Regular ArticleReactivity of Sulfhydryl Groups of the Catalytic Subunits of Rabbit Skeletal Muscle Protein Phosphatases 1 and 2A
References (0)
Cited by (41)
Exercise decreases PP2A-specific reversible thiol oxidation in human erythrocytes: Implications for redox biomarkers
2022, Free Radical Biology and MedicineNAD(P)H Oxidases in Coronary Artery Disease
2010, Advances in Clinical ChemistryCitation Excerpt :Akt may be involved in the redox-sensitive signaling leading to VSMC hypertrophy, because dominant negative Akt inhibits angiotensin II-stimulated [3H]leucine incorporation in cultured VSMCs [78]. Other potential redox-sensitive signaling targets include ras/rac [79–82], c-src [83], protein kinase C [84], tyrosine phosphatases [85–87], and regulation of Ca2+ signaling [88, 89]. Tissue and intracellular levels of ROS are altered by hormones and growth factors and the fact that ROS stimulate a variety of signaling pathways, it is not surprising that many cardiovascular-related genes are redox sensitive.
Brain PP2A is modified by thiol-disulfide exchange and intermolecular disulfide formation
2005, Biochemical and Biophysical Research CommunicationsCitation Excerpt :In this context, it is important to note that the catalytic subunit of PP2A contains six conserved cysteine residues [17,18]. While these residues are not considered to play a direct role in catalysis, findings that the PP2A activity of the isolated catalytic subunit from rabbit muscle is inhibited by disulfides and other thiol reagents [12] indicate that modification of one or more cysteine residues of the catalytic subunit is sufficient to inhibit enzyme activity. In accordance with this view, we have found that GSSG inhibits the PP2A activity of immune complexes obtained by immunoprecipitation of rat brain soluble protein with antibody to the catalytic subunit of PP2A (Petro and Foley, unpublished observation).
Identification and H<inf>2</inf>O<inf>2</inf> sensitivity of the major constitutive MAPK phosphatase from rat brain
2004, Biochemical and Biophysical Research CommunicationsReversible inhibition of the protein phosphatase 1 by hydrogen peroxide. Potential regulation of eIF2α phosphorylation in differentiated PC12 cells
2003, Archives of Biochemistry and BiophysicsCitation Excerpt :This mechanism is strongly supported by several recent findings showing H2O2-induced inhibition of calcineurin signaling pathways and reversion with reducing agents such as Fe2+, ascorbate or DTT [8,9]. Regarding PP1, this enzyme is inactivated by sulfhydryl reagents more rapidly than PP2A [46]; conversely, the presence of a mixture of Fe2+ and Zn2+ or Fe2+ and ascorbate induces its activation [43,47]. Yet, other less documented findings suggest that, as is the case with PTPases, inactivation of PP1 [48] and calcineurin [10] might involve the oxidation of two closely spaced cysteinyl residues to a disulfide as well.
Cell signalling and the glutathione redox system
2002, Biochemical PharmacologyCitation Excerpt :Moreover, it should be noted that serine/threonine phosphatases as well as protein tyrosine phosphatases (PTPases; described later), are regulated by redox changes. Studies in invivo systems have demonstrated that thiol oxidation of protein phosphatases 1 and 2A inhibited their enzymatic activity [34]. Furthermore, superoxide dismutase 1 (SOD1) prevents calcineurin—a serine/threonine phospatase which contains Fe and Zn in its active site—from inactivation mediated by oxidative damage both in vivo and in vitro[35].