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Regulation of cys-based protein tyrosine phosphatases via reactive oxygen and nitrogen species in mast cells and basophils
Heneberg P, Dráber P.
Language English Country Netherlands
Document type Review
Grant support
NR8079
MZ0
CEP Register
Digital library NLK
Full text - Část
Source
NLK
ProQuest Central
from 2000-01-01 to 2008-12-31
Health & Medicine (ProQuest)
from 2000-01-01 to 2008-12-31
- MeSH
- Basophils enzymology metabolism MeSH
- Cysteine metabolism MeSH
- Financing, Organized MeSH
- Humans MeSH
- Mast Cells enzymology metabolism MeSH
- Reactive Nitrogen Species metabolism MeSH
- Reactive Oxygen Species metabolism MeSH
- Protein Tyrosine Phosphatases classification metabolism MeSH
- Animals MeSH
- Check Tag
- Humans MeSH
- Animals MeSH
- Publication type
- Review MeSH
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, PTP-PEST, SHP-2, PTP1B, PTPalpha, PTPepsilon, 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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- $a Department of Signal Transduction, Institute of Molecular Genetics, Academy of Sciences of the Czech Republic, Prague, Czech Republic
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