کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
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2432061 | 1106778 | 2012 | 7 صفحه PDF | دانلود رایگان |
Thioredoxin domain-containing protein 12 (Txndc12) belongs to the thioredoxin superfamily, and has roles in redox regulation, defense against oxidative stress, refolding of disulfide-containing proteins, and regulation of transcription factors. In this study, a thioredoxin domain-containing protein 12 was cloned from the marine fish grouper, Epinephelus coioides by RACE PCR, named as Ec-Txndc12. The Ec-Txndc12 encodes 173 amino acid residues with signal peptide in its N-terminal and a thioredoxin (Trx) domain that is homologous with some genes in Mus musculus, Xenopus laveis, etc. Ec-Txndc12 mRNA is predominately expressed in liver, brain and muscle. The expression of Ec-Txndc12 was up-regulated in the liver of grouper challenged with SGIV. In order to elucidate its biological functions, Ec-Txndc12 was recombined and expressed in Escherichia coli BL21 (DE3). The rEc-Txndc12 fusion protein was demonstrated to possess the antioxidant activity. The grouper spleen (GS) cells were treated with a high concentration of rEc-Txndc12 (30 μg/ml), which significantly enhanced cells viability under oxidative damage caused by viral infection. These results together indicated that Ec-Txndc12 could function as an important antioxidant in a physiological context, and might be involved in the responses to viral challenge.
► A thioredoxin domain-containing protein 12 (Txndc12) was firstly cloned from marine fish of orange-spotted grouper, Epinephelus coioides.
► The expression of Ec-Txndc12 was up-regulated in the liver of grouper challenged with SGIV.
► The rEc-Txndc12 fusion protein was demonstrated to possess the antioxidant activity.
Journal: Fish & Shellfish Immunology - Volume 33, Issue 3, September 2012, Pages 667–673