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Characterization of a catalase from red-lip mullet (Liza haematocheila): Demonstration of antioxidative activity and mRNA upregulation in response to immunostimulants.
Kim, Jeongeun; Perera, N C N; Godahewa, G I; Priyathilaka, Thanthrige Thiunuwan; Lee, Jehee.
Afiliación
  • Kim J; Department of Marine Life Sciences, School of Marine Biomedical Sciences, Jeju National University, Jeju Self-Governing Province 690-756, Republic of Korea.
  • Perera NCN; Department of Marine Life Sciences, School of Marine Biomedical Sciences, Jeju National University, Jeju Self-Governing Province 690-756, Republic of Korea.
  • Godahewa GI; Department of Marine Life Sciences, School of Marine Biomedical Sciences, Jeju National University, Jeju Self-Governing Province 690-756, Republic of Korea; Fish Vaccine Research Center, Jeju National University, Jeju Special Self-Governing Province 690-814, Republic of Korea.
  • Priyathilaka TT; Department of Marine Life Sciences, School of Marine Biomedical Sciences, Jeju National University, Jeju Self-Governing Province 690-756, Republic of Korea; Fish Vaccine Research Center, Jeju National University, Jeju Special Self-Governing Province 690-814, Republic of Korea.
  • Lee J; Department of Marine Life Sciences, School of Marine Biomedical Sciences, Jeju National University, Jeju Self-Governing Province 690-756, Republic of Korea; Fish Vaccine Research Center, Jeju National University, Jeju Special Self-Governing Province 690-814, Republic of Korea. Electronic address: je
Gene ; 712: 143945, 2019 Sep 05.
Article en En | MEDLINE | ID: mdl-31279712
Reactive oxygen species, generated in all the aerobic organisms, can cause oxidative stress. Excessive ROS may become a source of carcinogen due to DNA damage, lipid peroxidation, cell injury, and cell death. In order to prevent these adverse effects of ROS, antioxidant enzymes have evolved in aerobic organisms. Catalase is a major antioxidant enzyme that breaks down excessive H2O2 and inhibits apoptotic cell death. Here we molecularly characterized catalase from red-lip mullet. The cDNA sequence of LhCAT consists of an ORF of 1545 bp, which encodes a 527 amino acid peptide (~60 kDa). Based on bioinformatics analysis, LhCAT possesses a domain architecture characteristic of catalases, including a catalase proximal active site signature and a catalase proximal heme-ligand signature. It also has heme and NADPH binding sites homologous to previously described catalases. Pairwise alignment with its homologs revealed that LhCAT shares 95.1% identity with Oplegnathus fasciatus catalase and 97.4% similarity with Sparus aurata catalase. An uprooted phylogenetic tree demonstrated that LhCAT resides in a clade with catalases from other teleosts and exhibits a close relationship with Oplegnathus fasciatus catalase. Among twelve tissue types, we observed the highest LhCAT mRNA expression in the liver, followed by blood. Immune challenge by Lactococcus garvieae, or Poly I:C in the blood or spleen resulted in up-regulation at 24 h post injection. We also tested the antioxidant activity of recombinant LhCAT against hydrogen peroxide and found its optimal concentration to be 12.5 µg/mL. Collectively, these data suggested that LhCAT play an important role in antioxidant defense and immune response of red-lip mullet.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Catalasa / Smegmamorpha / Proteínas de Peces Límite: Animals Idioma: En Revista: Gene Año: 2019 Tipo del documento: Article Pais de publicación: Países Bajos
Texto completo
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XML
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Catalasa / Smegmamorpha / Proteínas de Peces Límite: Animals Idioma: En Revista: Gene Año: 2019 Tipo del documento: Article Pais de publicación: Países Bajos