Abstract
Two-dimensional gel electrophoresis (2-DE) was used to study alterations in intracellular proteins of the human T lymphoblastic cell line JURKAT by heat shock at 45 degrees C for 30 min. The 2-DE patterns indicated an increase in the amount of a spot of molecular weight (M(r)) 18,500 and isoelectric point (pI) 5.6, which was a monophosphorylated form of stathmin. Stathmin is a major substrate for a proline-rich peptide-specific serine protein kinase, a mitogen-activated protein kinase, however, the enzyme was not activated by the heat shock. Further examinations of the effects of cAMP, phorbol myristate acetate, cyclosporin A, and staurosporine on phosphorylation suggest that cyclin-dependent kinases might be responsible for the heat shock-induced monophosphorylation of stathmin.
MeSH terms
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Amino Acid Sequence
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Calcium-Calmodulin-Dependent Protein Kinases / antagonists & inhibitors
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Calcium-Calmodulin-Dependent Protein Kinases / metabolism
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Cyclic AMP / pharmacology
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Cyclosporine / pharmacology
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Electrophoresis, Gel, Two-Dimensional*
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Enzyme Inhibitors / pharmacology
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Hot Temperature*
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Humans
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Isoelectric Point
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Jurkat Cells / metabolism*
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Microtubule Proteins*
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Molecular Sequence Data
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Molecular Weight
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Phosphoproteins / chemistry
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Phosphoproteins / metabolism*
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Phosphorylation
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Protein Kinase Inhibitors
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Protein Kinases / metabolism
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Stathmin
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Staurosporine / pharmacology
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Tetradecanoylphorbol Acetate / pharmacology
Substances
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Enzyme Inhibitors
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Microtubule Proteins
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Phosphoproteins
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Protein Kinase Inhibitors
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STMN1 protein, human
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Stathmin
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Cyclosporine
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Cyclic AMP
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Protein Kinases
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Calcium-Calmodulin-Dependent Protein Kinases
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Staurosporine
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Tetradecanoylphorbol Acetate