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Zn Superoxide Dismutase (zn + superoxide_dismutase)
Selected AbstractsAn RNAi strategy for treatment of amyotrophic lateral sclerosis caused by mutant Cu,Zn superoxide dismutaseJOURNAL OF NEUROCHEMISTRY, Issue 6 2005Xu Gang Xia No abstract is available for this article. [source] Oxidative modulation of nuclear factor-,B in human cells expressing mutant fALS-typical superoxide dismutasesJOURNAL OF NEUROCHEMISTRY, Issue 5 2002Arianna Casciati Abstract Previous evidence supports the notion of a redox regulation of protein phosphatase calcineurin that might be relevant for neurodegenerative processes where an imbalance between generation and removal of reactive oxygen species occurs. We have recently observed that calcineurin activity is depressed in human neuroblastoma cells expressing Cu,Zn superoxide dismutase (SOD1) mutant G93A and in brain areas from G93A transgenic mice, and that mutant G93A-SOD1 oxidatively inactivates calcineurin in vitro. We have studied the possibility that, by interfering directly with calcineurin activity, mutant SOD1 can modulate pathways of signal transduction mediated by redox-sensitive transcription factors. In this paper, we report a calcineurin-dependent activation of nuclear factor-,B (NF-,B) induced by the expression of familial amyotrophic lateral sclerosis (fALS)-SOD1s in human neuroblastoma cell lines. Alteration of the phosphorylation state of I,B, (the inhibitor of NF-,B translocation into the nucleus) and induction of cyclooxygenase 2 are consistent with the up-regulation of this transcription factor in this system. All of these modifications might be relevant to signaling pathways involved in the pathogenesis of fALS. [source] Flexibility of the Cu,Zn superoxide dismutase structure investigated at 0.57,GPaACTA CRYSTALLOGRAPHICA SECTION D, Issue 6 2010Isabella Ascone The 2,Å resolution crystal structure of bovine erythrocyte Cu,Zn superoxide dismutase (CuZnSOD) has been determined by X-ray diffraction at high pressure (0.57,GPa) and room temperature. At 0.57,GPa the secondary, tertiary and quaternary structures are similar to other previously determined bovine erythrocyte CuZnSOD structures. Nevertheless, pressure has a localized impact on the atomic coordinates of C, atoms and on side chains. The compression of the crystal and of the protein backbone is anisotropic. This anisotropy is discussed, taking into account intermolecular contacts and protein conformation. Pressure perturbation highlights the more flexible zones in the protein such as the electrostatic loop. At 0.57,GPa, a global shift of the dimetallic sites in both subunits and changes in the oxidation state of Cu were observed. The flexibility of the electrostatic loop may be useful for the interaction of different metal carriers in the copper-uptake process, whereas the flexibility of the metal sites involved in the activity of the protein could contribute to explaining the ubiquitous character of CuZnSODs, which are found in organisms living in very different conditions, including the deep-sea environment. This work illustrates the potential of combining X-ray crystallography with high pressure to promote and stabilize higher energy conformational substates. [source] Expression, purification and crystallization of Chaetomium thermophilum Cu,Zn superoxide dismutaseACTA CRYSTALLOGRAPHICA SECTION F (ELECTRONIC), Issue 9 2010Sachin Wakadkar Cu,Zn superoxide dismutase (Cu,ZnSOD) from the thermophilic fungus Chaetomium thermophilum was expressed in Pichia pastoris and purified. Crystals were grown in over 120 conditions but only those produced with 1.4,M sodium potassium phosphate pH 8.2 as precipitant were suitable for structural studies. Data were collected to 1.9,Å resolution at 100,K from a single crystal using a synchrotron-radiation source. The crystals belonged to space group P61/P65, with unit-cell parameters a = 90.2, c = 314.5,Å and eight molecules in the asymmetric unit. Elucidation of the crystal structure will provide insights into the active site of the enzyme and a better understanding of the structure,activity relationship, assembly and thermal stability of Cu,ZnSODs. [source] | ||||||||||