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Cisplatin induced a significant reduction in testicular weights, plasma testosterone, and testicular reduced glutathione levels in addition to a significant elevation of testicular malondialdehyde levels and testicular gene expressions of inducible nitric oxide synthase (iNOS), tumor necrosis factor‐α (TNF‐α), and p38 mitogen‐activated protein kinase (MAPK) when compared with the control group (\u003Cjats:italic>p\u003C\u002Fjats:italic> < 0.05). Lower tubular diameters and depletion of germ cells and irregular small seminiferous tubules with Sertoli cells only were observed in the cisplatin group. Arjunolic acid administration significantly corrected the changes in both biochemical and histopathological parameters. Arjunolic acid plays a significant protective role against cisplatin‐induced testicular injury by attenuating oxidative stress parameters along with downregulation of iNOS, TNF‐α, and p38‐MAPK testicular expressions.\u003C\u002Fjats:p>",{"EN":191},"Cisplatin‐Induced Testicular Toxicity in Rats: The Protective Effect of Arjunolic Acid",{"VOID":193},"25130312",{"VOID":195},"10.1002\u002Fjbt.21593","PUBLICATION","VERIFIED","2024-10-09T23:07:10.940+00:00","Auto Verify",[201],"EN","https:\u002F\u002Fonlinelibrary.wiley.com\u002Fdoi\u002F10.1002\u002Fjbt.21593",[204,226,248],{"id":205,"sortIndex":152,"researcher":24,"roles":206,"affiliations":207,"properties":219},"284238b4-a01d-4f7a-bdbb-6aa1357aeb56",[],[208],{"id":209,"sortIndex":25,"affiliation":210,"properties":24},"aa1b808d-9d13-4548-85de-955ce719f53c",{"id":211,"createTime":212,"updateTime":213,"relativeEntities":214,"slug":215,"properties":216,"entityType":85,"verifyStatus":23,"verifyTime":24,"verifyNote":24,"syncStatus":23,"languages":24,"translateLanguages":24,"viewCount":25},"74c66926-c1b7-412b-807d-3a0e8a3adbfe","2024-01-09T01:53:10.888+00:00","2024-10-09T23:07:10.978+00:00",[],"Urology-and-Nephrology-Center-Faculty-of-Medicine-Mansoura-University-Mansoura-Egypt",{"title":217},{"VI":218},"Urology and Nephrology Center, Faculty of Medicine, Mansoura University, Mansoura, Egypt",{"openalex":220,"orcid":222,"title":224},{"VOID":221},"A5053494576",{"VOID":223},"https:\u002F\u002Forcid.org\u002F0000-0002-1529-8909",{"EN":225},"Osama Sarhan",{"id":227,"sortIndex":25,"researcher":24,"roles":228,"affiliations":229,"properties":241},"18c6b1c7-e1de-4d7c-92c8-7d759bdbd6df",[],[230],{"id":231,"sortIndex":25,"affiliation":232,"properties":24},"eaa931d3-223f-4098-b712-16e0bea25f40",{"id":233,"createTime":234,"updateTime":235,"relativeEntities":236,"slug":237,"properties":238,"entityType":85,"verifyStatus":23,"verifyTime":24,"verifyNote":24,"syncStatus":23,"languages":24,"translateLanguages":24,"viewCount":25},"f8e608c1-14ad-4a97-b45d-37c748cd0684","2023-11-29T14:18:48.361+00:00","2024-10-09T23:07:10.954+00:00",[],"Department-of-Biochemistry-Mansoura-University-Mansoura-Egypt",{"title":239},{"VI":240},"Department of Biochemistry, Mansoura University, Mansoura, Egypt",{"openalex":242,"orcid":244,"title":246},{"VOID":243},"A5013192978",{"VOID":245},"https:\u002F\u002Forcid.org\u002F0000-0002-9487-3456",{"EN":247},"Iman O. 