NDLI: Independent regulation of JNK/p38 mitogen-activated protein kinases by metabolic oxidative stress in the liver.

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Independent regulation of JNK/p38 mitogen-activated protein kinases by metabolic oxidative stress in the liver.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Tevosian, S. G. Davis, R. J. Contois, L. R. Mendelson, K. G. Paulson, K. E.
Description	Author Affiliation: Mendelson KG ( Department of Biochemistry, Tufts University School of Medicine, Boston, MA 02111, USA.);
Abstract	The stress-activated protein kinases JNK and p38 mediate increased gene expression and are activated by environmental stresses and proinflammatory cytokines. Using an in vivo model in which oxidative stress is generated in the liver by intracellular metabolism, rapid protein-DNA complex formation on stress-activated AP-1 target genes was observed. Analysis of the induced binding complexes indicates that c-fos, c-jun, and ATF-2 were present, but also two additional jun family members, JunB and JunD. Activation of JNK precedes increased AP-1 DNA binding. Furthermore, JunB was shown to be a substrate for JNK, and phosphorylation requires the N-terminal activation domain. Unexpectedly, p38 activity was found to be constitutively active in the liver and was down-regulated through selective dephosphorylation following oxidative stress. One potential mechanism for p38 dephosphorylation is the rapid stress-induced activation of the phosphatase MKP-1, which has high affinity for phosphorylated p38 as a substrate. These data demonstrate that there are mechanisms for independent regulation of the JNK and p38 mitogen-activated protein kinase signal transduction pathways after metabolic oxidative stress in the liver.
ISSN	00278424
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	23
Volume Number	93
Language	English
Publisher	National Academy of Sciences
Publisher Date	1996-12-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Calcium-Calmodulin-Dependent Protein Kinases Metabolism Carbon Tetrachloride Poisoning Cell Cycle Proteins Liver Enzymology Mitogen-Activated Protein Kinases Oxidative Stress Phosphoprotein Phosphatases Transcription Factor AP-1 Animals Binding Sites Cell Division DNA Dual Specificity Phosphatase 1 Enzyme Activation Immediate-Early Proteins JNK Mitogen-Activated Protein Kinases Kinetics Pathology Mice Mice, Inbred C57BL Models, Biological Protein Phosphatase 1 Protein Tyrosine Phosphatases Substrate Specificity Time Factors P38 Mitogen-Activated Protein Kinases Research Support, U.S. Gov't, Non-P.H.S. Research Support, U.S. Gov't, P.H.S. Multidisciplinary
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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