Redox proteomic identification of HNE-bound mitochondrial proteins in cardiac tissues reveals a systemic effect on energy metabolism after doxorubicin treatment
Doxorubicin (DOX), one of the most effective anticancer drugs, is known to generate progressive cardiac damage, which is due, in part, to DOX-induced reactive oxygen species (ROS). The elevated ROS often induce oxidative protein modifications that result in alteration of protein functions. This stud...
Saved in:
Published in | Free radical biology & medicine Vol. 72; pp. 55 - 65 |
---|---|
Main Authors | , , , , , , , , , , , , , |
Format | Journal Article |
Language | English |
Published |
United States
Elsevier Inc
01.07.2014
|
Subjects | |
Online Access | Get full text |
Cover
Loading…
Abstract | Doxorubicin (DOX), one of the most effective anticancer drugs, is known to generate progressive cardiac damage, which is due, in part, to DOX-induced reactive oxygen species (ROS). The elevated ROS often induce oxidative protein modifications that result in alteration of protein functions. This study demonstrates that the level of proteins adducted by 4-hydroxy-2-nonenal (HNE), a lipid peroxidation product, is significantly increased in mouse heart mitochondria after DOX treatment. A redox proteomics method involving two-dimensional electrophoresis followed by mass spectrometry and investigation of protein databases identified several HNE-modified mitochondrial proteins, which were verified by HNE-specific immunoprecipitation in cardiac mitochondria from the DOX-treated mice. The majority of the identified proteins are related to mitochondrial energy metabolism. These include proteins in the citric acid cycle and electron transport chain. The enzymatic activities of the HNE-adducted proteins were significantly reduced in DOX-treated mice. Consistent with the decline in the function of the HNE-adducted proteins, the respiratory function of cardiac mitochondria as determined by oxygen consumption rate was also significantly reduced after DOX treatment. Treatment with Mn(III) meso-tetrakis(N-n-butoxyethylpyridinium-2-yl)porphyrin, an SOD mimic, averted the doxorubicin-induced mitochondrial dysfunctions as well as the HNE–protein adductions. Together, the results demonstrate that free radical-mediated alteration of energy metabolism is an important mechanism mediating DOX-induced cardiac injury, suggesting that metabolic intervention may represent a novel approach to preventing cardiac injury after chemotherapy.
•Doxorubicin increased total HNE-adducted proteins in cardiac mitochondria.•Redox proteomics identified several HNE-targeted cardiac mitochondria proteins important for energy metabolism.•Doxorubicin reduced the activities of complex I, SDHA, ATP synthase, and DLD in ETC.•MnP averted doxorubicin-induced mitochondrial dysfunction and HNE adductions. |
---|---|
AbstractList | Doxorubicin (DOX), one of the most effective anticancer drugs, is known to generate progressive cardiac damage, which is due, in part, to DOX-induced reactive oxygen species (ROS). The elevated ROS often induce oxidative protein modifications that result in alteration of protein functions. This study demonstrates that the level of proteins adducted by 4-hydroxy-2-nonenal (HNE), a lipid peroxidation product, is significantly increased in mouse heart mitochondria after DOX treatment. A redox proteomics method involving two-dimensional electrophoresis followed by mass spectrometry and investigation of protein databases identified several HNE-modified mitochondrial proteins, which were verified by HNE-specific immunoprecipitation in cardiac mitochondria from the DOX-treated mice. The majority of the identified proteins are related to mitochondrial energy metabolism. These include proteins in the citric acid cycle and electron transport chain. The enzymatic activities of the HNE-adducted proteins were significantly reduced in DOX-treated mice. Consistent with the decline in the function of the HNE-adducted proteins, the respiratory function of cardiac mitochondria as determined by oxygen consumption rate was also significantly reduced after DOX treatment. Treatment with Mn(III) meso-tetrakis(N-n-butoxyethylpyridinium-2-yl)porphyrin, an SOD mimic, averted the doxorubicin-induced mitochondrial dysfunctions as well as the HNE-protein adductions. Together, the results demonstrate that free radical-mediated alteration of energy metabolism is an important mechanism mediating DOX-induced cardiac injury, suggesting that metabolic intervention may represent a novel approach to preventing cardiac injury after chemotherapy. Doxorubicin (DOX), one of the most effective anticancer drugs, is known to generate progressive cardiac damage, which is due, in part, to DOX-induced reactive oxygen species (ROS). The elevated ROS often induce oxidative protein modifications that result in alteration of protein functions. This study demonstrates that the level of proteins adducted by 4-hydroxy-2-nonenal (HNE), a lipid peroxidation product, is significantly increased in mouse heart mitochondria following DOX treatment. A redox proteomics method involving 2D electrophoresis followed by mass spectrometry and investigation of protein data bases identified several HNE-modified mitochondria proteins, which were verified by HNE-specific immunoprecipitation in cardiac mitochondria from the DOX-treated mice. The majority of the identified proteins are related to mitochondrial energy metabolism. These include proteins in the citric acid cycle (TCA) and electron transport chain (ETC). The enzymatic activities of the HNE-adducted proteins were significantly reduced in DOX-treated mice. Consistent with the decline in the function of the HNE adducted proteins, the respiratory function of cardiac mitochondria as determined by oxygen consumption rate (OCR) was also significantly reduced after DOX treatment. The treatment with Mn(III) meso-tetrakis( N -n-butoxyethylpyridinium-2-yl)porphyrin, MnP, an SOD mimic, averted the doxorubicin-induced mitochondrial dysfunctions as well as the HNE protein adductions. Together, the results demonstrate that free radical-mediated alteration of energy metabolism is an important mechanism mediating DOX-induced cardiac injury suggesting that metabolic intervention may represent a novel approach to preventing cardiac injury after chemotherapy. Doxorubicin (DOX), one of the most effective anticancer drugs, is known to generate progressive cardiac damage, which is due, in part, to DOX-induced reactive oxygen species (ROS). The elevated ROS often induce oxidative protein modifications that result in alteration of protein functions. This study demonstrates that the level of proteins adducted by 4-hydroxy-2-nonenal (HNE), a lipid peroxidation product, is significantly increased in mouse heart mitochondria after DOX treatment. A redox proteomics method involving two-dimensional electrophoresis followed by mass spectrometry and investigation of protein databases identified several HNE-modified mitochondrial proteins, which were verified by HNE-specific immunoprecipitation in cardiac mitochondria from the DOX-treated mice. The majority of the identified proteins are related to mitochondrial energy metabolism. These include proteins in the citric acid cycle and electron transport chain. The enzymatic activities of the HNE-adducted proteins were significantly reduced in DOX-treated mice. Consistent with the decline in the function of the HNE-adducted proteins, the respiratory function of cardiac mitochondria as determined by oxygen consumption rate was also significantly reduced after DOX treatment. Treatment with Mn(III) meso-tetrakis(N-n-butoxyethylpyridinium-2-yl)porphyrin, an SOD mimic, averted the doxorubicin-induced mitochondrial dysfunctions as well as the HNE–protein adductions. Together, the results demonstrate that free radical-mediated alteration of energy metabolism is an important mechanism mediating DOX-induced cardiac injury, suggesting that metabolic intervention may represent a novel approach to preventing cardiac injury after chemotherapy. •Doxorubicin increased total HNE-adducted proteins in cardiac mitochondria.•Redox proteomics identified several HNE-targeted cardiac mitochondria proteins important for energy metabolism.•Doxorubicin reduced the activities of complex I, SDHA, ATP synthase, and DLD in ETC.•MnP averted doxorubicin-induced mitochondrial dysfunction and HNE adductions. |
Author | Cai, J. Sultana, R. Dhar, S.K. Vore, M. Batinic-Haberle, I. Zhao, Y. Schnell, D. St. Clair, D.K. Klein, J.B. Mitov, M. Butterfield, D.A. Miriyala, S. Bondada, S. Miao, L. |
AuthorAffiliation | 6 Department of Immunology, University of Kentucky, Lexington, Kentucky 1 Graduate Center for Toxicology, University of Kentucky, Lexington, Kentucky 2 Department of Cellular Biology and Anatomy, Louisiana State UniversityHealth Sciences,Shreveport, Louisiana 7 Department of Radiation Oncology, Duke University School of Medicine, Durham, North Carolina 5 Department of Chemistry, Center of Membrane Sciences, and Sanders-Brown Center on Aging, University of Kentucky, Lexington, Kentucky 3 Free Radical Biology in Cancer Shared Resource Facility, Markey Cancer Center, University of Kentucky, Lexington, Kentucky 4 Department of Nephrology and Proteomics Facility, University of Louisville, Louisville, Kentucky |
