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Article: Effects of N-acetylcysteine on nicotinamide dinucleotide phosphate oxidase activation and antioxidant status in heart, lung, liver and kidney in streptozotocin-induced diabetic rats

TitleEffects of N-acetylcysteine on nicotinamide dinucleotide phosphate oxidase activation and antioxidant status in heart, lung, liver and kidney in streptozotocin-induced diabetic rats
Authors
Keywords15-F 2T-Isoprostane
Antioxidant Status
Diabetes
N-Acetylcysteine
Nadph Oxidase
Issue Date2012
Citation
Yonsei Medical Journal, 2012, v. 53 n. 2, p. 294-303 How to Cite?
Abstract
Purpose: Hyperglycemia increases reactive oxygen species (ROS) and the resulting oxidative stress plays a key role in the pathogenesis of diabetic complications. Nicotinamide dinucleotide phosphate (NADPH) oxidase is one of the major sources of ROS production in diabetes. We, therefore, examined the possibility that NADPH oxidase activation is increased in various tissues, and that the antioxidant N-acetylcysteine (NAC) may have tissue specifc effects on NADPH oxidase and tissue antioxidant status in diabetes. Materials and Methods: Control (C) and streptozotocin-induced diabetic (D) rats were treated either with NAC (1.5 g/kg/ day) orally or placebo for 4 weeks. The plasma, heart, lung, liver, kidney were harvested immediately and stored for biochemical or immunoblot analysis. Results: levels of free 15-F 2t-isoprostane were increased in plasma, heart, lung, liver and kidney tissues in diabetic rats, accompanied with significantly increased membrane translocation of the NADPH oxidase subunit p67phox in all tissues and increased expression of the membrane-bound subunit p22phox in heart, lung and kidney. The tissue antioxidant activity in lung, liver and kidney was decreased in diabetic rats, while it was increased in heart tissue. NAC reduced the expression of p22phox and p67phox, suppressed p67phox membrane translocation, and reduced free 15-F 2t-isoprostane levels in all tissues. NAC increased antioxidant activity in liver and lung, but did not signifcantly affect antioxidant activity in heart and kidney. Conclusion: The current study shows that NAC inhibits NADPH oxidase activation in diabetes and attenuates tissue oxidative damage in all organs, even though its effects on antioxidant activity are tissue specifc. © Yonsei University College of Medicine 2012.
Persistent Identifierhttp://hdl.handle.net/10722/147290
ISSN
2013 Impact Factor: 1.263
2013 SCImago Journal Rankings: 0.495
PubMed Central ID
ISI Accession Number ID
Funding AgencyGrant Number
National Natural Science Foundation of China (NSFC)30872447
Research Grants Council of Hong Kong782910M
Funding Information:

This is supported by grant 30872447 from the National Natural Science Foundation of China (NSFC) and General Research Fund grants 782910M from Research Grants Council of Hong Kong.

References

 

Author Affiliations
  1. The University of Hong Kong
  2. Wuhan University
DC FieldValueLanguage
dc.contributor.authorLei, Sen_US
dc.contributor.authorLiu, Yen_US
dc.contributor.authorLiu, Hen_US
dc.contributor.authorYu, Hen_US
dc.contributor.authorWang, Hen_US
dc.contributor.authorXia, Zen_US
dc.date.accessioned2012-05-29T06:01:17Z-
dc.date.available2012-05-29T06:01:17Z-
dc.date.issued2012en_US
dc.identifier.citationYonsei Medical Journal, 2012, v. 53 n. 2, p. 294-303en_US
dc.identifier.issn0513-5796en_US
dc.identifier.urihttp://hdl.handle.net/10722/147290-
dc.description.abstractPurpose: Hyperglycemia increases reactive oxygen species (ROS) and the resulting oxidative stress plays a key role in the pathogenesis of diabetic complications. Nicotinamide dinucleotide phosphate (NADPH) oxidase is one of the major sources of ROS production in diabetes. We, therefore, examined the possibility that NADPH oxidase activation is increased in various tissues, and that the antioxidant N-acetylcysteine (NAC) may have tissue specifc effects on NADPH oxidase and tissue antioxidant status in diabetes. Materials and Methods: Control (C) and streptozotocin-induced diabetic (D) rats were treated either with NAC (1.5 g/kg/ day) orally or placebo for 4 weeks. The plasma, heart, lung, liver, kidney were harvested immediately and stored for biochemical or immunoblot analysis. Results: levels of free 15-F 2t-isoprostane were increased in plasma, heart, lung, liver and kidney tissues in diabetic rats, accompanied with significantly increased membrane translocation of the NADPH oxidase subunit p67phox in all tissues and increased expression of the membrane-bound subunit p22phox in heart, lung and kidney. The tissue antioxidant activity in lung, liver and kidney was decreased in diabetic rats, while it was increased in heart tissue. NAC reduced the expression of p22phox and p67phox, suppressed p67phox membrane translocation, and reduced free 15-F 2t-isoprostane levels in all tissues. NAC increased antioxidant activity in liver and lung, but did not signifcantly affect antioxidant activity in heart and kidney. Conclusion: The current study shows that NAC inhibits NADPH oxidase activation in diabetes and attenuates tissue oxidative damage in all organs, even though its effects on antioxidant activity are tissue specifc. © Yonsei University College of Medicine 2012.en_US
dc.languageengen_US
dc.relation.ispartofYonsei Medical Journalen_US
dc.subject15-F 2T-Isoprostaneen_US
dc.subjectAntioxidant Statusen_US
dc.subjectDiabetesen_US
dc.subjectN-Acetylcysteineen_US
dc.subjectNadph Oxidaseen_US
dc.titleEffects of N-acetylcysteine on nicotinamide dinucleotide phosphate oxidase activation and antioxidant status in heart, lung, liver and kidney in streptozotocin-induced diabetic ratsen_US
dc.typeArticleen_US
dc.identifier.emailXia, Z:zyxia@hkucc.hku.hken_US
dc.identifier.authorityXia, Z=rp00532en_US
dc.description.naturelink_to_OA_fulltexten_US
dc.identifier.doi10.3349/ymj.2012.53.2.294en_US
dc.identifier.pmid22318816-
dc.identifier.pmcidPMC3282981-
dc.identifier.scopuseid_2-s2.0-84863138767-
dc.identifier.hkuros204908-
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-84856945423&selection=ref&src=s&origin=recordpageen_US
dc.identifier.volume53en_US
dc.identifier.issue2en_US
dc.identifier.spage294en_US
dc.identifier.epage303en_US
dc.identifier.isiWOS:000300213600008-

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