction response. Results from further experiments demonstrated
that these protein synthesis inhibitors stimulated rapid and
differential phosphorylation of the stress-activated protein
kinase/c-Jun kinase (SAPK/JNK) pathway, indicating nonselective actions
on cellular processes. Puromycin aminonucleoside was without effect on
these pathways, despite its efficacy as an inhibitor of PB induction.
These results demonstrate that de novo protein synthesis is
not a requirement for PB induction, nor is activation of the
SAPK/JNK kinase cascade responsible for down-regulating PB
responsiveness in primary hepatocytes.
Protein Synthesis Inhibitors Exhibit a Nonspecific Effect on
Phenobarbital-inducible Cytochome P450 Gene Expression in Primary Rat
Hepatocytes
Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.
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