hVH-5: a protein tyrosine phosphatase abundant in brain that inactivates mitogen-activated protein kinase
Autor: | Karen J. Martell, Audrey F. Seasholtz, Jack E. Dixon, Seung Kwak, Kristina K. Clemens |
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Rok vydání: | 1995 |
Předmět: |
Phosphatase
Molecular Sequence Data Protein tyrosine phosphatase Biochemistry PC12 Cells Receptor tyrosine kinase Cellular and Molecular Neuroscience Mice Dual-specificity phosphatase Animals Tissue Distribution c-Raf Amino Acid Sequence Cloning Molecular Protein kinase A In Situ Hybridization biology Base Sequence GRB10 Brain Cell Differentiation Protein phosphatase 2 Molecular biology Phosphoric Monoester Hydrolases Rats Enzyme Activation biology.protein Dual-Specificity Phosphatases Mitogens Protein Tyrosine Phosphatases Protein Kinases |
Zdroj: | Journal of neurochemistry. 65(4) |
ISSN: | 0022-3042 |
Popis: | A novel protein tyrosine phosphatase [homologue of vaccinia virus H1 phosphatase gene clone 5 (hVH-5)] was cloned; it shared sequence similarity with a subset of protein tyrosine phosphatases that regulate mitogen-activated protein kinase. The catalytic region of hVH-5 was expressed as a fusion protein and was shown to hydrolyze p-nitrophenylphosphate and inactivate mitogen-activated protein kinase, thus proving that hVH-5 possessed phosphatase activity. A unique proline-rich region distinguished hVH-5 from other closely related protein tyrosine phosphatases. Another feature that distinguished hVH-5 from related phosphatases was that hVH-5 was expressed predominantly in the adult brain, heart, and skeletal muscle. In addition, in situ hybridization histochemistry of mouse embryo revealed high levels of expression and a wide distribution in the central and peripheral nervous system. Some specific areas of abundant hVH-5 expression included the olfactory bulb, retina, layers of the cerebral cortex, and cranial and spinal ganglia. hVH-5 was induced in PC12 cells upon nerve growth factor and insulin treatment in a manner characteristic of an immediate-early gene, suggesting a possible role in the signal transduction cascade. |
Databáze: | OpenAIRE |
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