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present study was designed to evaluate the preventive effects of \u003Cjats:italic>N\u003C\u002Fjats:italic>‐acetyl cysteine on lipid peroxide metabolism in isoproterenol (ISO) induced myocardial infarcted rats. Male albino Wistar rats were pretreated with \u003Cjats:italic>N\u003C\u002Fjats:italic>‐acetyl cysteine (5 and 10 mg\u002Fkg) daily for a period of 14 days. After the pretreatment period, ISO (100 mg\u002Fkg) was subcutaneously injected to rats twice at an interval of 24 h. Increased activities of serum creatine kinase, creatine kinase‐MB, lactate dehydrogenase, and increased intensities of serum lactate dehydrogenase‐isoenzyme bands (LDH‐1, LDH‐2) were observed in ISO‐induced rats. The heart lipid peroxidation products were significantly increased, and the antioxidant system was significantly reduced in ISO‐induced rats. Pretreatment with \u003Cjats:italic>N\u003C\u002Fjats:italic>‐acetyl cysteine (5 and 10 mg\u002Fkg) to ISO‐induced rats showed significant effects on all the biochemical parameters studied. Histopathological findings of the myocardium also showed the protective role of \u003Cjats:italic>N\u003C\u002Fjats:italic>‐acetyl cysteine in ISO‐induced rats. Furthermore, in vitro study confirmed the potent‐free radical scavenging activity of \u003Cjats:italic>N\u003C\u002Fjats:italic>‐acetyl cysteine. The effect at a dose of 10 mg\u002Fkg of \u003Cjats:italic>N\u003C\u002Fjats:italic>‐acetyl cysteine was more pronounced than the dose, 5 mg\u002Fkg. The results of our study show that \u003Cjats:italic>N\u003C\u002Fjats:italic>‐acetyl cysteine protects the heart against ISO‐induced myocardial infarction by its free radical scavenging effect. © 2010 Wiley Periodicals, Inc. J Biochem Mol Toxicol 25:151–157 2011; View this article online at \u003Cjats:ext-link xmlns:xlink=\"http:\u002F\u002Fwww.w3.org\u002F1999\u002Fxlink\" xlink:href=\"http:\u002F\u002Fwileyonlinelibrary.com\">wileyonlinelibrary.com\u003C\u002Fjats:ext-link>. DOI 10.1002\u002Fjbt.20371\u003C\u002Fjats:p>",{"EN":421},"RETRACTED: Protective effects of \u003Ci>N\u003C\u002Fi>‐acetyl cysteine on lipid peroxide metabolism on isoproterenol‐induced myocardial infarcted rats",{"VOID":423},"21671307",{"VOID":425},"10.1002\u002Fjbt.20371",[201],"https:\u002F\u002Fonlinelibrary.wiley.com\u002Fdoi\u002F10.1002\u002Fjbt.20371",[429,451],{"id":430,"sortIndex":25,"researcher":24,"roles":431,"affiliations":432,"properties":444},"e248f7bd-b023-4c5f-9b7f-fd9412ac6829",[],[433],{"id":434,"sortIndex":25,"affiliation":435,"properties":24},"06aa5e3e-728f-42b9-9203-25cf967655c3",{"id":436,"createTime":437,"updateTime":438,"relativeEntities":439,"slug":440,"properties":441,"entityType":85,"verifyStatus":23,"verifyTime":24,"verifyNote":24,"syncStatus":23,"languages":24,"translateLanguages":24,"viewCount":25},"e902d3b5-cad3-4a68-adae-01f89925ff00","2023-12-19T18:41:09.964+00:00","2024-11-25T21:22:45.411+00:00",[],"Department-of-Biochemistry-and-Biotechnology-Annamalai-University-Annamalai-Nagar-608-002-Tamil-Nadu-India",{"title":442},{"VI":443},"Department of Biochemistry and Biotechnology, Annamalai University, Annamalai Nagar—608 002, Tamil Nadu, India",{"openalex":445,"orcid":447,"title":449},{"VOID":446},"A5070454315",{"VOID":448},"https:\u002F\u002Forcid.org\u002F0000-0001-6863-7372",{"EN":450},"Mohamed Fizur Nagoor Meeran",{"id":452,"sortIndex":150,"researcher":24,"roles":453,"affiliations":454,"properties":461},"71f895ba-98c9-4001-86a1-366e85031f91",[],[455],{"id":456,"sortIndex":25,"affiliation":457,"properties":24},"16eb09e6-ad21-4312-a26e-31d7079b2a70",{"id":436,"createTime":437,"updateTime":438,"relativeEntities":458,"slug":440,"properties":459,"entityType":85,"verifyStatus":23,"verifyTime":24,"verifyNote":24,"syncStatus":23,"languages":24,"translateLanguages":24,"viewCount":25},[],{"title":460},{"VI":443},{"openalex":462,"orcid":464,"title":466},{"VOID":463},"A5078640076",{"VOID":465},"https:\u002F\u002Forcid.org\u002F0000-0002-6840-4074",{"EN":467},"P. 