Response of a novel selenium-dependent glutathione peroxidase from thick shell mussel Mytilus coruscus exposed to lipopolysaccharide, copper and benzo[α]pyrene.
Fish Shellfish Immunol
; 89: 595-602, 2019 Jun.
Article
en En
| MEDLINE
| ID: mdl-30991153
ABSTRACT
Glutathione peroxidase (GPx) plays an important antioxidant role in cellular defense against environmental stress. In the present study, a novel selenium-dependent glutathione peroxidase termed McSeGPx firstly identified in thick shell mussel Mytilus coruscus. McSeGPx consists of 197 amino acid residues, characterized with one selenocysteine residue encoded by an opal stop codon TGA, one selenocysteine insertion sequence (SECIS) in the 3' untranslated region (UTR), two active site motifs and one signature sequence motif. McSeGPx transcripts were constitutively expressed in all examined tissues, and were significantly induced in gills and digestive glands with the stimulations of lipopolysaccharide (LPS), copper (Cu) and benzo[α]pyrene (B[α]P). Additionally, rough increases in McSeGPx activity were detected in both tissues under the challenge of LPS, Cu and B[α]P. Collectively, these results suggested that McSeGPx affiliate to selenocysteine dependent GPx (SeGPx) family and might play an important role in mediating the environmental stressors and antioxidant response in M. coruscus.
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Bases de datos:
MEDLINE
Asunto principal:
Contaminantes Químicos del Agua
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Regulación de la Expresión Génica
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Mytilus
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Glutatión Peroxidasa
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Inmunidad Innata
Idioma:
En
Revista:
Fish Shellfish Immunol
Año:
2019
Tipo del documento:
Article
País de afiliación:
China