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Omeka, W.K.M.,Liyanage, D.S.,Priyathilaka, Thanthrige Thiunuwan,Godahewa, G.I.,Lee, Seongdo,Lee, Sukkyoung,Lee, Jehee ACADEMIC PRESS LTD 2019 FISH AND SHELLFISH IMMUNOLOGY Vol.90 No.-
<P><B>Abstract</B></P> <P>Glutaredoxins (Grx) are redox enzymes conserved in viruses, eukaryotes, and prokaryotes. In this study, we characterized glutaredoxin 1 (HaGrx1) from big-belly seahorse, <I>Hippocampus abdominalis. In-silico</I> analysis showed that HaGrx1 contained the classical glutaredoxin 1 structure with a CSYC thioredoxin active site motif. According to multiple sequence alignment and phylogenetic reconstruction, HaGrx1 presented the highest homology to the Grx1 ortholog from <I>Hippocampus comes</I>. Transcriptional studies demonstrated the ubiquitous distribution of <I>HaGrx1</I> transcripts in all the seahorse tissues tested. Significant modulation (<I>p</I> < 0.05) of <I>HaGrx1</I> transcripts were observed in blood upon stimulation with pathogen-associated molecular patterns and live pathogens. The β-hydroxyethyl disulfide reduction assay confirmed the antioxidant activity of recombinant HaGrx1. Further, dehydroascorbate reduction and insulin disulfide reduction assays revealed the oxidoreductase activity of HaGrx1. HaGrx1 utilized 1,4-dithiothreitol, <SMALL>L</SMALL>-cysteine, 2-mercaptoethanol, and reduced <SMALL>L</SMALL>-glutathione as reducing agent with different dehydroascorbate reduction activity levels. Altogether, our results suggested a vital role of HaGrx1 in redox homeostasis as well as the host innate immune defense system.</P> <P><B>Highlights</B></P> <P> <UL> <LI> Grx1 from <I>Hippocampus abdominalis</I> were characterized. </LI> <LI> CSYC thioredoxin active motif and classical Grx1 structure was found. </LI> <LI> Spatial and temporal expression patterns of <I>HaGrx1</I> were observed. </LI> <LI> Antioxidant activity of Grx1 assessed by different functional assays<I>.</I> </LI> </UL> </P>
Liyanage, D.S.,Omeka, W.K.M.,Yang, Hyerim,Godahewa, G.I.,Kwon, Hyukjae,Nam, Bo-Hye,Lee, Jehee Elsevier 2019 Fish & shellfish immunology Vol.86 No.-
<P><B>Abstract</B></P> <P>Thioredoxin domain-containing protein 17 (TXNDC17) is a small protein (∼14 kDa) involved in maintaining cellular redox homeostasis via a thiol-disulfide reductase activity. In this study, TXNDC17 was identified and characterized from <I>Hippocampus abdominalis</I>. The open reading frame (ORF) consisted of 369 bp and 123 amino acids. Similar to the other thioredoxins, TXNDC17 contained a conserved WCXXC functional motif. The highest spatial mRNA expressions of <I>HaTXNDC17</I> were observed in the muscle, brain, and intestine. Interestingly, the mRNA expression of <I>HaTXNDC17</I> in blood showed significant upregulation at 48 h against all the pathogen associated molecular patterns (PAMPs) and bacteria. Further, <I>HaTXNDC17</I> transcripts in the trunk kidney were significantly upregulated at 24–48 h by bacterial endotoxin lipopolysaccharides (LPS), viral mimic polyinosinic: polycytidylic acid (poly I:C), and gram-negative bacteria (<I>Edwardsiella tarda</I>). The DPPH assay showed that the radical scavenging activity varies in a concentration-dependent manner. The insulin reduction assay demonstrated a significant logarithmic relationship with the concentration of rHaTXNDC17. Moreover, FHM cells treated with recombinant HaTXNDC17 significantly enhanced cellular viability under oxidative stress. Together, these results show that HaTXNDC17 function is important for maintaining cellular redox homeostasis and that it is also involved in the immune mechanism in seahorses.</P> <P><B>Highlights</B></P> <P> <UL> <LI> Big-belly seahorse thioredoxin domain containing protein 17 maintain redox homeostasis. </LI> <LI> TXNDC17 is ubiquitously found in cytosol and extracellular space. </LI> <LI> Thiol active CXXC conserved motif consists in HaTXNDC17. </LI> <LI> Spatial and temporal mRNA expression was evaluated. </LI> <LI> Radical scavenging ability, antioxidant activity and cellular viability were measured. </LI> </UL> </P>
Liyanage, D.S.,Omeka, W.K.M.,Godahewa, G.I.,Lee, Jehee Elsevier 2018 Fish & shellfish immunology Vol.75 No.-
<P><B>Abstract</B></P> <P>Thioredoxin is a highly conserved protein found in both prokaryotes and eukaryotes. Reactive oxygen species (ROS) are produced in response to metabolic processes, radiation, metal oxidation, and pathological infections. High levels of ROS lead to cell death via autophagy. However, thioredoxin acts as an active regulatory enzyme in response to excessive ROS. Here, we performed <I>in-silico</I> analysis, immune challenge experiments, and functional assays of seahorse thioredoxin-like protein 1 (ShTXNL1). Evolutionary identification showed that ShTXNL1 protein belongs to the thioredoxin superfamily comprising 289 amino acids. It possesses an N-terminal active thioredoxin domain and C-terminal proteasome-interacting thioredoxin domain (PITH) of ShTXNL1 which is a component of 26S proteasome and binds to the matrix or cell. Pairwise alignment results showed 99.0% identity and 99.7% similarity with the sequence of <I>Hippocampus</I> species. Conserved thiol-disulfide cysteine residue containing Cys-X-X-Cys motif may be found in the first few amino acids in the second beta sheet starting from the N-terminus. This motif can be discovered in ShTXNL1 as <SUP>14</SUP>CRPC<SUP>17</SUP> and comprised two N-linked glycosylation sites at <SUP>72</SUP>NISA<SUP>75</SUP> and <SUP>139</SUP>NESD<SUP>142</SUP>. According to the quantitative real-time polymerase chain reaction analysis from healthy seahorses, highest <I>ShTXNL1</I> mRNA expression was observed in muscle, followed by ovary, brain, gill, and blood tissues. Moreover, significant temporal expression of <I>ShTXNL1</I> was observed in gill and blood tissues after bacterial stimuli. Thus, the <I>ShTXNL1</I> gene may be identified as an immunologically important gene in seahorse.</P> <P><B>Highlights</B></P> <P> <UL> <LI> Big-belly seahorse thioredoxin-like protein 1 maintain redox homeostasis. </LI> <LI> TXNL1 is a component of 26S proteasome. </LI> <LI> Thiol active CXXC conserved motif consists in ShTXNL1. </LI> <LI> Spatial and temporal mRNA expression was evaluated. </LI> <LI> Radical scavenging ability, antioxidant activity, ferric-reducing activity measured. </LI> </UL> </P>