AuthorAffiliation_xml | – name: 3 Free Radical Biology in Cancer Shared Resource Facility, Markey Cancer Center, University of Kentucky, Lexington, Kentucky – name: 5 Department of Chemistry, Center of Membrane Sciences, and Sanders-Brown Center on Aging, University of Kentucky, Lexington, Kentucky – name: 7 Department of Radiation Oncology, Duke University School of Medicine, Durham, North Carolina – name: 4 Department of Nephrology and Proteomics Facility, University of Louisville, Louisville, Kentucky – name: 2 Department of Cellular Biology and Anatomy, Louisiana State UniversityHealth Sciences,Shreveport, Louisiana – name: 6 Department of Immunology, University of Kentucky, Lexington, Kentucky – name: 1 Graduate Center for Toxicology, University of Kentucky, Lexington, Kentucky |
Author_xml | – sequence: 1 givenname: Y. surname: Zhao fullname: Zhao, Y. organization: Graduate Center for Toxicology, University of Kentucky, Lexington, KY 40506, USA – sequence: 2 givenname: S. surname: Miriyala fullname: Miriyala, S. organization: Graduate Center for Toxicology, University of Kentucky, Lexington, KY 40506, USA – sequence: 3 givenname: L. surname: Miao fullname: Miao, L. organization: Graduate Center for Toxicology, University of Kentucky, Lexington, KY 40506, USA – sequence: 4 givenname: M. surname: Mitov fullname: Mitov, M. organization: Free Radical Biology in Cancer Shared Resource Facility, Markey Cancer Center, University of Kentucky, Lexington, KY 40506, USA – sequence: 5 givenname: D. surname: Schnell fullname: Schnell, D. organization: Graduate Center for Toxicology, University of Kentucky, Lexington, KY 40506, USA – sequence: 6 givenname: S.K. surname: Dhar fullname: Dhar, S.K. organization: Graduate Center for Toxicology, University of Kentucky, Lexington, KY 40506, USA – sequence: 7 givenname: J. surname: Cai fullname: Cai, J. organization: Department of Nephrology and Proteomics Facility, University of Louisville, Louisville, KY 40292, USA – sequence: 8 givenname: J.B. surname: Klein fullname: Klein, J.B. organization: Department of Nephrology and Proteomics Facility, University of Louisville, Louisville, KY 40292, USA – sequence: 9 givenname: R. surname: Sultana fullname: Sultana, R. organization: Department of Chemistry, Center of Membrane Sciences, and Sanders-Brown Center on Aging, University of Kentucky, Lexington, KY 40506, USA – sequence: 10 givenname: D.A. surname: Butterfield fullname: Butterfield, D.A. organization: Free Radical Biology in Cancer Shared Resource Facility, Markey Cancer Center, University of Kentucky, Lexington, KY 40506, USA – sequence: 11 givenname: M. surname: Vore fullname: Vore, M. organization: Graduate Center for Toxicology, University of Kentucky, Lexington, KY 40506, USA – sequence: 12 givenname: I. surname: Batinic-Haberle fullname: Batinic-Haberle, I. organization: Department of Radiation Oncology, Duke University School of Medicine, Durham, NC 27710, USA – sequence: 13 givenname: S. surname: Bondada fullname: Bondada, S. organization: Department of Immunology, University of Kentucky, Lexington, KY 40506, USA – sequence: 14 givenname: D.K. surname: St. Clair fullname: St. Clair, D.K. email: dstcl00@uky.edu organization: Graduate Center for Toxicology, University of Kentucky, Lexington, KY 40506, USA |
BackLink | https://www.ncbi.nlm.nih.gov/pubmed/24632380$$D View this record in MEDLINE/PubMed |
BookMark | eNqNUdFqFDEUDVKx7eovSMAXX2ZNJpOZLIIgZbVCURB9Dpnkpr3LTLIm2aX7N36qWbYW--ZDuJB77jmHcy7JWYgBCHnD2ZIz3r_bLH0CSMaNGGdwy5bxbsnEkjH-jFxwNYimk6v-jFwwteKNVN3qnFzmvGGMdVKoF-S87XrRCsUuyO_v4OI93aZYIM5oKToIBT1aUzAGGj29_rpuxrgLjs5Yor2LwSU00-kGQ6YYqDXJobG0YM47yDTBHsyUqaH5kAscicF7sIVWTgiQbg90hmLGOGGeqfEFEq1GYtqNaCthSWDKXK28JM99ZYJXD3NBfn5a_7i6bm6-ff5y9fGmsXLFStOqVjIwvXCt6oxv-95Y3jnTKjus2GhAMqXqL3RQxyDd2A7SCw6-94MyTizIhxPvdjfWVG2VTmbS24SzSQcdDeqnm4B3-jbudcekkPUtyNsHghR_1QyKnjFbmCYTIO6y5r0aeiUFbyv0_QlqU8w5gX-U4UwfO9Yb_aRjfexYM6Frx_X69b9OH2__lloB6xMAal57hKSzRQgWHKZagXYR_0voDz3Qx6k |
