A thioredoxin domain-containing protein 12 from black rockfish Sebastes schlegelii

Responses to immune challenges and protection from apoptosis against oxidative stress

William Shanthakumar Thulasitha, Navaneethaiyer Umasuthan, R. G P T Jayasooriya, Jae Koo Noh, Hae Chul Park, Jehee Lee

Research output: Contribution to journalArticle

8 Citations (Scopus)

Abstract

Thioredoxin (TXN) superfamily proteins are identified by the presence of a thioredoxin active site with a conserved CXXC active motif. TXN members are involved in a wide range of biochemical and biological functions including redox regulation, refolding of disulfide containing proteins, and regulation of transcription factors. In the present study, a thioredoxin domain-containing protein 12 was identified and characterized from black rockfish, Sebastes schlegelii (RfTXNDC12). The full length of RfTXNDC12 consists of a 522-bp coding region encoding a 173-amino acid protein. It has a 29-amino acid signal peptide and a single TXN active site with a consensus atypical WCGAC active motif. Multiple sequence alignment revealed that the active site is conserved among vertebrates. RfTXNDC12 shares highest identity with its Epinephelus coioides homolog. Transcriptional analysis revealed its ubiquitous expression in a wide range of tissues with the highest expression in the ovary. Immune challenges conducted with Streptococcus iniae and poly I:C caused upregulation of RfTXNDC12 transcript levels in gills and peripheral blood cells (PBCs), while lipopolysaccharide injection caused downregulation of RfTXNDC12 in gills and upregulation in PBCs. Similar to TXN, RfTXNDC12 exhibited insulin disulfide reducing activity. Interestingly, the recombinant protein showed significant protection of LNCaP cells against apoptosis induced by H2O2-mediated oxidative stress in a concentration dependent manner. Collectively, the present data indicate that RfTXNDC12 is a TXN superfamily member, which could function as a potential antioxidant enzyme and be involved in a defense mechanism against immune challenges.

Original languageEnglish
Pages (from-to)29-37
Number of pages9
JournalComparative Biochemistry and Physiology Part - C: Toxicology and Pharmacology
Volume185-186
DOIs
Publication statusPublished - 2016 Jul 1

Fingerprint

Thioredoxins
Oxidative stress
Oxidative Stress
Apoptosis
Proteins
Catalytic Domain
Disulfides
Blood Cells
Blood
Up-Regulation
Amino Acids
Poly I-C
Cytoprotection
Sequence Alignment
Protein Sorting Signals
Protein Domains
Recombinant Proteins
Oxidation-Reduction
Lipopolysaccharides
Vertebrates

Keywords

  • Immune challenge
  • Oxidative stress
  • Rockfish
  • Thioredoxin domain containing protein 12

ASJC Scopus subject areas

  • Biochemistry
  • Cell Biology
  • Physiology
  • Health, Toxicology and Mutagenesis
  • Toxicology

Cite this

A thioredoxin domain-containing protein 12 from black rockfish Sebastes schlegelii : Responses to immune challenges and protection from apoptosis against oxidative stress. / Thulasitha, William Shanthakumar; Umasuthan, Navaneethaiyer; Jayasooriya, R. G P T; Noh, Jae Koo; Park, Hae Chul; Lee, Jehee.

In: Comparative Biochemistry and Physiology Part - C: Toxicology and Pharmacology, Vol. 185-186, 01.07.2016, p. 29-37.

Research output: Contribution to journalArticle

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abstract = "Thioredoxin (TXN) superfamily proteins are identified by the presence of a thioredoxin active site with a conserved CXXC active motif. TXN members are involved in a wide range of biochemical and biological functions including redox regulation, refolding of disulfide containing proteins, and regulation of transcription factors. In the present study, a thioredoxin domain-containing protein 12 was identified and characterized from black rockfish, Sebastes schlegelii (RfTXNDC12). The full length of RfTXNDC12 consists of a 522-bp coding region encoding a 173-amino acid protein. It has a 29-amino acid signal peptide and a single TXN active site with a consensus atypical WCGAC active motif. Multiple sequence alignment revealed that the active site is conserved among vertebrates. RfTXNDC12 shares highest identity with its Epinephelus coioides homolog. Transcriptional analysis revealed its ubiquitous expression in a wide range of tissues with the highest expression in the ovary. Immune challenges conducted with Streptococcus iniae and poly I:C caused upregulation of RfTXNDC12 transcript levels in gills and peripheral blood cells (PBCs), while lipopolysaccharide injection caused downregulation of RfTXNDC12 in gills and upregulation in PBCs. Similar to TXN, RfTXNDC12 exhibited insulin disulfide reducing activity. Interestingly, the recombinant protein showed significant protection of LNCaP cells against apoptosis induced by H2O2-mediated oxidative stress in a concentration dependent manner. Collectively, the present data indicate that RfTXNDC12 is a TXN superfamily member, which could function as a potential antioxidant enzyme and be involved in a defense mechanism against immune challenges.",
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AU - Jayasooriya, R. G P T

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AU - Park, Hae Chul

AU - Lee, Jehee

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