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Res Commun, Chem Pathol Pharmacol, 57, 15",{},{"id":24,"text":525,"url":24,"identifiers":526},"10.1074\u002Fjbc.M004583200",{"doi":525},{"id":24,"text":528,"url":24,"identifiers":529},"10.1111\u002Fj.1742-7843.2004.pto940303.x",{"doi":528},{"id":24,"text":531,"url":24,"identifiers":532},"10.1016\u002FS0300-9084(02)00039-1",{"doi":531},{"id":24,"text":534,"url":24,"identifiers":535},"De Caro L, 1989, Pharmacokinetics and bioavailability of oral acetylcysteine in healthy volunteers, Arzneim Forsch, 39, 382",{},{"id":24,"text":537,"url":24,"identifiers":538},"Bonanomi L, 1980, Toxicological, pharmacokinetic and metabolic studies on acetylcysteine, Eur J Respir Dis, 61, 45",{},{"id":24,"text":540,"url":24,"identifiers":541},"10.1093\u002Fclinchem\u002F29.1.189",{"doi":540},{"id":24,"text":543,"url":24,"identifiers":544},"10.1016\u002F0891-5849(88)90023-8",{"doi":543},{"id":24,"text":546,"url":24,"identifiers":547},"10.1016\u002F0003-2697(92)90122-N",{"doi":546},{"id":24,"text":549,"url":24,"identifiers":550},"Kakkar P, 1984, A modified spectrophotometric assay of superoxide dismutase, Ind J Biochem Biophys, 21, 130",{},{"id":24,"text":552,"url":24,"identifiers":553},"10.1016\u002F0003-2697(72)90132-7",{"doi":552},{"id":24,"text":555,"url":24,"identifiers":556},"10.1126\u002Fscience.179.4073.588",{"doi":555},{"id":24,"text":558,"url":24,"identifiers":559},"10.1016\u002F0003-9861(59)90090-6",{"doi":558},{"id":24,"text":561,"url":24,"identifiers":562},"10.1016\u002F0076-6879(79)62181-X",{"doi":561},{"id":24,"text":564,"url":24,"identifiers":565},"Baker H, 1980, Plasma tocopherol in man at various times after ingesting free or acetylated tocopherol, Nutr Rep Int, 21, 531",{},{"id":24,"text":567,"url":24,"identifiers":568},"10.1016\u002FS0021-9258(19)52451-6",{"doi":567},{"id":24,"text":570,"url":24,"identifiers":571},"10.1002\u002Fptr.687",{"doi":570},{"id":24,"text":573,"url":24,"identifiers":574},"Mathew S, 1985, Effect of administration of vitamin A, ascorbic acid and nicotinamide adenine dinucleotide + flavin adenine nucleotide on severity of myocardial infarction induced by isoproterenol in rats, Ind J Exp Biol, 23, 500",{},{"id":24,"text":576,"url":24,"identifiers":577},"10.1093\u002Fclinchem\u002F42.11.1770",{"doi":576},{"id":24,"text":579,"url":24,"identifiers":580},"10.1080\u002F09553008014550261",{"doi":579},{"id":24,"text":582,"url":24,"identifiers":583},"10.1002\u002Fjcb.240531040",{"doi":582},{"id":585,"createTime":586,"updateTime":586,"relativeEntities":587,"slug":588,"properties":589,"entityType":196,"verifyStatus":197,"verifyTime":586,"verifyNote":199,"syncStatus":23,"languages":603,"translateLanguages":24,"viewCount":25,"primaryUrl":604,"fullTextUrl":24,"authors":605,"publicationType":270,"publisherRelationship":639,"citationCount":677,"citationInfo":678,"publishDate":680,"publishYear":681,"citationAnalyzeStatus":23,"lastCitationAnalyze":24,"indexDatabases":24,"openAccess":24,"references":682,"isForceReanalyzing":406},"2d4e809a-ea5e-4c28-b25e-1c06494b30b7","2024-09-26T21:21:18.978+00:00",[],"Protective-effects-of-i-N-i-acetyl-cysteine-on-membrane-bound-adenosine-triphosphatases-and-minerals-in-isoproterenol-induced-myocardial-infarcted-rats-An-in-vivo-and-in-vitro-study",{"mag":590,"keywords":592,"openalex":593,"abstract":595,"title":597,"pm":599,"doi":601},{"VOID":591},"2151560522",{},{"VOID":594},"W2151560522",{"EN":596},"\u003Cjats:title>Abstract\u003C\u002Fjats:title>\u003Cjats:p>The