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Anti-apoptotic protein Bcl-2 interacts with and destabilizes the sarcoplasmic/endoplasmic reticulum Ca2+-ATPase (SERCA).
- E. Dremina, V. Sharov, KESHAVA N. Kumar, A. Zaidi, E. Michaelis, C. Schöneich
- Biology, Computer ScienceBiochemical Journal
- 15 October 2004
The results suggest that the direct interaction of Bcl-2 with SERCA may be involved in the regulation of apoptotic processes in vivo through modulation of cytoplasmic and/or endoplasmic reticulum calcium levels required for the execution of apoptosis.
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.
- V. Sharov, E. Dremina, N. Galeva, T. Williams, C. Schöneich
- Biology, ChemistryBiochemical Journal
- 15 March 2006
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.
Apoptosis in differentiating C2C12 muscle cells selectively targets Bcl-2-deficient myotubes
Overall, the data advocate for a Bcl-2-dependent mechanism of apoptosis in differentiated muscle cells, however, downstream processes for spontaneous and hydrogen peroxide induced apoptosis are not completely similar.
Oxidation and inactivation of SERCA by selective reaction of cysteine residues with amino acid peroxides.
- E. Dremina, V. Sharov, M. Davies, C. Schöneich
- Biology, ChemistryChemical Research in Toxicology
- 25 September 2007
The data demonstrate a potential role of peptide- and protein-derived peroxides as important mediators of oxidative stress in vivo, which may cause a selective oxidation of Cys residues leading to inactivation of membrane proteins.
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).
Fluorogenic Tagging of Peptide and Protein 3-Nitrotyrosine with 4-(Aminomethyl)benzenesulfonic Acid for Quantitative Analysis of Protein Tyrosine Nitration
A novel approach of fluorescent tagging and quantitation of peptide-bound 3-NT residues based on the selective reduction to 3-AT followed by reaction with 4-(aminomethyl)benzenesulfonic acid (ABS) in the presence of K3Fe(CN)6 to form a highly fluorescent 2-phenylbenzoxazole product is described.
Bcl-2 suppresses sarcoplasmic/endoplasmic reticulum Ca2+-ATPase expression in cystic fibrosis airways: role in oxidant-mediated cell death.
- Shama Ahmad, Aftab Ahmad, C. White
- Biology, MedicineAmerican Journal of Respiratory and Critical Care…
- 1 May 2009
Reduced SERCA2 expression may alter calcium signaling and apoptosis in CF and decrease the likelihood of therapeutic benefit of SERCA inhibition in CF.
Heat-shock proteins attenuate SERCA inactivation by the anti-apoptotic protein Bcl-2: possible implications for the ER Ca2+-mediated apoptosis.
The data demonstrate that the mechanism of SERCA inactivation by Bcl-2 established in vitro for the SERCA1 isoform can be extended to the main housekeeping SERCA2b isoform, and that functional interactions of SER CA2b and B cl-2 in the cell may be modulated by HSP70 and other chaperones and stress-regulated proteins.
A methodology for simultaneous fluorogenic derivatization and boronate affinity enrichment of 3-nitrotyrosine-containing peptides.
Inactivation of rabbit muscle glycogen phosphorylase b by peroxynitrite revisited: does the nitration of Tyr613 in the allosteric inhibition site control enzymatic function?