CitedBy_id | crossref_primary_10_1016_j_preteyeres_2021_100941 crossref_primary_10_1016_j_freeradbiomed_2020_10_303 crossref_primary_10_1016_j_jep_2016_05_020 crossref_primary_10_1161_CIRCULATIONAHA_120_045470 crossref_primary_10_1186_s13075_018_1592_1 crossref_primary_10_1021_acschembio_7b00480 crossref_primary_10_1155_2020_3598715 crossref_primary_10_1089_ars_2019_7955 crossref_primary_10_1016_j_yexcr_2017_03_004 crossref_primary_10_3390_antiox11061194 crossref_primary_10_3390_antiox12040856 crossref_primary_10_1016_j_cbi_2022_110028 crossref_primary_10_1089_ars_2020_8122 crossref_primary_10_3389_fphys_2015_00098 crossref_primary_10_1038_s41418_019_0470_y crossref_primary_10_1530_REP_22_0126 crossref_primary_10_1089_ars_2015_6362 crossref_primary_10_1016_j_redox_2019_101237 crossref_primary_10_1016_j_ab_2017_03_024 crossref_primary_10_1016_j_freeradbiomed_2019_11_023 crossref_primary_10_1021_acs_chemrev_7b00698 crossref_primary_10_1016_j_taap_2016_02_003 crossref_primary_10_1152_ajpheart_00554_2015 crossref_primary_10_1371_journal_pone_0181632 crossref_primary_10_3390_ijms241814013 crossref_primary_10_1016_j_tox_2021_152852 crossref_primary_10_3390_plants10071451 crossref_primary_10_1016_j_cclet_2019_03_029 crossref_primary_10_1016_j_fct_2018_06_010 crossref_primary_10_1016_j_fct_2018_12_017 crossref_primary_10_1016_j_freeradbiomed_2016_10_494 crossref_primary_10_1194_jlr_R066597 crossref_primary_10_1002_pmic_201400164 crossref_primary_10_3390_biom5042247 crossref_primary_10_1016_j_freeradbiomed_2017_04_363 crossref_primary_10_1071_RD22219 crossref_primary_10_1016_j_redox_2016_12_028 crossref_primary_10_1016_j_redox_2020_101740 crossref_primary_10_1016_j_redox_2017_05_018 crossref_primary_10_3389_fcell_2022_850145 crossref_primary_10_1016_j_bbagen_2019_129487 crossref_primary_10_1089_ars_2017_7485 crossref_primary_10_1002_cam4_6806 crossref_primary_10_1016_j_bbadis_2017_07_030 crossref_primary_10_1016_j_redox_2017_02_005 crossref_primary_10_3390_antiox5010007 crossref_primary_10_1016_j_ejphar_2021_173955 crossref_primary_10_1007_s10815_020_01707_8 crossref_primary_10_1038_s41467_023_41570_6 crossref_primary_10_5352_JLS_2016_26_2_226 crossref_primary_10_1016_j_bbrc_2016_06_113 crossref_primary_10_1007_s00204_016_1759_y crossref_primary_10_1021_ic501329p crossref_primary_10_1371_journal_pone_0126278 crossref_primary_10_1002_jcsm_12794 crossref_primary_10_1021_ac504685y crossref_primary_10_1016_j_redox_2014_12_011 crossref_primary_10_15436_2381_0793_15_013 crossref_primary_10_3109_10715762_2014_960865 crossref_primary_10_1080_13880209_2016_1266672 crossref_primary_10_1177_1074248416686189 crossref_primary_10_1002_pmic_201500317 crossref_primary_10_1016_j_toxlet_2019_01_003 crossref_primary_10_1016_j_freeradbiomed_2015_10_416 crossref_primary_10_1016_j_redox_2014_09_003 crossref_primary_10_1016_j_biopha_2018_09_171 crossref_primary_10_3390_brainsci14010022 crossref_primary_10_1089_ars_2021_0177 crossref_primary_10_1158_1078_0432_CCR_17_2046 crossref_primary_10_1016_j_freeradbiomed_2018_08_020 crossref_primary_10_1155_2020_5347204 crossref_primary_10_1016_j_cbi_2019_03_027 crossref_primary_10_1038_s41598_024_51675_7 crossref_primary_10_1038_s41598_017_18701_3 crossref_primary_10_3390_toxics7020032 crossref_primary_10_1080_10715762_2021_1876856 crossref_primary_10_3390_antiox11020306 crossref_primary_10_3390_biom12111555 crossref_primary_10_1016_j_freeradbiomed_2015_05_028 crossref_primary_10_1007_s12012_022_09721_1 crossref_primary_10_1161_RES_0000000000000097 crossref_primary_10_1016_j_yjmcc_2018_04_002 crossref_primary_10_29254_2077_4214_2019_1_1_148_375_380 crossref_primary_10_1016_j_metabol_2022_155250 |
Cites_doi | 10.1016/j.nbd.2007.12.007 10.1016/S0891-5849(00)00194-5 10.1016/S0925-4439(02)00144-8 10.1016/S0008-6363(00)00307-2 10.1161/01.HYP.15.3.237 10.1038/clpt.1993.69 10.1097/FPC.0b013e32833ffb56 10.1074/jbc.R700019200 10.1002/path.1863 10.1042/BJ20090934 10.1042/bj2590181 10.1038/nm.2919 10.1089/ars.2011.4406 10.1007/s00280-010-1441-7 10.1002/jbt.2570040204 10.1016/0301-4622(90)80012-V 10.3109/10715762.2012.752078 10.1006/bbrc.1993.2135 10.1021/tx015532n 10.1172/JCI118909 10.1074/jbc.M112.366690 10.1016/j.freeradbiomed.2013.06.017 10.2174/092986709788186228 10.1016/S0006-2952(98)00307-4 10.1038/ncomms2921 10.1093/jnci/55.1.191 10.1016/S0021-9258(17)35746-0 10.1016/j.bbadis.2011.12.002 10.1161/01.RES.56.3.377 10.1042/BJ20081615 10.1200/JCO.2007.14.9401 10.1038/ejhg.2010.83 10.1371/journal.pone.0018005 10.1016/j.cbi.2010.12.002 10.1021/tx960133r 10.1124/mi.7.3.6 10.1152/ajpheart.01073.2011 10.1016/j.freeradbiomed.2012.02.006 10.1096/fasebj.12.7.541 10.1089/ars.2012.5147 10.1002/med.21280 10.3109/10715769609088013 10.3727/096504003108748294 10.1016/j.jprot.2011.07.009 10.1016/0005-2728(87)90236-2 10.1007/s10565-006-0140-y 10.1074/jbc.M306285200 10.1006/jmcc.2001.1454 10.1042/bj0800649 10.1016/0022-2828(79)90377-8 10.1073/pnas.85.10.3585 10.1159/000265166 10.1016/j.freeradbiomed.2008.06.006 10.1016/j.freeradbiomed.2005.10.040 10.1056/NEJM199809243391307 10.1124/pr.56.2.6 10.1158/1535-7163.MCT-06-0297 10.1002/1097-0142(197308)32:2<302::AID-CNCR2820320205>3.0.CO;2-2 10.1158/0008-5472.CAN-09-4572 10.1016/j.jmb.2005.05.014 10.18388/abp.2003_3689 10.1080/01926230490502601 10.1016/j.freeradbiomed.2006.08.006 10.1152/ajplung.00337.2005 10.1002/1531-8249(20010201)49:2<195::AID-ANA39>3.0.CO;2-M |