present study was aimed to evaluate the protective effects of \u003Cjats:italic>N\u003C\u002Fjats:italic>‐acetyl cysteine (NAC) on changes in the activities\u002Flevels of adenosine triphosphatases and minerals in isoproterenol‐induced myocardial‐infarcted rats. Male albino Wistar rats were pretreated with NAC (10 mg\u002Fkg body weight) daily for a period of 14 days. After pretreatment period, rats were induced myocardial infarction (MI) by isoproterenol (100 mg\u002Fkg body weight). The activity of sodium\u002Fpotassium‐dependent adenosine triphosphatase was decreased, and the activities of calcium‐ and magnesium‐dependent adenosine triphosphatases were increased in the heart of isoproterenol‐induced myocardial‐infarcted rats. Furthermore, the levels of potassium were lowered and the levels of sodium and calcium were increased in the heart of isoproterenol‐induced rats. Increased plasma lipid peroxidation was observed in isoproterenol‐induced rats. Pretreatment with NAC showed protective effects on adenosine triphosphatases, minerals, and lipid peroxidation. The in vitro study confirmed the reducing property of NAC. The observed effects are due to the membrane‐stabilizing and antioxidant effects of NAC. The results of this study will be useful for the prevention of MI. © 2012 Wiley Periodicals, Inc. J Biochem Mol Toxicol 26:276–281, 2012; View this article online at \u003Cjats:ext-link xmlns:xlink=\"http:\u002F\u002Fwww.w3.org\u002F1999\u002Fxlink\" xlink:href=\"wileyonlinelibrary.com\">wileyonlinelibrary.com\u003C\u002Fjats:ext-link>. DOI 10.1002\u002Fjbt.21419\u003C\u002Fjats:p>",{"EN":598},"Protective effects of \u003Ci>N\u003C\u002Fi>‐acetyl cysteine on membrane‐bound adenosine triphosphatases and minerals in isoproterenol‐induced myocardial‐infarcted rats: An in vivo and in vitro study",{"VOID":600},"22696312",{"VOID":602},"10.1002\u002Fjbt.21419",[201],"https:\u002F\u002Fonlinelibrary.wiley.com\u002Fdoi\u002F10.1002\u002Fjbt.21419",[606,625],{"id":607,"sortIndex":150,"researcher":24,"roles":608,"affiliations":609,"properties":621},"402079d6-9b04-45f0-b46c-3dc3621da46c",[],[610],{"id":611,"sortIndex":25,"affiliation":612,"properties":24},"6f31d355-b4bb-49c5-a50f-51136927d51d",{"id":613,"createTime":614,"updateTime":615,"relativeEntities":616,"slug":617,"properties":618,"entityType":85,"verifyStatus":23,"verifyTime":24,"verifyNote":24,"syncStatus":23,"languages":24,"translateLanguages":24,"viewCount":25},"f92c2cd8-5067-44fe-b47c-05138fa463e4","2023-12-25T17:01:14.018+00:00","2025-01-29T10:24:10.168+00:00",[],"Department-of-Biochemistry-and-Biotechnology-Annamalai-University-Annamalai-Nagar-608-002-India",{"title":619},{"VI":620},"Department of Biochemistry and Biotechnology, Annamalai University, Annamalai Nagar 608 002, 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flavonoids intake has been reported inversely related to the incidence of cardiovascular diseases (CVD). The present study is undertaken to evaluate the preventive role of naringin on mitochondrial enzymes in isoproterenol (ISO)‐induced myocardial infarction in male albino Wistar rats. Rats subcutaneously injected with ISO (85 mg\u002Fkg) at an interval of 24 h for 2 days, resulting in significant (\u003Cjats:italic>p\u003C\u002Fjats:italic> < 0.05) increase in the levels of mitochondrial lipid peroxides. ISO‐induction also showed significant (\u003Cjats:italic>p\u003C\u002Fjats:italic> < 0.05) decrease in the activities of mitochondrial tricarboxylic acid cycle enzymes (isocitrate dehydrogenase, succinate dehydrogenase, malate dehydrogenase, and