439
Views
3
CrossRef citations to date
0
Altmetric
Research Article

The influence of erdosteine administration on lead-induced oxidative stress in rat muscle

, ORCID Icon, , , , , & show all
Pages 88-92 | Received 05 Jul 2019, Accepted 18 Aug 2019, Published online: 10 Sep 2019

References

  • Aebi, H., 1984. Catalase in vitro. Methods in Enzymology, 105, 121–126.
  • Barlas, A.M., et al., 2017. Erdosteine ameliorates the harmful effects of ischemia-reperfusion injury on the liver of rats. Acta Cirurgica Brasileira, 32 (10), 796–806.
  • Basha, D.C., Basha, S.S., and Reddy, G.R., 2012. Lead-induced cardiac and hematological alterations in aging Wistar male rats: alleviating effects of nutrient metal mixture. Biogerontology, 13 (4), 359–368.
  • Basyigit, I., et al., 2005. Effects of erdosteine on smoking-induced lipid peroxidation in healthy smokers. Drugs in R&D, 6 (2), 83–89.
  • Dal Negro, R., Pozzi, E., and Cella, S.G., 2018. Erdosteine: drug exhibiting polypharmacy for the treatment of respiratory diseases. Pulmonary Pharmacology & Therapeutics, 53, 80–85.
  • Dal Negro, R.W., et al., 2017. Effect of erdosteine on the rate and duration of COPD exacerbations: the RESTORE study. European Respiratory Journal, 50 (4), pii: 1700711.
  • De Giovanni, L., et al., 1991. Lack of gastric adverse effects of erdosteine in rats and men. International Journal of Clinical Pharmacology, Therapy, and Toxicology, 29 (7), 269–273.
  • Dewanjee, S., et al., 2013. Toxic effects of lead exposure in Wistar rats: involvement of oxidative stress and the beneficial role of edible jute (Corchorus olitorius) leaves. Food and Chemical Toxicology, 55, 78–91.
  • Erdem, A., et al., 2017. Protective role of erdosteine pretreatment on oleic acid-induced acute lung injury. The Journal of Surgical Research, 213 (213), 234–242.
  • Gąssowska, M., et al., 2016. Perinatal exposure to lead (Pb) promotes Tau phosphorylation in the rat brain in a GSK-3β and CDK5 dependent manner: relevance to neurological disorders. Toxicology, 347–349, 17–28.
  • Habig, W.H., and Jakoby, W.B., 1981. Assays for differentiation of glutathione S-transferases. Methods in Enzymology, 77, 398–405.
  • Kang, H.G., et al., 2009. Time-dependent changes in lead and delta-aminolevulinic acid after subchronic lead exposure in rats. Human & Experimental Toxicology, 28 (10), 647–654.
  • Kasperczyk, A., et al., 2012. Gene expression and activity of antioxidant enzymes in the blood cells of workers who were occupationally exposed to lead. Toxicology, 301 (1–3), 79–84.
  • Kasperczyk, S., et al., 2013. The administration of N-acetylcysteine reduces oxidative stress and regulates glutathione metabolism in the blood cells of workers exposed to lead. Clinical Toxicology (Philadelphia, Pa.), 51 (6), 480–486.
  • Kasperczyk, S., et al., 2014. Effect of N-acetylcysteine administration on the expression and activities of antioxidant enzymes and the malondialdehyde level in the blood of lead-exposed workers. Environmental Toxicology and Pharmacology, 37 (2), 638–647.
  • Kasperczyk, S., et al., 2014. Effect of treatment with N-acetylcysteine on non-enzymatic antioxidant reserves and lipid peroxidation in workers exposed to lead. Annals of Agricultural and Environmental Medicine, 21 (2), 272–277.
  • Kasperczyk, S., et al., 2016. Effect of N-acetylcysteine administration on homocysteine level, oxidative damage to proteins, and levels of iron (Fe) and Fe-related proteins in lead-exposed workers. Toxicology and Industrial Health, 32 (9), 1607–1618.
  • Lamidi, I.Y., and Akefe, I.O., 2017. Mitigate effects of antioxidants in lead toxicity. Clinical Pharmacology & Toxicology, 1 (1:3), 1–9.
  • Lee, C.M., et al., 2016. Chronic lead poisoning magnifies bone detrimental effects in an ovariectomized rat model of postmenopausal osteoporosis. Experimental and Toxicologic Pathology, 68 (1), 47–53.
  • Matés, J.M., Pérez-Gómez, C., and Núñez de Castro, I., 1999. Antioxidant enzymes and human diseases. Clinical Biochemistry, 32 (8), 595–603.
  • Ohkawa, H., Ohishi, N., and Yagi, K., 1979. Assay for lipid peroxides in animal tissues by thiobarbituric acid reaction. Analytical Biochemistry, 95 (2), 351–358.
  • Oyanagui, Y., 1984. Reevaluation of assay methods and establishment of kit for superoxide dismutase activity. Analytical Biochemistry, 142 (2), 290–296.
  • Paglia, D.E., and Valentine, W.N., 1967. Studies on the quantitative and qualitative characterization of erythrocyte glutathione peroxidase. Journal of Laboratory and Clinical Medicine, 70 (1), 158–169.
  • Richterich, R., 1971. Chemia kliniczna. Warszawa: PZWL.
  • Sisombath, N.S., and Jalilehvand, F., 2015. Similarities between N-Acetylcysteine and Glutathione in Binding to lead(II) Ions. Chemical Research in Toxicology, 28 (12), 2313–2324.
  • Tunc, T., et al., 2009. Protective effect of sulfhydryl-containing antioxidants against ischemia/reperfusion injury of prepubertal rat intestine. Journal of Gastroenterology and Hepatology, 24 (4), 681–687.
  • Tutanc, M., et al., 2012. Effects of erdosteine on cyclosporin-A-induced nephrotoxicity. Human & Experimental Toxicology, 31 (6), 565–573.
  • Waissbluth, S., et al., 2017. The impact of erdosteine on cisplatin-induced ototoxicity: a proteomics approach. European Archives of Oto-Rhino-Laryngology, 274 (3), 1365–1374.
  • Yesildağ, A., et al., 2009. Erdosteine modulates radiocontrast-induced hepatotoxicity in rat. Cell Biochemistry and Function, 27 (3), 142–147.
  • Zhou, S., et al., 2013. Functional interaction of glutathione S-transferase pi and peroxiredoxin 6 in intact cells. The International Journal of Biochemistry & Cell Biology, 45 (2), 401–407.

Reprints and Corporate Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

To request a reprint or corporate permissions for this article, please click on the relevant link below:

Academic Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

Obtain permissions instantly via Rightslink by clicking on the button below:

If you are unable to obtain permissions via Rightslink, please complete and submit this Permissions form. For more information, please visit our Permissions help page.