Disk Abalone, Haliotis discus discus, CuZn-Superoxide Dismutase cDNA and its Transcriptional Induction by Aroclor 1254 SCIE SCOPUS

DC Field Value Language
dc.contributor.author De Zoysa, Mahanama -
dc.contributor.author Ekanayake, Prashani Mudika -
dc.contributor.author Kang, Hyun-Sil -
dc.contributor.author Lee, Jehee -
dc.contributor.author Jee, Youngheun -
dc.contributor.author Lee, Youn-Ho -
dc.contributor.author Kim, Sang-Jin -
dc.date.accessioned 2021-03-17T08:27:55Z -
dc.date.accessioned 2021-03-17T08:27:55Z -
dc.date.available 2021-03-17T08:27:55Z -
dc.date.available 2021-03-17T08:27:55Z -
dc.date.created 2020-01-28 -
dc.date.issued 2009-10 -
dc.identifier.issn 0893-8849 -
dc.identifier.uri https://sciwatch.kiost.ac.kr/handle/2020.kiost/40461 -
dc.description.abstract CuZn-superoxide dismutase (CuZn-SOD) is a key antioxidant enzyme playing a first line protective role against reactive oxygen species (ROS) by converting superoxide (O-2(.)-) into H2O2. The CuZn-SOD gene was isolated from a whole abalone cDNA library and denoted as aCuZn-SOD. The full-length cDNA of aCuZn-SOD was 1021 bp, which contained 465-bp open reading frame (ORF) coding 154 amino acids. It contained highly conserved CuZn-SOD signature motif 1 (45GFHVHQFGDNT55) and motif 2 (139GNAGGRQACGVI150). Also, amino acid residues identified as Cu (His(47), His(49), His(64), and His(121)) and Zn (His(64), His(72), His(81), and ASP(84)) metal-binding sites were completely conserved in the aCuZn-SOD. The reverse transcription polymerase chain reaction (RT-PCR) results showed that aCuZn-SOD mRNA was expressed constitutively in gill, mantle, gonad, abductor muscle, digestive tract, and hemocytes in a tissue-specific manner. The aCuZn-SOD mRNA was significantly up-regulated (P < 0.05) in gill and digestive tract tissues after Aroclor 1254 induction compared to untreated and methanol-injected abalone groups, suggesting that abalone has a potential use in assessing the impact of marine pollutants with the application of gene expression concept. In addition, purified recombinant aCuZn-SOD fusion protein was shown to reduce O-2(.)- radical generated by xanthine oxidase assay, showing CuZn-SOD is a functionally active antioxidant enzyme in disk abalone. -
dc.description.uri 1 -
dc.language English -
dc.publisher WILEY -
dc.subject OXIDATIVE STRESS -
dc.subject MYTILUS-GALLOPROVINCIALIS -
dc.subject ANTIOXIDANT ENZYMES -
dc.subject BIOMARKERS -
dc.subject EXPRESSION -
dc.subject FISH -
dc.subject CONTAMINATION -
dc.subject POLLUTION -
dc.subject CLONING -
dc.subject PURIFICATION -
dc.title Disk Abalone, Haliotis discus discus, CuZn-Superoxide Dismutase cDNA and its Transcriptional Induction by Aroclor 1254 -
dc.type Article -
dc.citation.endPage 658 -
dc.citation.startPage 643 -
dc.citation.title JOURNAL OF THE WORLD AQUACULTURE SOCIETY -
dc.citation.volume 40 -
dc.citation.number 5 -
dc.contributor.alternativeName 이윤호 -
dc.contributor.alternativeName 김상진 -
dc.identifier.bibliographicCitation JOURNAL OF THE WORLD AQUACULTURE SOCIETY, v.40, no.5, pp.643 - 658 -
dc.identifier.doi 10.1111/j.1749-7345.2009.00284.x -
dc.identifier.scopusid 2-s2.0-70350408729 -
dc.identifier.wosid 000270428600006 -
dc.type.docType Article -
dc.description.journalClass 1 -
dc.subject.keywordPlus OXIDATIVE STRESS -
dc.subject.keywordPlus MYTILUS-GALLOPROVINCIALIS -
dc.subject.keywordPlus ANTIOXIDANT ENZYMES -
dc.subject.keywordPlus BIOMARKERS -
dc.subject.keywordPlus EXPRESSION -
dc.subject.keywordPlus FISH -
dc.subject.keywordPlus CONTAMINATION -
dc.subject.keywordPlus POLLUTION -
dc.subject.keywordPlus CLONING -
dc.subject.keywordPlus PURIFICATION -
dc.relation.journalWebOfScienceCategory Fisheries -
dc.description.journalRegisteredClass scie -
dc.description.journalRegisteredClass scopus -
dc.relation.journalResearchArea Fisheries -
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