α‐ketoglutarate dehydrogenase) and respiratory chain enzymes (NADH dehydrogenase and cytochrome c oxidase). Oral pretreatment with naringin (10, 20, and 40 mg\u002Fkg) to ISO‐induced rats daily for a period of 56 days significantly (\u003Cjats:italic>p\u003C\u002Fjats:italic> < 0.05) minimized the alterations in all the biochemical parameters and restored the normal mitochondrial function. Transmission electron microscopic (TEM) observations also correlated with these biochemical findings. Thus, our findings demonstrate that naringin prevents the mitochondrial dysfunction during ISO‐induced myocardial infarction in rats. © 2007 Wiley Periodicals, Inc. J Biochem Mol Toxicol 21:354–361, 2007; Published online in Wiley InterScience (\u003Cjats:ext-link xmlns:xlink=\"http:\u002F\u002Fwww.w3.org\u002F1999\u002Fxlink\" xlink:href=\"http:\u002F\u002Fwww.interscience.wiley.com\">www.interscience.wiley.com\u003C\u002Fjats:ext-link>). DOI 10.1002\u002Fjbt.20203\u003C\u002Fjats:p>",{"EN":758},"RETRACTED: Preventive effect of naringin on cardiac mitochondrial enzymes during isoproterenol‐induced myocardial infarction in rats: A transmission electron microscopic study",{"VOID":760},"17994577",{"VOID":762},"10.1002\u002Fjbt.20203","2024-09-26T21:21:10.796+00:00",[201],"https:\u002F\u002Fonlinelibrary.wiley.com\u002Fdoi\u002F10.1002\u002Fjbt.20203",[767,786],{"id":768,"sortIndex":150,"researcher":24,"roles":769,"affiliations":770,"properties":782},"f762603b-7335-43f6-842f-a883a74356bf",[],[771],{"id":772,"sortIndex":25,"affiliation":773,"properties":24},"bcac4a2b-ed11-47ed-b70c-fcb47d172532",{"id":774,"createTime":775,"updateTime":776,"relativeEntities":777,"slug":778,"properties":779,"entityType":85,"verifyStatus":23,"verifyTime":24,"verifyNote":24,"syncStatus":23,"languages":24,"translateLanguages":24,"viewCount":25},"751d446e-7ff7-4629-8263-4b5cf59e80a5","2023-12-05T15:29:55.143+00:00","2024-09-26T21:21:10.812+00:00",[],"Department-of-Biochemistry-and-Biotechnology-Annamalai-University-Annamalainagar-608-002-Tamil-Nadu-India",{"title":780},{"VI":781},"Department of Biochemistry and Biotechnology, Annamalai University, Annamalainagar 608 002, Tamil Nadu, India",{"openalex":783,"orcid":784,"title":785},{"VOID":463},{"VOID":465},{"EN":467},{"id":787,"sortIndex":25,"researcher":24,"roles":788,"affiliations":789,"properties":796},"253cc04c-8239-43f4-97e7-37b076b316b0",[],[790],{"id":791,"sortIndex":25,"affiliation":792,"properties":24},"31b8fcab-68d6-4eff-b382-1bbc1b399b86",{"id":774,"createTime":775,"updateTime":776,"relativeEntities":793,"slug":778,"properties":794,"entityType":85,"verifyStatus":23,"verifyTime":24,"verifyNote":24,"syncStatus":23,"languages":24,"translateLanguages":24,"viewCount":25},[],{"title":795},{"VI":781},{"openalex":797,"orcid":799,"title":801},{"VOID":798},"A5017776581",{"VOID":800},"https:\u002F\u002Forcid.org\u002F0000-0003-3382-8421",{"EN":802},"M. 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Male albino Wistar rats were pre and cotreated with thymol (7.5 mg\u002Fkg body weight) daily for 7 days. ISO (100 mg\u002Fkg body weight) was subcutaneously injected into rats on 6th and 7th day to induce myocardial infarction (MI). Increased activity\u002Flevels of serum creatine kinase‐MB (CK‐MB), plasma thiobarbituric acid reactive substances, lipid hydroperoxides, and conjugated dienes with decreased levels of plasma reduced glutathione (GSH), vitamin C, and vitamin E were observed in ISO‐induced myocardial infarcted rats. Pre and cotreatment with thymol (7.5 mg\u002Fkg body weight) showed normalized