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- Title
Characterization of copper, zinc superoxide dismutase from a cartilaginous shark species, Scyliorhinus torazame (Carcharhiniformes).
- Authors
Nam, Yoon; Cho, Young; Kim, Keun-Yong; Bang, In; Kim, Ki; Kim, Sung; Kim, Dong
- Abstract
A full-length complementary DNA clone encoding copper, zinc superoxide dismutase (Cu, Zn-SOD), a key antioxidant enzyme, was isolated from the evolutionary lower vertebrate shark species, Scyliorhinus torazame. The shark SOD cDNA comprised 30 bp of 5′-untranslated region (UTR), 456 bp of a single open reading frame (ORF) encoding 152 amino acids and 401 bp of 3′-UTR, including consensus polyadenylation signal (AATAAA) and 20 bp of poly-(A+) tail. Deduced amino acid sequence of shark SOD shared relatively high identities with those not only from teleosts (57–72%) but also from other advanced vertebrates (53–65%) with intermediate characteristics. In addition, shark SOD represented unique molecular features that were not seen in other vertebrate SODs. The SOD transcripts were expressed ubiquitously in all tissues examined, including brain, intestine, kidney, liver, muscle and spleen, as determined by reverse transcriptase-polymerase chain reaction (RT-PCR). Acute exposure to cadmium by either injection (0, 1, 2 or 5 mg CdCl2 kg−1 body weight for 2 days) or immersion (0 or 25 μM Cd for 0, 1, 4 and 7 days) altered hepatic SOD mRNA level, based on RNA blot hybridization and semi-quantitative and/or real-time RT-PCR assays. Transcriptional levels of SOD were significantly increased by cadmium exposure generally in a dose- or time-dependent fashion.
- Subjects
CADMIUM; COPPER; CARCHARHINIFORMES; MESSENGER RNA; SCYLIORHINIDAE
- Publication
Fish Physiology & Biochemistry, 2006, Vol 32, Issue 4, p305
- ISSN
0920-1742
- Publication type
Article
- DOI
10.1007/s10695-006-9107-4