ContentType | Journal Article |
Copyright | 2014 Elsevier Inc. Copyright © 2014 Elsevier Inc. All rights reserved. 2014 Elsevier Inc. All rights reserved. 2014 |
Copyright_xml | – notice: 2014 Elsevier Inc. – notice: Copyright © 2014 Elsevier Inc. All rights reserved. – notice: 2014 Elsevier Inc. All rights reserved. 2014 |
DBID | CGR CUY CVF ECM EIF NPM AAYXX CITATION 7U7 C1K 5PM |
DOI | 10.1016/j.freeradbiomed.2014.03.001 |
DatabaseName | Medline MEDLINE MEDLINE (Ovid) MEDLINE MEDLINE PubMed CrossRef Toxicology Abstracts Environmental Sciences and Pollution Management PubMed Central (Full Participant titles) |
DatabaseTitle | MEDLINE Medline Complete MEDLINE with Full Text PubMed MEDLINE (Ovid) CrossRef Toxicology Abstracts Environmental Sciences and Pollution Management |
DatabaseTitleList | Toxicology Abstracts MEDLINE |
Database_xml | – sequence: 1 dbid: NPM name: PubMed url: https://proxy.k.utb.cz/login?url=http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=PubMed sourceTypes: Index Database – sequence: 2 dbid: EIF name: MEDLINE url: https://proxy.k.utb.cz/login?url=https://www.webofscience.com/wos/medline/basic-search sourceTypes: Index Database |
DeliveryMethod | fulltext_linktorsrc |
Discipline | Anatomy & Physiology Biology |
EISSN | 1873-4596 |
EndPage | 65 |
ExternalDocumentID | 10_1016_j_freeradbiomed_2014_03_001 24632380 S0891584914001075 |
Genre | Research Support, Non-U.S. Gov't Journal Article Research Support, N.I.H., Extramural |
GrantInformation_xml | – fundername: NCI NIH HHS grantid: P30 CA177558 – fundername: NIGMS NIH HHS grantid: P20 GM103527 – fundername: NCI NIH HHS grantid: CA049797 – fundername: NCI NIH HHS grantid: R01 CA080152 – fundername: NCI NIH HHS grantid: R01 CA049797 – fundername: NCI NIH HHS grantid: CA 139843 – fundername: NIDDK NIH HHS grantid: T32 DK007778 – fundername: NCI NIH HHS grantid: P30CA177558 |
GroupedDBID | --- --K --M -~X .GJ .HR .~1 0R~ 1B1 1RT 1~. 1~5 29H 4.4 457 4G. 53G 5GY 5VS 7-5 71M 8P~ 9JM AABNK AACTN AAEDT AAEDW AAIAV AAIKJ AAKOC AALRI AAOAW AAQFI AAQXK AAXUO ABBQC ABFNM ABFRF ABGSF ABJNI ABLJU ABLVK ABMAC ABMZM ABUDA ABXDB ABYKQ ACDAQ ACGFO ACGFS ACIUM ACRLP ADBBV ADEZE ADMUD ADUVX AEBSH AEFWE AEHWI AEKER AENEX AFKWA AFTJW AFXIZ AGHFR AGRDE AGUBO AGYEJ AHHHB AIEXJ AIKHN AITUG AJBFU AJOXV AJRQY ALMA_UNASSIGNED_HOLDINGS AMFUW AMRAJ ANZVX ASPBG AVWKF AXJTR AZFZN BKOJK BLXMC BNPGV C45 CS3 DOVZS DU5 EBS EFJIC EFLBG EJD EO8 EO9 EP2 EP3 F5P FDB FEDTE FGOYB FIRID FNPLU FYGXN G-2 G-Q GBLVA HEA HLW HMK HMO HVGLF HX~ HZ~ IHE J1W KOM LCYCR LX3 LZ2 M29 M41 MO0 N9A O-L O9- OAUVE OVD OZT P-8 P-9 P2P PC. Q38 R2- RIG ROL RPZ SAE SBG SCC SDF SDG SDP SES SEW SPCBC SSH SSU SSZ T5K TEORI WUQ XPP ZGI ~G- AAXKI AFJKZ AKRWK CGR CUY CVF ECM EIF NPM AAYXX ACRPL ADNMO CITATION 7U7 C1K 5PM |
ID | FETCH-LOGICAL-c590t-28250ea63d284af266ac14da28c790bae5088266e4e82675db275f31ef6f78ad3 |
IEDL.DBID | AIKHN |
ISSN | 0891-5849 |
IngestDate | Tue Sep 17 20:38:46 EDT 2024 Fri Oct 25 21:32:58 EDT 2024 Fri Dec 06 01:10:23 EST 2024 Sat Nov 02 12:17:32 EDT 2024 Fri Feb 23 02:21:34 EST 2024 |
IsDoiOpenAccess | false |
IsOpenAccess | true |
IsPeerReviewed | true |
IsScholarly | true |
Keywords | Oxidative stress FH Doxorubicin CKMT2 ATP5B ATP synthase Succinate dehydrogenase [ubiquinone] flavoprotein Free radicals Cardiac injury TCA cycle Oxct1 Dihydrolipoyl dehydrogenase DOX SDHA Metabolism MnP ECAR HADHA NAC Redox proteomics NADH dehydrogenase [ubiquinone] iron–sulfur protein 2 ETC ROS NDUFS2 DLD HNE OCR |
Language | English |
License | Copyright © 2014 Elsevier Inc. All rights reserved. |
LinkModel | DirectLink |
MergedId | FETCHMERGED-LOGICAL-c590t-28250ea63d284af266ac14da28c790bae5088266e4e82675db275f31ef6f78ad3 |
Notes | ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 |
OpenAccessLink | https://uknowledge.uky.edu/cgi/viewcontent.cgi?article=1073&context=toxicology_facpub |
PMID | 24632380 |
PQID | 1687685312 |
PQPubID | 23462 |
PageCount | 11 |
ParticipantIDs | pubmedcentral_primary_oai_pubmedcentral_nih_gov_4053505 proquest_miscellaneous_1687685312 crossref_primary_10_1016_j_freeradbiomed_2014_03_001 pubmed_primary_24632380 elsevier_sciencedirect_doi_10_1016_j_freeradbiomed_2014_03_001 |
PublicationCentury | 2000 |
PublicationDate | 2014-07-01 |
PublicationDateYYYYMMDD | 2014-07-01 |
PublicationDate_xml | – month: 07 year: 2014 text: 2014-07-01 day: 01 |
PublicationDecade | 2010 |
