Molecular cloning and differential expression patterns of sigma and omega glutathione S-transferases from Venerupis philippinarum to heavy metals and benzo[a]pyrene exposure
Glutathione S-transferases (GSTs) are a class of enzymes that facilitate the detoxification of xenobiotics, and also play important roles in antioxidant defense. We identified two glutathione S-transferase isoforms (VpGSTS, sigma GST; VpGSTO, omega GST) from Venerupis philippinarum by RACE approache...
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Published in | Chinese journal of oceanology and limnology Vol. 30; no. 3; pp. 413 - 423 |
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Main Author | |
Format | Journal Article |
Language | English |
Published |
Heidelberg
Springer-Verlag
01.05.2012
SP Science Press Springer Nature B.V |
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Online Access | Get full text |
ISSN | 0254-4059 2096-5508 1993-5005 2523-3521 |
DOI | 10.1007/s00343-012-1173-0 |
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Abstract | Glutathione S-transferases (GSTs) are a class of enzymes that facilitate the detoxification of xenobiotics, and also play important roles in antioxidant defense. We identified two glutathione S-transferase isoforms (VpGSTS, sigma GST; VpGSTO, omega GST) from Venerupis philippinarum by RACE approaches. The open reading frames of VpGSTS and VpGSTO were of 612 bp and 729 bp, encoding 203 and 242 amino acids with an estimated molecular mass of 22.88 and 27.94 kDa, respectively. The expression profiles of VpGSTS and VpGSTO responded to heavy metals and benzo[a]pyrene (B[a]P) exposure were investigated by quantitative real-time RT-PCR. The expression of VpGSTS and VpGSTO were both rapidly up-regulated, however, they showed differential expression patterns to different toxicants. Cd displayed stronger induction of VpGSTS expression with an approximately 12-fold increase than that of VpGSTO with a maximum 6.4-fold rise. Cu exposure resulted in similar expression patterns for both VpGSTS and VpGSTO. For B[a]P exposure, the maximum induction of VpGSTO was approximately two times higher than that of VpGSTS. Altogether, these findings implied the involvement of VpGSTS and VpGSTO in host antioxidant responses, and highlighted their potential as a biomarker to Cd and B[a]P exposure. |
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AbstractList | Glutathione S-transferases (GSTs) are a class of enzymes that facilitate the detoxification of xenobiotics, and also play important roles in antioxidant defense. We identified two glutathione S-transferase isoforms (VpGSTS, sigma GST; VpGSTO, omega GST) from
Venerupis philippinarum
by RACE approaches. The open reading frames of VpGSTS and VpGSTO were of 612 bp and 729 bp, encoding 203 and 242 amino acids with an estimated molecular mass of 22.88 and 27.94 kDa, respectively. The expression profiles of VpGSTS and VpGSTO responded to heavy metals and benzo[a]pyrene (B[a]P) exposure were investigated by quantitative real-time RT-PCR. The expression of VpGSTS and VpGSTO were both rapidly up-regulated, however, they showed differential expression patterns to different toxicants. Cd displayed stronger induction of VpGSTS expression with an approximately 12-fold increase than that of VpGSTO with a maximum 6.4-fold rise. Cu exposure resulted in similar expression patterns for both VpGSTS and VpGSTO. For B[a]P exposure, the maximum induction of VpGSTO was approximately two times higher than that of VpGSTS. Altogether, these findings implied the involvement of VpGSTS and VpGSTO in host antioxidant responses, and highlighted their potential as a biomarker to Cd and B[a]P exposure. Glutathione S-transferases (GSTs) are a class of enzymes that facilitate the detoxification of xenobiotics, and also play important roles in antioxidant defense. We identified two glutathione S-transferase isoforms (VpGSTS, sigma GST; VpGSTO, omega GST) from Venerupis philippinarum by RACE approaches. The open reading frames of VpGSTS and VpGSTO were of 612 bp and 729 bp, encoding 203 and 242 amino acids with an estimated molecular mass of 22.88 and 27.94 kDa, respectively. The expression profiles of VpGSTS and VpGSTO responded to heavy metals and benzo[a]pyrene (B[a]P) exposure were investigated by quantitative real-time RT-PCR. The expression of VpGSTS and VpGSTO were both rapidly up-regulated, however, they showed differential expression patterns to different toxicants. Cd displayed stronger induction of VpGSTS expression with an approximately 12-fold increase than that of VpGSTO with a maximum 6.4-fold rise. Cu exposure resulted in similar expression patterns for both VpGSTS and VpGSTO. For B[a]P exposure, the maximum induction of VpGSTO was approximately two times higher than that of VpGSTS. Altogether, these findings implied the involvement of VpGSTS and VpGSTO in host antioxidant responses, and highlighted their potential as a biomarker to Cd and B[a]P exposure. Glutathione S-transferases (GSTs) are a class of enzymes that facilitate the detoxification of xenobiotics, and also play important roles in antioxidant defense. We identified two glutathione S-transferase isoforms (VpGSTS, sigma GST; VpGSTO, omega GST) from Venerupis philippinarum by RACE approaches. The open reading frames of VpGSTS and VpGSTO were of 612 bp and 729 bp, encoding 203 and 242 amino acids with an estimated molecular