Primary structure from amino acid and cDNA sequences of two Cu,Zn superoxide dismutase variants from Xenopus laevis☆
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In-depth proteomic analysis of the byssus from marine mussel Mytilus coruscus
2016, Journal of ProteomicsCitation Excerpt :In addition, two superoxide dismutase (unigene62420 and unigene62486), with Cu/Zn superoxide dismutase (SOD) domains, were identified from both of the thread and the plaque. The SOD domain participates in preventing damage from oxygen-mediated free radicals by catalyzing the dismutation of superoxide into molecular oxygen and hydrogen peroxide [42–44]. Mussel adhesion relies on the process of DOPA oxidation that leads to dopaquinone formation [8,45].
Free-radical first responders: The characterization of CuZnSOD and MnSOD regulation during freezing of the freeze-tolerant North American wood frog, Rana sylvatica
2015, Biochimica et Biophysica Acta - General SubjectsCitation Excerpt :It has been suggested that the cytoplasmic form, CuZnSOD, acts like a buffer against the buildup of intracellular O2−, whereas the mitochondrial form, MnSOD, plays a pivotal role in the disproportionation of the large amount of O2− generated by the electron transport chain housed within the mitochondria [14,15]. CuZnSOD and MnSOD have been sequenced from the African clawed frog, Xenopus laevis, and exist as homodimers with molecular weights of approximately 32 kDa and 46 kDa, respectively [10,13]. Studies have shown the importance of functional CuZnSOD as many disease states can be attributed to mutations in the sod1 gene [16].
Characterization of rock bream (Oplegnathus fasciatus) cytosolic Cu/Zn superoxide dismutase in terms of molecular structure, genomic arrangement, stress-induced mRNA expression and antioxidant function
2014, Comparative Biochemistry and Physiology Part - B: Biochemistry and Molecular BiologyCitation Excerpt :Moreover, it is highly sensitive to stress stimuli such as heat shock (Hass and Massaro, 1988), heavy metals (Yoo et al., 1999), xenobiotics (Ken et al., 2003) and pathogens (Marikovsky et al., 2003; Chakravarthy et al., 2012) in terms of both mRNA levels and enzyme activity. Although, many Cu/ZnSOD homologs have been previously identified from amphibians (Schinina et al., 1989), molluscs (Ni et al., 2007; Bao et al., 2009), arthropods (Cheng et al., 2006), only a few reports described the Cu/ZnSODs from teleost origins including zebrafish (Ken et al., 2003), emerald rockcod (Santovito et al., 2006), silver carp (Zhang et al., 2011), Asian seabass (Chakravarthy et al., 2012); most of which were limited to cDNA cloning and mRNA expression. In 2005, Nam et al. identified a Cu/ZnSOD-like gene from rock bream (GenBank Accession AY613390) and reported its mRNA expression during starvation, along with few other antioxidant enzymes (Nam et al., 2005).
Proteomic biomarkers for ovarian cancer risk in women with polycystic ovary syndrome: A systematic review and biomarker database integration
2012, Fertility and SterilityCitation Excerpt :Superoxide dismutase, vimentin, malate dehydrogenase, and lamin B2 were also overexpressed in the same two studies (28, 29) in which calreticulin was overexpressed. Superoxide dismutase is an antioxidant that prevents oxygen-mediated free radical cellular damage (39), whereas increased manganese superoxide dismutase expression has been demonstrated in animal models of OC and primary OC tissues from patients (40). In women with PCOS, superoxide dismutase was elevated in T lymphocytes from women with PCOS compared with controls (41).
Identification and analysis of a Cu/Zn superoxide dismutase from Haliotis diversicolor supertexta with abalone juvenile detached syndrome
2010, Journal of Invertebrate PathologycDNA cloning, high-level expression, purification, and characterization of an avian Cu,Zn superoxide dismutase from Peking duck
2002, Protein Expression and Purification
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This work was partially supported by the CNR Special Project “Biotecnologie e Biostrumentazione.”