Activation of mitogen-activated protein (MAP) kinase pathway by pervanadate, a potent inhibitor of tyrosine phosphatases
| Autor: | Min You, Edmond H. Fischer, Zhongjia Tan, Curtis D. Diltz, Zhizhuang Zhao |
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| Rok vydání: | 1996 |
| Předmět: |
Time Factors
MAPK7 Protein tyrosine phosphatase Mitogen-activated protein kinase kinase environment and public health Biochemistry MAP2K7 chemistry.chemical_compound Humans ASK1 Molecular Biology Mitogen-Activated Protein Kinase 1 Mitogen-Activated Protein Kinase 3 MAP kinase kinase kinase Dose-Response Relationship Drug Chemistry Tyrosine phosphorylation Cell Biology Cell biology Enzyme Activation enzymes and coenzymes (carbohydrates) Calcium-Calmodulin-Dependent Protein Kinases Cyclin-dependent kinase 9 Mitogen-Activated Protein Kinases Protein Tyrosine Phosphatases Vanadates HeLa Cells |
| Zdroj: | The Journal of biological chemistry. 271(36) |
| ISSN: | 0021-9258 |
| Popis: | Rapid tyrosine phosphorylation of key cellular proteins is a crucial event in signal transduction. The regulatory role of protein-tyrosine phosphatases (PTPs) in this process was explored by studying the effects of a powerful PTP inhibitor, pervanadate, on the activation of the mitogen-activated protein (MAP) kinase cascade. Treatment of HeLa cells with pervanadate resulted in a marked inhibition of PTP activity, accompanied by a drastic increase in tyrosine phosphorylation of cellular proteins. The increased tyrosine phosphorylation coincided with the activation of the MAP kinase cascade as indicated by enzymatic activity assays of MEK (MAP kinase/ERK-kinase) and MAP kinase and gel mobility shift analyses of Raf-1 and MAP kinase. The activation was sustained but reversible. Upon removal of pervanadate, both tyrosine phosphorylation and MAP kinase activation declined to basal levels. Therefore, inhibition of PTP activity is sufficient per se to initiate a complete MAP kinase activation program. |
| Databáze: | OpenAIRE |
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