Molecular cloning, characterization and expression analysis of peroxiredoxin 6 from disk abalone Haliotis discus discus and the antioxidant activity of its recombinant protein
| Autor: | Choon-Gon Kim, Mahanama De Zoysa, Ilson Whang, Sang-Jin Kim, Chamilani Nikapitiya, Jehee Lee, Youn-Ho Lee |
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| Rok vydání: | 2009 |
| Předmět: |
Molecular Sequence Data
Mollusk Venoms Apoptosis DNA Fragmentation Aquatic Science Molecular cloning Biology Antioxidants law.invention law Complementary DNA Haliotis discus Animals Humans Environmental Chemistry Amino Acid Sequence RNA Messenger Cloning Molecular Peptide sequence Phylogeny chemistry.chemical_classification Base Sequence cDNA library Gene Expression Profiling General Medicine biology.organism_classification Molecular biology Recombinant Proteins Amino acid Oxidative Stress Open reading frame Gene Expression Regulation Biochemistry chemistry Recombinant DNA Sequence Alignment Peroxiredoxin VI |
| Zdroj: | Fish & Shellfish Immunology. 27:239-249 |
| ISSN: | 1050-4648 |
| DOI: | 10.1016/j.fsi.2009.05.002 |
| Popis: | Peroxiredoxins (Prxs) play an important role against various oxidative stresses and intra-cellular signal transduction. Peroxiredoxin 6 (PrxVI) was identified from the disk abalone Haliotis discus discus cDNA library and named HdPrxVI. The full length cDNA of HdPrxVI was 1457 bp with a 654 bp open reading frame (ORF) encoding 218 amino acids. The predicted molecular mass and estimated isoelectric point (pI) of HdPrxVI were 24 kDa and 7.3, respectively. The deduced amino acid sequence demonstrated the greatest degree (72.4%) of identity with Crassostrea gigas PrxVI. The conserved peroxidase catalytic center (42PVCTTE47) with a conserved cysteine residue (Cys44) and a catalytic center for PLA2 activity (27GGSWA31) were observed in the sequence, indicating that it is a member of 1-Cys Prx. Real time PCR results revealed that HdPrxVI mRNA is constitutively expressed in all tissues in a tissue-specific manner. During exposure to haemorrhagic septicaemia virus (VHSV), HdPrxVI mRNA transcription was down-regulated in the gill, suggesting that the abalone responded to the viral infection quickly, and HdPrxVI played a physiological role against virus-induced oxidative stress. The purified recombinant HdPrxVI, together with dithiothreitol (DTT), was shown to scavenge H2O2 in human leukemia THP-1 cells and provided protection against H2O2-induced apoptosis. |
| Databáze: | OpenAIRE |
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