activity of serum CK‐MB and near normalized levels of plasma lipid peroxidation products, reduced GSH, vitamin C, and vitamin E in myocardial infarcted rats. Furthermore, the in vitro study on reducing power of thymol confirmed its potent antioxidant action. Thus, thymol protects ISO‐induced MI in rats by its antilipid peroxidation and antioxidant properties. © 2012 Wiley Periodicals, Inc. J Biochem Mol Toxicol 26:368–373, 2012; View this article online at \u003Cjats:ext-link xmlns:xlink=\"http:\u002F\u002Fwww.w3.org\u002F1999\u002Fxlink\" xlink:href=\"wileyonlinelibrary.com\">wileyonlinelibrary.com\u003C\u002Fjats:ext-link>. DOI 10.1002\u002Fjbt.21431\u003C\u002Fjats:p>",{"EN":961},"Protective effects of thymol on altered plasma lipid peroxidation and nonenzymic antioxidants in isoproterenol‐induced myocardial infarcted 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effect of Cadmium (Cd) on the expression of c‐Jun \u003Cjats:italic>N\u003C\u002Fjats:italic>‐terminal kinase (JNK), \u003Cjats:italic>c‐jun\u003C\u002Fjats:italic>, and activator protein‐1 (AP‐1) has been investigated. We previously reported that Cd causes cell damage as indicated by increases in the cytotoxic parameters, lactate dehydrogenase and lipid peroxidation, and this damage was mediated by decreases in cellular concentration of glutathione. In the present study, we investigate the molecular events involved prior to the Cd‐induced cellular toxicity and damage in primary rat hepatocytes. We propose that Cd, through the generation of reactive oxygen species (ROS) and prior to significant cellular damage, activates the stress activated signal protein JNK, regulates \u003Cjats:italic>c‐jun\u003C\u002Fjats:italic> expression, and promotes the binding of a redox sensitive transcription factor AP‐1. We show JNK activity and \u003Cjats:italic>c‐jun\u003C\u002Fjats:italic> mRNA level significantly increased at 1 h and AP‐1 DNA binding activity significantly enhanced at 3 h in the presence of 4 μM cadmium chloride. Blocking the Cd induction of JNK activity, \u003Cjats:italic>c‐jun\u003C\u002Fjats:italic> mRNA level, and AP‐1 binding activity using the antioxidants \u003Cjats:italic>N\u003C\u002Fjats:italic>‐acetyl cysteine (10 mM) or carnosol (0.5 μg\u002FmL) suggests a role for ROS. Blocking JNK activity and \u003Cjats:italic>c‐jun\u003C\u002Fjats:italic> mRNA by SP600125 (20 μM), a JNK inhibitor, supports the role of JNK in transmission of signals induced by Cd. © 2004 Wiley Periodicals, Inc. J Biochem Mol Toxicol 18:133–142, 2004; Published online in Wiley InterScience (www.interscience.wiley.com). DOI 10.1002\u002Fjbt.20018\u003C\u002Fjats:p>",{"EN":1110},"Characterization of Cd‐induced molecular events prior to cellular damage in primary rat hepatocytes in culture: Activation of the stress activated signal protein JNK and transcription factor AP‐1",{"VOID":1112},"15252869",{"VOID":1114},"10.1002\u002Fjbt.20018",[201],"https:\u002F\u002Fonlinelibrary.wiley.com\u002Fdoi\u002F10.1002\u002Fjbt.20018",[1118,1138],{"id":1119,"sortIndex":25,"researcher":24,"roles":1120,"affiliations":1121,"properties":1133},"a98a2a9c-2c79-484b-8ba6-9d679e458308",[],[1122],{"id":1123,"sortIndex":25,"affiliation":1124,"properties":24},"bd36f183-3ad9-46f8-84ac-432824af7b57",{"id":1125,"createTime":1126,"updateTime":1127,"relativeEntities":1128,"slug":1129,"properties":1130,"entityType":85,"verifyStatus":23,"verifyTime":24,"verifyNote":24,"syncStatus":23,"languages":24,"translateLanguages":24,"viewCount":25},"9ff8bca1-4ff3-4778-a37b-2a1545210989","2023-12-07T12:47:47.255+00:00","2024-10-03T21:17:32.475+00:00",[],"Department-of-Biological-Sciences-Western-Michigan-University-Kalamazoo-MI-49008-USA",{"title":1131},{"VI":1132},"Department of Biological Sciences, Western Michigan University, Kalamazoo, MI 49008, USA",{"openalex":1134,"title":1136},{"VOID":1135},"A5077679281",{"EN":1137},"Chin-Ju J. 