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Glutathione S-transferase as a biomarker in the Antarctic bivalve Laternula elliptica after exposure to the polychlorinated biphenyl mixture Aroclor 1254

Cited 26 time in scopus
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Title
Glutathione S-transferase as a biomarker in the Antarctic bivalve Laternula elliptica after exposure to the polychlorinated biphenyl mixture Aroclor 1254
Other Titles
남극큰띠조개 Glutathione S-transferase의 PCBs 오염에 대한 생체지표로서의 이용
Authors
Park, Hyun
Ahn, In-Young
Lee, Jiyeon
Shin, Seung Chul
Kim, Hak Jun
Subject
Biochemistry & Molecular Biology; Endocrinology & Metabolism; Toxicology; Zoology
Keywords
Antarctic; Glutathione S-transferases; Induction; Laternula elliptica; Polychlorinated biphenyls
Issue Date
2009
Publisher
Elsevier
Citation
Park, Hyun, et al. 2009. "Glutathione S-transferase as a biomarker in the Antarctic bivalve Laternula elliptica after exposure to the polychlorinated biphenyl mixture Aroclor 1254". COMPARATIVE BIOCHEMISTRY AND PHYSIOLOGY C-TOXICOLOGY & PHARMACOLOGY, 150(4): 528-836.
Abstract
Glutathione S-transferases (GSTs) are a family of multifunctional enzymes involved in cellular detoxification that catalyze the attachment of electrophilic substrates to glutathione. Two classes of GSTs related to the rho and sigma classes of enzymes in Antarctic bivalves have been cloned from Laternula elliptica. The full-length cDNA of rho class GST (leGSTr) is 1530 bp in length and contains an open reading frame (ORF) of 672 bp encoding 223 amino acid residues. The deduced amino acid sequences of this gene have 41% and 40% identity to rho class GSTs from Ctenopharyngodon idella and Pleuronectes platessa, respectively. The sigma class GST (leGSTs) cDNA, however, is 1127 bp in length and contains an ORF of 696 bp encoding 231 amino acid residues. The deduced amino acid sequences share only 22% identity with sigma class GST from Xenopus laevis. The transcriptional expression of leGSTr, leGSTs, and leGSTp cloned in our previous study were examined using real-time polymerase chain reaction in response to exposure to a polychlorinated biphenyl (PCB) mixture. The expressions of these three GST transcripts were rapidly upregulated, although they showed different expression levels and patterns within each isoform. Moreover, leGSTs was the most upregulated in the gill and digestive gland in response to PCB exposure. The recombinant GSTs were highly expressed in transformed Escherichia coli, and their kinetic properties were studied with various substrates. As a result, the three classes of GSTs were found to have diverse biological functions and were responsible for different enzymatic features.
URI
http://repository.kopri.re.kr/handle/201206/6231
DOI
http://dx.doi.org/10.1016/j.cbpc.2009.07.008
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