2012
DOI: 10.1016/j.fsi.2012.03.029
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Molecular characterization, immune responses and DNA protection activity of rock bream (Oplegnathus fasciatus), peroxiredoxin 6 (Prx6)

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Cited by 31 publications
(16 citation statements)
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“…The relatively higher expression of recombinant OaPrdx6 proteins in E. coli BL21-Codonplus cells could imply that E. coli BL21-Codonplus cells as host were suitable for the expression of OaPrdx6. It was reported that recombinant Prdx6 proteins from various sources display the DNA protection activity (De Zoysa et al, 2012;Sharapov et al, 2009). In this study, we identified the DNA protection activity of the recombinant OaPrdx6 was in a dose dependent manner.…”
Section: Discussionmentioning
confidence: 77%
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“…The relatively higher expression of recombinant OaPrdx6 proteins in E. coli BL21-Codonplus cells could imply that E. coli BL21-Codonplus cells as host were suitable for the expression of OaPrdx6. It was reported that recombinant Prdx6 proteins from various sources display the DNA protection activity (De Zoysa et al, 2012;Sharapov et al, 2009). In this study, we identified the DNA protection activity of the recombinant OaPrdx6 was in a dose dependent manner.…”
Section: Discussionmentioning
confidence: 77%
“…The mammalian Prdx family has six isoforms which are classified into two sub-groups including five 2-Cys Prdxs (from Prdx1 to Prdx5) and one 1-Cys Prdx (Prdx6), and the 2-Cys Prdxs are divided into two classes called 'typical' and 'atypical' 2-Cys Prdxs depending on whether the conserved cysteine residues form intermolecular or intramolecular disulfide bridges respectively (Manevich and Fisher, 2005;Wood et al, 2003). The expression and role of Prdxs were reported against bacterial infections (Bacano Maningas et al, 2008;Zhang et al, 2007), and it is implicated that Prdxs take part in immune responses against viral or bacterial infection (De Zoysa et al, 2012;Yang et al, 2007). In mammals, the 1-Cys Prdx referred to as Peroxiredoxin 6 (Prdx6) contains the sole conserved cysteine residue at the molecular catalytic site (Rhee et al, 2005b).…”
Section: Introductionmentioning
confidence: 99%
“…The physiological importance of Prx6 has been demonstrated in a mutational study that showed that mice lacking Prx6 are viable but sensitive to oxidative stress [30]. Increased expressions of Prx6 for protecting the host against stressful conditions has been reported in some aquatic organisms, such as Pacific oyster Crassostrea gigas [31], Antarctic bivalve Laternula elliptica [32], disk abalone Haliotis discus discus [33], turbot Scophthalmus maximus [34] and rock bream Oplegnathus fasciatus [35]. On the other hand, negative regulation of Prx6 expression has also been reported.…”
Section: A C C E P T E D Accepted Manuscriptmentioning
confidence: 99%
“…Prx6 has a single conserved catalytic cysteine residue in the N-terminal catalytic motif (PVCTTE) that is responsible for the peroxidase activity (Manevich and Fisher 2005). Evidence suggests Prx6 is distributed in all major tissues that are sensitive to oxidative stress (Manevich and Fisher 2005), and its expression is induced by stimuli such as bacteria (Zheng et al 2010), viruses (Nikapitiya et al 2009), pathogen-associated molecular patterns (PAMPs) (De Zoysa et al 2012), chemicals (Wang et al 2008), thermal stress (Park et al 2008;Tolomeo et al 2016) and environmental pollutants (David et al 2007).…”
Section: Introductionmentioning
confidence: 99%