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Covalent Protein Modification: An Unignorable Factor for Bisphenol A-Induced Hepatotoxicity.
Hu, Xiaolan; Wu, Jian-Lin; Miao, Wen; Long, Fei; Pan, Hudan; Peng, Tao; Yao, Xiaojun; Li, Na.
Afiliación
  • Hu X; State Key Laboratory of Quality Research in Chinese Medicine, Macau University of Science and Technology, Avenida Wai Long, Taipa 999078, Macau SAR, China.
  • Wu JL; State Key Laboratory of Quality Research in Chinese Medicine, Macau University of Science and Technology, Avenida Wai Long, Taipa 999078, Macau SAR, China.
  • Miao W; State Key Laboratory of Quality Research in Chinese Medicine, Macau University of Science and Technology, Avenida Wai Long, Taipa 999078, Macau SAR, China.
  • Long F; Sino-French Hoffmann Institute, School of Basic Medical Science, State Key Laboratory of Respiratory Disease, Guangzhou Medical University, Guangzhou 510180, China.
  • Pan H; State Key Laboratory of Quality Research in Chinese Medicine, Macau University of Science and Technology, Avenida Wai Long, Taipa 999078, Macau SAR, China.
  • Peng T; Sino-French Hoffmann Institute, School of Basic Medical Science, State Key Laboratory of Respiratory Disease, Guangzhou Medical University, Guangzhou 510180, China.
  • Yao X; State Key Laboratory of Quality Research in Chinese Medicine, Macau University of Science and Technology, Avenida Wai Long, Taipa 999078, Macau SAR, China.
  • Li N; State Key Laboratory of Quality Research in Chinese Medicine, Macau University of Science and Technology, Avenida Wai Long, Taipa 999078, Macau SAR, China.
Environ Sci Technol ; 56(13): 9536-9545, 2022 07 05.
Article en En | MEDLINE | ID: mdl-35593067
Covalent modification of proteins by reactive pollutants/metabolites might trigger various toxicities resulting from the disruption of protein structures and/or functions, which is critical for understanding the mechanism of pollutants-induced toxicity. However, this mechanism has rarely been touched on due to the lack of a methodology. In this research, the protein modification of bisphenol A (BPA) in rats was characterized using a series of liquid chromatography-tandem mass spectrometry (LC-MS) approaches. BPA-modified cysteine (Cys1) was first released from proteins via enzymatic hydrolysis and identified using LC-MS. Moreover, the positive correlation between Cys1 and hepatotoxicity indicated the involvement of protein modification in BPA toxicity. Then, in vitro incubation of BPA with amino acids and protein confirmed that BPA could specifically modify cysteine residues of proteins after bioactivation and provided four additional modification patterns. Finally, 24 BPA-modified proteins were identified from the liver of BPA-exposed rats using proteomic analysis, and they were mainly enriched in oxidative stress-related pathways. The modification on superoxide dismutases, catalase, and glutathione S-transferases disrupted their enzymatic functions, leading to oxidative damage. These results revealed that the covalent protein modification is an unignorable factor for BPA hepatotoxicity. Moreover, the workflow can be applied to identify protein adducts of other emerging contaminants and possible risk.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Contexto en salud: 12_ODS3_hazardous_contamination Problema de salud: 12_unintentional_poisoning Asunto principal: Contaminantes Ambientales / Enfermedad Hepática Inducida por Sustancias y Drogas Tipo de estudio: Prognostic_studies Límite: Animals Idioma: En Revista: Environ Sci Technol Año: 2022 Tipo del documento: Article País de afiliación: China

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Contexto en salud: 12_ODS3_hazardous_contamination Problema de salud: 12_unintentional_poisoning Asunto principal: Contaminantes Ambientales / Enfermedad Hepática Inducida por Sustancias y Drogas Tipo de estudio: Prognostic_studies Límite: Animals Idioma: En Revista: Environ Sci Technol Año: 2022 Tipo del documento: Article País de afiliación: China
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