Regulation of protein tyrosine phosphatases by reversible oxidation
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TLDR
The role of PTP oxidation for physiological signalling processes as well as in different pathologies is described on the basis of well-investigated examples and criteria to establish the causal involvement of P TP oxidation in a given process are proposed.Abstract:
Oxidation of the catalytic cysteine of protein-tyrosine phosphatases (PTP), which leads to their reversible inactivation, has emerged as an important regulatory mechanism linking cellular tyrosine phosphorylation and signalling by reactive-oxygen or -nitrogen species (ROS, RNS). This review focuses on recent findings about the involved pathways, enzymes and biochemical mechanisms. Both the general cellular redox state and extracellular ligand-stimulated ROS production can cause PTP oxidation. Members of the PTP family differ in their intrinsic susceptibility to oxidation, and different types of oxidative modification of the PTP catalytic cysteine can occur. The role of PTP oxidation for physiological signalling processes as well as in different pathologies is described on the basis of well-investigated examples. Criteria to establish the causal involvement of PTP oxidation in a given process are proposed. A better understanding of mechanisms leading to selective PTP oxidation in a cellular context, and finding ways to pharmacologically modulate these pathways are important topics for future research.read more
Citations
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References
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Insulin Stimulates Tyrosine Phosphorylation and Inactivation of Protein-tyrosine Phosphatase 1B in Vivo
TL;DR: PTP1B appears to be a critical point for insulin and catecholamine counter-regulation, and Elevation of intracellular cyclic AMP provokes a sharp increase in PTP 1B activity and leads to increased phosphorylation of serine residues and decreased tyrosine phosphorylated, and suppression leads to a sharp decline in activity, a decrease in phosphoserine content, and an increase in phosphotyrosine content.
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The myeloperoxidase-derived oxidant HOSCN inhibits protein tyrosine phosphatases and modulates cell signalling via the mitogen-activated protein kinase (MAPK) pathway in macrophages.
Amanda E. Lane,Joanne T.M. Tan,Clare L. Hawkins,Alison K. Heather,Alison K. Heather,Michael J. Davies,Michael J. Davies +6 more
TL;DR: HOSCN targets cysteine residues present in PTPs with this resulting in a loss of PTP activity for the isolated enzyme, in cell lysates and intact J774A.1 macrophage-like cells, and implicate HOSCN as an important mediator of inflammation-induced oxidative damage, particularly in smokers who have elevated plasma levels of SCN−.
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Antioxidants Relieve Phosphatase Inhibition and Reduce PDGF Signaling in Cultured VSMCs and in Restenosis
Kai Kappert,Jan Sparwel,Åsa Sandin,Alexander Seiler,Udo Siebolts,Olli Leppänen,Stephan Rosenkranz,Arne Östman +7 more
TL;DR: The reduction in PDGF &bgr;-receptor phosphorylation in vivo, and the increase in PTP activity, by antioxidants indicate activation of oxidized PTPs as a previously unrecognized mechanism for the antirestenotic effects of antioxidants.
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Redox Regulation of Protein Tyrosine Phosphatase 1B by Manipulation of Dietary Selenium Affects the Triglyceride Concentration in Rat Liver
Andreas S. Mueller,Sandra D. Klomann,Nicole M. Wolf,Sandra Schneider,Rupert Schmidt,Julia Spielmann,Gabriele I. Stangl,Klaus Eder,Josef Pallauf +8 more
TL;DR: It is concluded that redox-regulated proteins, such as PTP1B, represent important interfaces between dietary antioxidants such as Se and the regulation of metabolic processes.
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Sphingosine 1-phosphate increases glucose uptake through trans-activation of insulin receptor
TL;DR: Evidence of a novel redox-based cross- talk between S1P and insulin signaling pathways is reported, recognizing the lipid as an insulin-mimetic cue and pointing at reactive oxygen species as critical regulators of the cross-talk.