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      Selective activation of JNK/SAPK by interleukin-1 in rabbit liver is mediated by MKK7.

      Febs Letters
      Amino Acid Sequence, Animals, Antibodies, Calcium-Calmodulin-Dependent Protein Kinases, metabolism, Chromatography, Ion Exchange, Enzyme Activation, Humans, Immunoblotting, Interleukin-1, pharmacology, JNK Mitogen-Activated Protein Kinases, Liver, enzymology, MAP Kinase Kinase 7, Mitogen-Activated Protein Kinase 1, Mitogen-Activated Protein Kinase Kinases, Mitogen-Activated Protein Kinases, Molecular Sequence Data, Peptide Fragments, chemical synthesis, chemistry, immunology, Phosphorylation, Protein Kinases, isolation & purification, Rabbits, Substrate Specificity, p38 Mitogen-Activated Protein Kinases

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          Abstract

          Activation of jun N-terminal kinase (JNK)/stress-activated protein kinase (SAPK) by interleukin-1 (IL-1) has been reported in many cells and in rabbit liver. Here we report selective activation of JNK/SAPK, without activation of p38 or p42 mitogen-activated protein kinases (MAPKs), by IL-1 in rabbit liver. We identified an IL-1 regulated JNK/SAPK activator present in rabbit liver using S Sepharose chromatography. It was purified and immunoprecipitated by two antisera to MAP kinase kinase 7 (MKK7). It was not recognised by an antibody to MKK4. We conclude that MKK7 is the activator of JNK/SAPK activated by IL-1 in liver and that JNK/SAPK is the only MAPK activated by IL-1 in liver.

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