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Paraquat-induced oxidative stress and dysfunction of cellular redox systems including antioxidative defense enzymes glutathione peroxidase and thioredoxin reductase.
Toxicol In Vitro. 2007 Apr; 21(3):355-63.TV

Abstract

We examined if paraquat-induced oxidative stress and cytotoxicity in pulmonary microvascular endothelial cells are associated with cellular redox systems such as the glutathione system and the thioredoxin system. Loss of viability, accompanied by marked decreases in glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and thioredoxin reductase activities, occurred 48 h after exposure to 1mM paraquat. These changes were preceded by an increased production of hydrogen peroxide after the decrease in glutathione peroxidase activity. Glutaredoxin activity was not decreased even after exposure to paraquat for 48 h, whereas thioredoxin activity was slightly decreased at 48 h. Unexpectedly, the activity of peroxiredoxin, a non-selenoenzyme, was almost completely lost at 24h. Loss of GAPDH activity and viability was notably aggravated by mercaptosuccinate. Selenium supplementation suppressed the loss of activities of glutathione peroxidase and thioredoxin reductase and alleviated paraquat-induced cytotoxicity. An in vitro experiment demonstrated that GAPDH was highly susceptible to reactive oxygen species generated in the xanthine-xanthine oxidase system, whereas thioredoxin reductase was considerably resistant. Taken together, the results suggest that the reduced regenerative ability of oxidatively damaged proteins including GAPDH due to the inactivation of thioredoxin reductase and glutathione peroxidase by paraquat may contribute to increasing oxidative stress, leading to cell death.

Authors+Show Affiliations

School of Pharmacy, Hokkaido Pharmaceutical University, Otaru, Hokkaido 047-0264, Japan.No affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article

Language

eng

PubMed ID

17055214

Citation

Takizawa, Masashi, et al. "Paraquat-induced Oxidative Stress and Dysfunction of Cellular Redox Systems Including Antioxidative Defense Enzymes Glutathione Peroxidase and Thioredoxin Reductase." Toxicology in Vitro : an International Journal Published in Association With BIBRA, vol. 21, no. 3, 2007, pp. 355-63.
Takizawa M, Komori K, Tampo Y, et al. Paraquat-induced oxidative stress and dysfunction of cellular redox systems including antioxidative defense enzymes glutathione peroxidase and thioredoxin reductase. Toxicol In Vitro. 2007;21(3):355-63.
Takizawa, M., Komori, K., Tampo, Y., & Yonaha, M. (2007). Paraquat-induced oxidative stress and dysfunction of cellular redox systems including antioxidative defense enzymes glutathione peroxidase and thioredoxin reductase. Toxicology in Vitro : an International Journal Published in Association With BIBRA, 21(3), 355-63.
Takizawa M, et al. Paraquat-induced Oxidative Stress and Dysfunction of Cellular Redox Systems Including Antioxidative Defense Enzymes Glutathione Peroxidase and Thioredoxin Reductase. Toxicol In Vitro. 2007;21(3):355-63. PubMed PMID: 17055214.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Paraquat-induced oxidative stress and dysfunction of cellular redox systems including antioxidative defense enzymes glutathione peroxidase and thioredoxin reductase. AU - Takizawa,Masashi, AU - Komori,Kumiko, AU - Tampo,Yoshiko, AU - Yonaha,Masanori, Y1 - 2006/09/14/ PY - 2006/03/02/received PY - 2006/08/02/revised PY - 2006/09/06/accepted PY - 2006/10/24/pubmed PY - 2007/6/8/medline PY - 2006/10/24/entrez SP - 355 EP - 63 JF - Toxicology in vitro : an international journal published in association with BIBRA JO - Toxicol In Vitro VL - 21 IS - 3 N2 - We examined if paraquat-induced oxidative stress and cytotoxicity in pulmonary microvascular endothelial cells are associated with cellular redox systems such as the glutathione system and the thioredoxin system. Loss of viability, accompanied by marked decreases in glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and thioredoxin reductase activities, occurred 48 h after exposure to 1mM paraquat. These changes were preceded by an increased production of hydrogen peroxide after the decrease in glutathione peroxidase activity. Glutaredoxin activity was not decreased even after exposure to paraquat for 48 h, whereas thioredoxin activity was slightly decreased at 48 h. Unexpectedly, the activity of peroxiredoxin, a non-selenoenzyme, was almost completely lost at 24h. Loss of GAPDH activity and viability was notably aggravated by mercaptosuccinate. Selenium supplementation suppressed the loss of activities of glutathione peroxidase and thioredoxin reductase and alleviated paraquat-induced cytotoxicity. An in vitro experiment demonstrated that GAPDH was highly susceptible to reactive oxygen species generated in the xanthine-xanthine oxidase system, whereas thioredoxin reductase was considerably resistant. Taken together, the results suggest that the reduced regenerative ability of oxidatively damaged proteins including GAPDH due to the inactivation of thioredoxin reductase and glutathione peroxidase by paraquat may contribute to increasing oxidative stress, leading to cell death. SN - 0887-2333 UR - https://www.unboundmedicine.com/medline/citation/17055214/Paraquat_induced_oxidative_stress_and_dysfunction_of_cellular_redox_systems_including_antioxidative_defense_enzymes_glutathione_peroxidase_and_thioredoxin_reductase_ L2 - https://linkinghub.elsevier.com/retrieve/pii/S0887-2333(06)00187-1 DB - PRIME DP - Unbound Medicine ER -