Generic placeholder image

Current Medicinal Chemistry

Editor-in-Chief

ISSN (Print): 0929-8673
ISSN (Online): 1875-533X

Regulation of Cys-Based Protein Tyrosine Phosphatases Via Reactive Oxygen and Nitrogen Species in Mast Cells and Basophils

Author(s): P. Heneberg and P. Draber

Volume 12, Issue 16, 2005

Page: [1859 - 1871] Pages: 13

DOI: 10.2174/0929867054546636

Price: $65

Abstract

Activation of mast cells and basophils is accompanied by the production of reactive oxygen and nitrogen species that regulate diverse signaling pathways leading to the release of inflammatory mediators and production of a variety of cytokines. Although the functional pathways of reactive oxygen and nitrogen species in vivo are not completely understood, some novel metabolic pathways can be envisioned based on recent findings that protein tyrosine phosphatases can be regulated by reversible oxidation. In this review, we describe major sources and targets of reactive oxide and nitrogen species in mast cells and basophils. Direct and indirect regulations of class I and II Cys-based protein tyrosine phosphatases (LMW-PTP, PTEN, PTPPEST, SHP-2, PTP1B, PTPα, PTPε, DEP-1, TC45, SHP-1, HePTP and LAR) are discussed. The combined data highlight the role of redox-regulated protein tyrosine phosphatases as targets in the development of new ways of therapeutic intervention in allergies and inflammatory diseases.

Keywords: mast cell, basophils, ige receptor, tyrosine phosphatase, hydrogen peroxide, superoxide, nitric oxide, redoxregulation


Rights & Permissions Print Export Cite as
© 2024 Bentham Science Publishers | Privacy Policy