Abstract
We have identified in rabbits two hepatic forms of T669 peptide kinases that are very strongly activated after systemic injection with the inflammatory cytokine interleukin 1 (IL-1). The T669 peptide contains a major phosphorylation site of the epidermal growth factor receptor, threonine 699 and is a substrate for mitogen-activated protein (MAP) kinases. The kinases were purified to homogeneity and corresponded to 50- and 55-kD proteins on sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Amino acid sequencing of 12 tryptic peptides of both kinases identified them as p54 MAP kinase alpha. This kinase belongs to the novel family of stress-activated protein kinases. This is the first evidence of IL-1 activating a specific protein kinase in vivo.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Sequence
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Animals
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Calcium-Calmodulin-Dependent Protein Kinases / isolation & purification
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Calcium-Calmodulin-Dependent Protein Kinases / metabolism*
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Chromatography, Affinity
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Chromatography, Gel
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Chromatography, Ion Exchange
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Electrophoresis, Polyacrylamide Gel
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Enzyme Activation
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ErbB Receptors / chemistry
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ErbB Receptors / metabolism
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Humans
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Interleukin-1 / pharmacology*
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Isoenzymes / isolation & purification
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Isoenzymes / metabolism*
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Kinetics
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Liver / enzymology*
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Molecular Sequence Data
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Molecular Weight
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Rabbits
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Recombinant Proteins / pharmacology
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Substrate Specificity
Substances
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Interleukin-1
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Isoenzymes
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Recombinant Proteins
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ErbB Receptors
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Calcium-Calmodulin-Dependent Protein Kinases