mass of 22.88 and 27.94 kDa, respectively. The expression profiles of VpGSTS and VpGSTO responded to heavy metals and benzo[a]pyrene (B[a]P) exposure were investigated by quantitative real-time RT-PCR. The expression of VpGSTS and VpGSTO were both rapidly up-regulated, however, they showed differential expression patterns to different toxicants. Cd displayed stronger induction of VpGSTS expression with an approximately 12-fold increase than that of VpGSTO with a maximum 6.4-fold rise. Cu exposure resulted in similar expression patterns for both VpGSTS and VpGSTO. For B[a]P exposure, the maximum induction of VpGSTO was approximately two times higher than that of VpGSTS. Altogether, these findings implied the involvement of VpGSTS and VpGSTO in host antioxidant responses, and highlighted their potential as a biomarker to Cd and B[a]P exposure. |
Author | Wu, Huifeng Chen, Leilei You, Liping Wang, Qing Zhang, Linbao Liu, Xiaoli Zhao, Jianmin |
AuthorAffiliation | Key Laboratory of Coastal Zone Environmental Processes, Yantai Institute of Coastal Zone Research (YIC), Chinese Academyof Scienees (CAS); Shandong Provincial Key Laboratory of Coastal Zone Environmental Processes, YICCAS, Yantai 264003,China Graduate University of Chinese Academy of Sciences, Beijing 100049, China |
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CitedBy_id | crossref_primary_10_1016_j_aquatox_2016_12_016 crossref_primary_10_1016_j_cbpb_2013_05_005 crossref_primary_10_1016_j_aquatox_2019_105318 crossref_primary_10_1016_j_ecoenv_2016_05_024 crossref_primary_10_1016_j_marpolbul_2025_117858 crossref_primary_10_3390_ijms19103102 |
Cites_doi | 10.1007/s10646-006-0069-1 10.1016/j.aquatox.2009.07.017 10.1016/j.bbagen.2007.05.007 10.1146/annurev.pharmtox.45.120403.095857 10.1016/0025-326X(95)00116-5 10.1379/1466-1268(2003)8<76:MIAEOH>2.0.CO;2 10.1016/j.taap.2004.11.006 10.1021/es010300w 10.1039/b414773a 10.1016/j.gene.2004.11.031 10.1016/j.chemosphere.2005.10.045 10.1016/j.scitotenv.2003.10.021 10.1016/j.fsi.2011.07.026 10.1017/S0025315400018014 10.1016/j.marenvres.2004.03.083 10.1016/j.ecoenv.2009.12.032 10.1007/s00227-004-1423-6 10.1016/S0304-4165(02)00328-8 10.1016/j.marpolbul.2005.12.012 10.1016/j.scitotenv.2003.09.026 10.1016/j.aquatox.2008.06.011 10.1289/ehp.834959 10.1007/s10126-007-9034-0 10.1016/j.chemosphere.2007.05.087 10.1016/S0021-9258(18)68495-9 10.1016/j.cbpb.2007.04.010 10.1016/j.cbpb.2008.03.002 10.1016/j.cbpb.2008.07.012 10.1039/B414773A |
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Notes | Glutathione S-transferases (GSTs) are a class of enzymes that facilitate the detoxification of xenobiotics, and also play important roles in antioxidant defense. We identified two glutathione S-transferase isoforms (VpGSTS, sigma GST; VpGSTO, omega GST) from Venerupis philippinarum by RACE approaches. The open reading frames of VpGSTS and VpGSTO were of 612 bp and 729 bp, encoding 203 and 242 amino acids with an estimated molecular mass of 22.88 and 27.94 kDa, respectively. The expression profiles of VpGSTS and VpGSTO responded to heavy metals and benzo[a]pyrene (B[a]P) exposure were investigated by quantitative real-time RT-PCR. The expression of VpGSTS and VpGSTO were both rapidly up-regulated, however, they showed differential expression patterns to different toxicants. Cd displayed stronger induction of VpGSTS expression with an approximately 12-fold increase than that of VpGSTO with a maximum 6.4-fold rise. Cu exposure resulted in similar expression patterns for both VpGSTS and VpGSTO. For B[a]P exposure, the maximum induction of VpGSTO was approximately two times higher than that of VpGSTS. Altogether, these findings implied the involvement of VpGSTS and VpGSTO in host antioxidant responses, and highlighted their potential as a biomarker to Cd and B[a]P exposure. 37-1150/P Venerupis philippinarum; Glutathione S-transferase; mRNA expression; heavy metals;benzo[a]pyrene; biomarker http://dx.doi.org/10.1007/s00343-012-1173-0 ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 14 content type line 23 |
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Snippet | Glutathione S-transferases (GSTs) are a class of enzymes that facilitate the detoxification of xenobiotics, and also play important roles in antioxidant... Glutathione S-transferases (GSTs) are a class of enzymes that facilitate the detoxification of xenobiotics, and also play important roles in antioxidant... |
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SubjectTerms | Amino acids Animal populations Antioxidants Aromatic hydrocarbons Benzo(a)pyrene Biology Biomarkers Cadmium Chemical contaminants Cloning Copper Detoxification Earth and Environmental Science Earth Sciences Enzymes Exposure Gene expression gene expression regulation Glutathione Glutathione transferase Heavy metals Isoforms Marine Metals molecular cloning Molecular weight Mollusks Nucleotide sequence Oceanography omega Open reading frames PCR Pyrene reverse transcriptase polymerase chain reaction RT-PCR技术 toxic substances Toxicants Transferases Venerupis Venerupis philippinarum Xenobiotics 分子克隆 苯并(a)芘 菲律宾蛤仔 表达模式 谷胱甘肽-S-转移酶 重金属 |
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Title | Molecular cloning and differential expression patterns of sigma and omega glutathione S-transferases from Venerupis philippinarum to heavy metals and benzo[a]pyrene exposure |
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