PublicationPlace | United States |
PublicationPlace_xml | – name: United States |
PublicationTitle | Free radical biology & medicine |
PublicationTitleAlternate | Free Radic Biol Med |
PublicationYear | 2014 |
Publisher | Elsevier Inc |
Publisher_xml | – name: Elsevier Inc |
References | Berthiaume, Wallace (bib14) 2007 Yang, Sharma, Sharma, Awasthi, Awasthi (bib7) 2003 Olson, Mushlin, Brenner, Fleischer, Cusack, Chang, Boucek (bib62) 1988 Yen, Oberley, Vichitbandha, Ho, St Clair (bib45) 1996 Zhou, O׳Rourke (bib11) 2012 Minotti, Menna, Salvatorelli, Cairo, Gianni (bib39) 2004 Reed, Perluigi, Sultana, Pierce, Klein, Turner, Coccia, Markesbery, Butterfield (bib20) 2008 Loeffen, Elpeleg, Smeitink, Smeets, Stockler-Ipsiroglu, Mandel, Sengers, Trijbels, van den Heuvel (bib55) 2001 Perluigi, Coccia, Butterfield (bib10) 2012 Takiyyuddin, Cervenka, Hsiao, Barbosa, Parmer, O׳Connor (bib26) 1990 Goormaghtigh, Huart, Praet, Brasseur, Ruysschaert (bib12) 1990 Gianni, Herman, Lipshultz, Minotti, Sarvazyan, Sawyer (bib40) 2008 Choksi, Nuss, Deford, Papaconstantinou (bib54) 2008 van Dalen, Caron, Dickinson, Kremer (bib69) 2011; 6 Bloodsworth, O׳Donnell, Batinic-Haberle, Chumley, Hurt, Day, Crow, Freeman (bib70) 2000 Batinic-Haberle, I.; Tovmasyan, A.; Roberts, E.R.; Vujaskovic, Z.; Leong, K.W.; Spasojevic I. SOD therapeutics: latest insights into their structure–activity relationships and impact on the cellular redox-based signaling pathways Hussain, Matar, Barreiro, Florian, Divangahi, Vassilakopoulos (bib29) 2006 Chen, Jungsuwadee, Vore, Butterfield, St Clair (bib66) 2007 Carvalho, Burgeiro, Garcia, Moreno, Carvalho, Oliveira (bib16) 2014 Brautigam, Chuang, Tomchick, Machius, Chuang (bib64) 2005 Aitken, Whiting, De Iuliis, McClymont, Mitchell, Baker (bib52) 2012 Barret, Barman, Boitano, Brooks (bib28) 2005 Lebrecht, Kokkori, Ketelsen, Setzer, Walker (bib59) 2005 Miriyala, Spasojevic, Tovmasyan, Salvemini, Vujaskovic, St Clair, Batinic-Haberle (bib36) 2012 Piscitelli, Rodvold, Rushing, Tewksbury (bib42) 1993 Nicolay, de Kruijff (bib58) 1987 al-Shabanah, Badary, Nagi, al-Gharably, al-Rikabi, al-Bekairi (bib9) 1998 Fiorini, Sultana, Forster, Perluigi, Cenini, Cini, Cai, Klein, Farr, Niehoff, Morley, Kumar, Allan Butterfield (bib22) 2013 Guo, Prokai-Tatrai, Nguyen, Rauniyar, Ughy, Prokai (bib53) 2011 Mihm, Coyle, Schanbacher, Weinstein, Bauer (bib31) 2001 Davies, Doroshow (bib13) 1986 , Stadtman, Berlett (bib6) 1997 Rosenoff, Olson, Young, Bostick, Young (bib43) 1975 Porta, Joun, Matsumura, Nakasone, Sablan (bib8) 1983 Marcillat, Zhang, Davies (bib4) 1989 Robison, Giri, Wilson (bib30) 1989 Pang, Qiao, Janssen, Velds, Groothuis, Kerkhoven, Nieuwland, Ovaa, Rottenberg, van Tellingen, Janssen, Huijgens, Zwart, Neefjes (bib1) 2013 Adachi, Fujiura, Mayumi, Nozuhara, Sugiu, Sakanashi, Hidaka, Toshima (bib35) 1993 Hill, Dranka, Zou, Chatham, Darley-Usmar (bib41) 2009 Chen, Daosukho, Opii, Turner, Pierce, Klein, Vore, Butterfield, St Clair (bib23) 2006 Zhang, Liu, Bawa-Khalfe, Lu, Lyu, Liu, Yeh (bib68) 2012 Singal, Iliskovic (bib3) 1998 Pennington (bib25) 1961 Minotti, Recalcati, Mordente, Liberi, Calafiore, Mancuso, Preziosi, Cairo (bib5) 1998 Rajic, Tovmasyan, Spasojevic, Sheng, Lu, Li, Gralla, Warner, Benov, Batinic-Haberle (bib34) 2012 Chatterjee, Zhang, Honbo, Karliner (bib2) 2010 in press Green, Leeuwenburgh (bib18) 2002 Yan, Sumien, Thangthaeng, Forster (bib24) 2013 Hill, Awe, Vladykovskaya, Ahmed, Liu, Bhatnagar, Srivastava (bib48) 2009 Jungsuwadee, Cole, Sultana, Joshi, Tangpong, Butterfield, St Clair, Vore (bib21) 2006 Thorn, Oshiro, Marsh, Hernandez-Boussard, McLeod, Klein, Altman (bib56) 2011 Smith, Stone, Darley-Usmar (bib65) 1996 Lefrak, Pitha, Rosenheim, Gottlieb (bib17) 1973 Pawlowska, Tarasiuk, Wolf, Paine, Borowski (bib57) 2003 Mordente, Meucci, Silvestrini, Martorana, Giardina (bib63) 2009 Levitas, Muhammad, Harel, Saada, Caspi, Manor, Beck, Sheffield, Parvari (bib61) 2010 Grimsrud, Xie, Griffin, Bernlohr (bib15) 2008 Velez, Miriyala, Nithipongvanitch, Noel, Plabplueng, Oberley, Jungsuwadee, Van Remmen, Vore, St Clair (bib19) 2011 Schaper, Meiser, Stammler (bib47) 1985 Bugger, Guzman, Zechner, Palmeri, Russell, Russell (bib33) 2011 Sun, St Clair, Xu, Crooks, St Clair (bib27) 2010 Benderdour, Charron, DeBlois, Comte, Des Rosiers (bib50) 2003 Sansbury, Jones, Riggs, Darley-Usmar, Hill (bib32) 2011 Lashin, Szweda, Szweda, Romani (bib60) 2006 Eaton, Li, Hearse, Shattock (bib49) 1999 Chaiswing, Cole, St Clair, Ittarat, Szweda, Oberley (bib44) 2004 David, Meyer, Marx, Guski, Wenzelides (bib46) 1979 Chen, Henderson, Freeman (bib51) 2001 Gewirtz (bib38) 1999 Kang, Sun, Chen, Zhou (bib67) 2002 Chen (10.1016/j.freeradbiomed.2014.03.001_bib51) 2001; 33 Lashin (10.1016/j.freeradbiomed.2014.03.001_bib60) 2006; 40 Minotti (10.1016/j.freeradbiomed.2014.03.001_bib39) 2004; 56 Stadtman (10.1016/j.freeradbiomed.2014.03.001_bib6) 1997; 10 Gianni (10.1016/j.freeradbiomed.2014.03.001_bib40) 2008; 26 Mihm (10.1016/j.freeradbiomed.2014.03.001_bib31) 2001; 49 Robison (10.1016/j.freeradbiomed.2014.03.001_bib30) 1989; 4 Adachi (10.1016/j.freeradbiomed.2014.03.001_bib35) 1993; 195 Sansbury (10.1016/j.freeradbiomed.2014.03.001_bib32) 2011; 191 Piscitelli (10.1016/j.freeradbiomed.2014.03.001_bib42) 1993; 53 Carvalho (10.1016/j.freeradbiomed.2014.03.001_bib16) 2014; 34 Hussain (10.1016/j.freeradbiomed.2014.03.001_bib29) 2006; 290 Nicolay (10.1016/j.freeradbiomed.2014.03.001_bib58) 1987; 892 Aitken (10.1016/j.freeradbiomed.2014.03.001_bib52) 2012; 287 al-Shabanah (10.1016/j.freeradbiomed.2014.03.001_bib9) 1998; 17 Grimsrud (10.1016/j.freeradbiomed.2014.03.001_bib15) 2008; 283 Eaton (10.1016/j.freeradbiomed.2014.03.001_bib49) 1999; 276 Yan (10.1016/j.freeradbiomed.2014.03.001_bib24) 2013; 47 Chen (10.1016/j.freeradbiomed.2014.03.001_bib23) 2006; 41 Fiorini (10.1016/j.freeradbiomed.2014.03.001_bib22) 2013; 65C Rajic (10.1016/j.freeradbiomed.2014.03.001_bib34) 2012; 52 Kang (10.1016/j.freeradbiomed.2014.03.001_bib67) 2002; 15 Sun (10.1016/j.freeradbiomed.2014.03.001_bib27) 2010; 70 Reed (10.1016/j.freeradbiomed.2014.03.001_bib20) 2008; 30 Levitas (10.1016/j.freeradbiomed.2014.03.001_bib61) 2010; 18 Porta (10.1016/j.freeradbiomed.2014.03.001_bib8) 1983; 41 Olson (10.1016/j.freeradbiomed.2014.03.001_bib62) 1988; 85 Yang (10.1016/j.freeradbiomed.2014.03.001_bib7) 2003; 50 Zhou (10.1016/j.freeradbiomed.2014.03.001_bib11) 2012; 302 Bugger (10.1016/j.freeradbiomed.2014.03.001_bib33) 2011; 67 van Dalen (10.1016/j.freeradbiomed.2014.03.001_bib69) 2011; 6 Barret (10.1016/j.freeradbiomed.2014.03.001_bib28) 2005 Guo (10.1016/j.freeradbiomed.2014.03.001_bib53) 2011; 74 Chatterjee (10.1016/j.freeradbiomed.2014.03.001_bib2) 2010; 115 Pawlowska (10.1016/j.freeradbiomed.2014.03.001_bib57) 2003; 13 Lefrak (10.1016/j.freeradbiomed.2014.03.001_bib17) 1973; 32 Yen (10.1016/j.freeradbiomed.2014.03.001_bib45) 1996; 98 Pang (10.1016/j.freeradbiomed.2014.03.001_bib1) 2013; 4 Singal (10.1016/j.freeradbiomed.2014.03.001_bib3) 1998; 339 Choksi (10.1016/j.freeradbiomed.2014.03.001_bib54) 2008; 45 Minotti (10.1016/j.freeradbiomed.2014.03.001_bib5) 1998; 12 Zhang (10.1016/j.freeradbiomed.2014.03.001_bib68) 2012; 18 Chaiswing (10.1016/j.freeradbiomed.2014.03.001_bib44) 2004; 32 Lebrecht (10.1016/j.freeradbiomed.2014.03.001_bib59) 2005; 207 Davies (10.1016/j.freeradbiomed.2014.03.001_bib13) 1986; 261 Loeffen (10.1016/j.freeradbiomed.2014.03.001_bib55) 2001; 49 10.1016/j.freeradbiomed.2014.03.001_bib37 Smith (10.1016/j.freeradbiomed.2014.03.001_bib65) 1996; 24 Schaper (10.1016/j.freeradbiomed.2014.03.001_bib47) 1985; 56 Rosenoff (10.1016/j.freeradbiomed.2014.03.001_bib43) 1975; 55 Hill (10.1016/j.freeradbiomed.2014.03.001_bib41) 2009; 424 Pennington (10.1016/j.freeradbiomed.2014.03.001_bib25) 1961; 80 Green (10.1016/j.freeradbiomed.2014.03.001_bib18) 2002; 1588 Berthiaume (10.1016/j.freeradbiomed.2014.03.001_bib14) 2007; 23 Miriyala (10.1016/j.freeradbiomed.2014.03.001_bib36) 2012; 1822 Benderdour (10.1016/j.freeradbiomed.2014.03.001_bib50) 2003; 278 Mordente (10.1016/j.freeradbiomed.2014.03.001_bib63) 2009; 16 David (10.1016/j.freeradbiomed.2014.03.001_bib46) 1979; 11 Perluigi (10.1016/j.freeradbiomed.2014.03.001_bib10) 2012; 17 Velez (10.1016/j.freeradbiomed.2014.03.001_bib19) 2011; 6 Gewirtz (10.1016/j.freeradbiomed.2014.03.001_bib38) 1999; 57 Hill (10.1016/j.freeradbiomed.2014.03.001_bib48) 2009; 417 Chen (10.1016/j.freeradbiomed.2014.03.001_bib66) 2007; 7 Bloodsworth (10.1016/j.freeradbiomed.2014.03.001_bib70) 2000; 28 Marcillat (10.1016/j.freeradbiomed.2014.03.001_bib4) 1989; 259 Brautigam (10.1016/j.freeradbiomed.2014.03.001_bib64) 2005; 350 Thorn (10.1016/j.freeradbiomed.2014.03.001_bib56) 2011; 21 Jungsuwadee (10.1016/j.freeradbiomed.2014.03.001_bib21) 2006; 5 Goormaghtigh (10.1016/j.freeradbiomed.2014.03.001_bib12) 1990; 35 Takiyyuddin (10.1016/j.freeradbiomed.2014.03.001_bib26) 1990; 15 |
