hVH-5: a protein tyrosine phosphatase abundant in brain that inactivates mitogen-activated protein kinase

J Neurochem. 1995 Oct;65(4):1823-33. doi: 10.1046/j.1471-4159.1995.65041823.x.

Abstract

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.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Base Sequence
  • Brain / enzymology*
  • Cell Differentiation
  • Cloning, Molecular
  • Dual-Specificity Phosphatases
  • Enzyme Activation
  • In Situ Hybridization
  • Mice
  • Mitogens / pharmacology*
  • Molecular Sequence Data
  • PC12 Cells / pathology
  • Phosphoric Monoester Hydrolases / metabolism
  • Protein Kinases / metabolism*
  • Protein Tyrosine Phosphatases / genetics
  • Protein Tyrosine Phosphatases / metabolism*
  • Protein Tyrosine Phosphatases / physiology*
  • Rats
  • Tissue Distribution

Substances

  • Mitogens
  • Protein Kinases
  • Phosphoric Monoester Hydrolases
  • DUSP8 protein, human
  • Dual-Specificity Phosphatases
  • Protein Tyrosine Phosphatases

Associated data

  • GENBANK/U27193