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We have made considerable progress in understanding the fundamental mechanisms that regulate the biological response to ozone. It is increasingly clear that genes of innate immunity play a central role in both infectious and noninfectious lung disease. The biological response to ambient ozone provides a clinically relevant environmental exposure that allows us to better understand the role of innate immunity in noninfectious airways disease. In this brief review, we focus on (1) specific cell types in the lung modified by ozone, (2) ozone and oxidative stress, (3) the relationship between genes of innate immunity and ozone, (4) the role of extracellular matrix in reactive airways disease, and (5) the effect of ozone on the adaptive immune system. We summarize recent advances in understanding the mechanisms that ozone contributes to environmental airways disease. © 2012 Wiley Periodicals, Inc. 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proteomics was performed to identify proteins in the liver of \u003Cjats:italic>Takifugu rubripes\u003C\u002Fjats:italic> in response to excessive fluoride exposure. Sixteen fish were randomly divided into a control group and an experimental group. The control group was raised in soft water alone (F\u003Cjats:sup>−\u003C\u002Fjats:sup> = 0.4 mg\u002FL), and the experimental group was raised in the same water with sodium fluoride at a high concentration of 35 mg\u002FL. After 3 days, proteins were extracted from the fish livers and then subjected to two‐dimensional polyacrylamide gel electrophoresis analysis. The matrix‐assisted laser desorption ionization time‐of‐flight mass spectrometry (MALDI‐TOF‐MS) was applied to identify the proteins that were differentially expressed from the two groups of fish. Among an average of 816 and 918 proteins detected in the control and treated groups, respectively, 16 proteins were upregulated and 35 were downregulated (\u003Cjats:italic>P\u003C\u002Fjats:italic> < 0.01) in the fluoride‐treated group as compared with those in the control group. Twenty‐four highly differentially expressed proteins were further analyzed by MALDI‐TOF\u002FTOF‐MS, and eight were identified by Mascot. These eight proteins include disulfide isomerase ER‐60, 4SNc‐Tudor domain protein, SMC3 protein, Cyclin D1, and mitogen‐activated protein kinase 10, as well as three unknown proteins. Consistent with their previously known functions, these identified proteins seem to be involved in apoptosis and other functions associated with fluorosis. These results will greatly contribute to our understanding of the effects of fluoride exposure on the physiological and biochemical functions of \u003Cjats:italic>Takifugu\u003C\u002Fjats:italic> and the toxicological mechanism of fluoride causing fluorosis in both fish and human. © 2010 Wiley Periodicals, Inc. J Biochem Mol Toxicol 24:21–28, 2010; Published online in Wiley InterScience (\u003Cjats:ext-link xmlns:xlink=\"http:\u002F\u002Fwww.w3.org\u002F1999\u002Fxlink\" xlink:href=\"http:\u002F\u002Fwww.interscience.wiley.com\">www.interscience.wiley.com\u003C\u002Fjats:ext-link>). DOI 10.1002\u002Fjbt.20308\u003C\u002Fjats:p>",{"EN":2376},"Proteomics analysis