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S-Glutathiolation by peroxynitrite activates SERCA during arterial relaxation by nitric oxide
Nitric oxide (NO) physiologically stimulates the sarco/endoplasmic reticulum calcium (Ca2+) ATPase (SERCA) to decrease intracellular Ca2+ concentration and relax cardiac, skeletal and vascular smoothExpand
SOD1 mutations disrupt redox-sensitive Rac regulation of NADPH oxidase in a familial ALS model.
It is demonstrated that SOD1 is not just a catabolic enzyme, but can also directly regulate NADPH oxidase-dependent (Nox-dependent) O(2)(*-) production by binding Rac1 and inhibiting its GTPase activity. Expand
Glutathione Peroxidase Protects against Peroxynitrite-mediated Oxidations
A novel function of GPx is demonstrated, and potentially of other selenoproteins containing selenocysteine or selenomethionine, in the GSH-dependent maintenance of a defense line against peroxynitrite-mediated oxidations, as a peroxlynitrite reductase. Expand
3-Nitrotyrosine modification of SERCA2a in the aging heart: a distinct signature of the cellular redox environment.
It is shown that the additional loss of activity in the senescent Fischer 344 rat heart relative to that of young adult hearts is a result of increased 3-nitrotyrosine modification of the Ca-ATPase, and age-dependent increases in nitration of cardiac SERCA2a are identified using multiple analytical methods. Expand
Diastereoselective reduction of protein‐bound methionine sulfoxide by methionine sulfoxide reductase
It is reported for the first time that pMSR selectively reduces the D‐sulfoxide diastereomer of CaM‐bound L‐MetSO (L‐Met‐D‐SO) and the accumulation of MetSO upon oxidative stress and aging in vivo may be related to incomplete, diastsereoselective, repair by pMSr. Expand
Oxidative inactivation of purified plasma membrane Ca2+-ATPase by hydrogen peroxide and protection by calmodulin.
In the present studies, inhibition of PMCA by H( 2)O(2) was characterized in enzyme purified from human erythrocyte membranes, indicating a CaM-induced conformational state resistant to oxidation. Expand
Quantitative mapping of oxidation-sensitive cysteine residues in SERCA in vivo and in vitro by HPLC-electrospray-tandem MS: selective protein oxidation during biological aging.
A quantitative method to monitor the oxidation state of the individual SERCA cysteine residues using a maleimide-based fluorescence dye, TG1 (ThioGlo 1), as a label for cysteines that have not been altered by oxidation and are not involved in disulphide bridges is developed and optimized. Expand
Diastereoselective protein methionine oxidation by reactive oxygen species and diastereoselective repair by methionine sulfoxide reductase.
Exposing CaM to various biologically relevant reactive oxygen species and oxidizing systems to investigate whether one of these systems would lead to an oxidation pattern of CaM similar to that observed in vivo indicated that other, yet unidentified oxidation mechanisms may be important in vivo. Expand
Cysteine-674 oxidation and degradation of sarcoplasmic reticulum Ca(2+) ATPase in diabetic pig aorta.
A sequence-specific antibody is demonstrated that detects partial degradation products of SERCA, which represent the majority of the protein in some diabetic hypercholesterolemic pig aortae, and an association between irreversible oxidation ofSERCA and its degradation, and that an important portion of the oxidized protein in tissue samples may be partially degraded. Expand
Displacement of SERCA from SR lipid caveolae-related domains by Bcl-2: a possible mechanism for SERCA inactivation.
This work shows that the transmembrane (TM) domain of Bcl-2 accelerates SERCA inactivation, and both B cl-2delta21 and full-length BCl-2 selectively interact with SERCA1, and the inactivation of SERCA is accompanied by a translocation ofSERCA from caveolae-related domains (CRD) of the sarcoplasmic reticulum (SR). Expand