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

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

Document Type: Review Article

Affiliations: Department of Signal Transduction, Institute of Molecular Genetics, Academy of Sciences of the Czech Republic, VĂ­denska 1083, CZ-142 20 Prague 4 - Krc , Czech Republic;

Publication date: August 1, 2005

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  • Current Medicinal Chemistry covers all the latest and outstanding developments in medicinal chemistry and rational drug design. Each issue contains a series of timely in-depth reviews written by leaders in the field covering a range of the current topics in medicinal chemistry. Current Medicinal Chemistry is an essential journal for every medicinal chemist who wishes to be kept informed and up-to-date with the latest and most important developments.
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