of liver samples from puffer fish \u003Ci>Takifugu rubripes\u003C\u002Fi> exposed to excessive fluoride: An insight into molecular response to 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YR, 1996, The role of c‐Jun N‐terminal kinase (JNK) in apoptosis induced by ultraviolet C and radiation, J Bio Chem, 271, 31929, 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full‐length cDNAs encoding glutathione \u003Cjats:italic>S\u003C\u002Fjats:italic>‐transferase (GST) were cloned and sequenced from the hepatopancreas of planktivorous silver carp (\u003Cjats:italic>Hypophthalmichthys molitrix\u003C\u002Fjats:italic>) and bighead carp (\u003Cjats:italic>Aristichthys nobilis\u003C\u002Fjats:italic>). The silver carp and bighead carp GST cDNA were 920 and 978 bp in length, respectively, and both contained an open reading frame that encoding 223 amino acids. Partial GST cDNA sequences were also obtained from the liver of grass carp (\u003Cjats:italic>Ctenopharyngodon idellus\u003C\u002Fjats:italic>), crucian carp (\u003Cjats:italic>Carassius auratu\u003C\u002Fjats:italic>), mud carp (\u003Cjats:italic>Cirrhinus molitorella\u003C\u002Fjats:italic>), and tilapia (\u003Cjats:italic>Oreochromis nilotica\u003C\u002Fjats:italic>). All these GSTs could be classified as alpha‐class GSTs on the basis of their amino acid sequence identity with other species. The three‐dimensional structure of the silver carp GST was predicted using a computer program, and was found to fit the classical two‐domain GST structure. Using the genome walker method, a 875‐bp 5′‐flanking region of the silver carp GST gene was obtained, and several lipopolysaccharide (LPS) response elements were identified in the promoter region of the phytoplanktivorous fish GST gene, indicating that the GST gene expression of this fish might be regulated by LPS, released from the toxic blue‐green algae producing microcystins. To compare the constitutive expression level of the liver GST gene among the six freshwater fishes with completely different tolerance to microcystins, beta‐actin was used as control and the ratio GST\u002Fbeta‐actin mRNA (%) was determined as 130.7 ± 6.6 (grass carp), 103.1 ± 8.9 (bighead carp), 92.6 ± 15.0 (crucian carp), 72.3 ± 7.8 (mud carp), 58.8 ± 11.5 (silver carp), and 33.6 ± 13.7 (tilapia). The constitutive expression level of the liver GST gene clearly shows that all the six freshwater fishes had a negative relationship with their tolerance to microcystins: high‐resistant fishes (phytoplanktivorous silver carp and tilapia) had the lowest tolerance to microcystins and the high‐sensitive fish (herbivorous grass carp) had the highest tolerance to microcystins. Taken together with the reciprocal relationship of constitutive and inducible liver GST expression level in some of the tested fish species to microcystin exposure, a molecular mechanism for different microcystin detoxification abilities of the warm freshwater fishes was discussed. © 2006 Wiley Periodicals, Inc. J Biochem Mol Toxicol 20:114–126, 2006; Published online in Wiley InterScience (\u003Cjats:ext-link xmlns:xlink=\"http:\u002F\u002Fwww.w3.org\u002F1999\u002Fxlink\" xlink:href=\"http:\u002F\u002Fwww.interscience.wiley.com\">www.interscience.wiley.com\u003C\u002Fjats:ext-link>). DOI 10.1002\u002Fjbt.20125\u003C\u002Fjats:p>",{"EN":2679},"Molecular cloning and characterization of alpha‐class glutathione \u003Ci>S\u003C\u002Fi>‐transferase gene from the liver of silver carp, bighead carp, and other major chinese freshwater 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