References_xml | – start-page: 155 year: 2010 end-page: 162 ident: bib2 article-title: Doxorubicin cardiomyopathy publication-title: Cardiology contributor: fullname: Karliner – start-page: 245 year: 2003 end-page: 252 ident: bib57 article-title: Differential ability of cytostatics from anthraquinone group to generate free radicals in three enzymatic systems: NADH dehydrogenase, NADPH cytochrome P450 reductase, and xanthine oxidase publication-title: Oncol. Res. contributor: fullname: Borowski – start-page: 320 year: 1987 end-page: 330 ident: bib58 article-title: Effects of adriamycin on respiratory chain activities in mitochondria from rat liver, rat heart and bovine heart: evidence for a preferential inhibition of complex III and IV publication-title: Biochim. Biophys. Acta contributor: fullname: de Kruijff – start-page: 195 year: 2001 end-page: 201 ident: bib55 article-title: Mutations in the complex I NDUFS2 gene of patients with cardiomyopathy and encephalomyopathy publication-title: Ann. Neurol. contributor: fullname: van den Heuvel – start-page: 945 year: 1993 end-page: 951 ident: bib35 article-title: A deletion of mitochondrial DNA in murine doxorubicin-induced cardiotoxicity publication-title: Biochem. Biophys. Res. Commun. contributor: fullname: Toshima – start-page: 1160 year: 2010 end-page: 1165 ident: bib61 article-title: Familial neonatal isolated cardiomyopathy caused by a mutation in the flavoprotein subunit of succinate dehydrogenase publication-title: Eur. J. Hum. Genet. contributor: fullname: Parvari – start-page: 107 year: 2008 end-page: 120 ident: bib20 article-title: Redox proteomic identification of 4-hydroxy-2-nonenal-modified brain proteins in amnestic mild cognitive impairment: insight into the role of lipid peroxidation in the progression and pathogenesis of Alzheimer׳s disease publication-title: Neurobiol. Dis. contributor: fullname: Butterfield – start-page: 1908 year: 2013 ident: bib1 article-title: Drug-induced histone eviction from open chromatin contributes to the chemotherapeutic effects of doxorubicin publication-title: Nat. Commun. contributor: fullname: Neefjes – start-page: 1639 year: 2012 end-page: 1642 ident: bib68 article-title: Identification of the molecular basis of doxorubicin-induced cardiotoxicity publication-title: Nat. Med. contributor: fullname: Yeh – start-page: 555 year: 1993 end-page: 561 ident: bib42 article-title: Pharmacokinetics and pharmacodynamics of doxorubicin in patients with small cell lung cancer publication-title: Clin. Pharmacol. Ther. contributor: fullname: Tewksbury – start-page: 1470 year: 2006 end-page: 1477 ident: bib23 article-title: Redox proteomic identification of oxidized cardiac proteins in adriamycin-treated mice publication-title: Free Radic. Biol. Med. contributor: fullname: St Clair – start-page: 123 year: 2013 end-page: 133 ident: bib24 article-title: Reversible inactivation of dihydrolipoamide dehydrogenase by mitochondrial hydrogen peroxide publication-title: Free Radic. Res. contributor: fullname: Forster – start-page: 377 year: 1985 end-page: 391 ident: bib47 article-title: Ultrastructural morphometric analysis of myocardium from dogs, rats, hamsters, mice, and from human hearts publication-title: Circ. Res. contributor: fullname: Stammler – start-page: 319 year: 2003 end-page: 336 ident: bib7 article-title: Lipid peroxidation and cell cycle signaling: 4-hydroxynonenal, a key molecule in stress mediated signaling publication-title: Acta Biochim. Pol. contributor: fullname: Awasthi – start-page: 2880 year: 2010 end-page: 2890 ident: bib27 article-title: A NADPH oxidase-dependent redox signaling pathway mediates the selective radiosensitization effect of parthenolide in prostate cancer cells publication-title: Cancer Res. contributor: fullname: St Clair – start-page: 1381 year: 2011 end-page: 1388 ident: bib33 article-title: Uncoupling protein downregulation in doxorubicin-induced heart failure improves mitochondrial coupling but increases reactive oxygen species generation publication-title: Cancer Chemother. Pharmacol. contributor: fullname: Russell – start-page: 15 year: 2007 end-page: 25 ident: bib14 article-title: Adriamycin-induced oxidative mitochondrial cardiotoxicity publication-title: Cell Biol. Toxicol. contributor: fullname: Wallace – start-page: 798 year: 2001 end-page: 807 ident: bib31 article-title: Peroxynitrite induced nitration and inactivation of myofibrillar creatine kinase in experimental heart failure publication-title: Cardiovasc. Res. contributor: fullname: Bauer – start-page: 237 year: 1990 end-page: 246 ident: bib26 article-title: Chromogranin A: storage and release in hypertension publication-title: Hypertension contributor: fullname: O׳Connor – start-page: 3585 year: 1988 end-page: 3589 ident: bib62 article-title: Doxorubicin cardiotoxicity may be caused by its metabolite, doxorubicinol publication-title: Proc. Natl. Acad. Sci. USA contributor: fullname: Boucek – start-page: 1253 year: 1996 end-page: 1260 ident: bib45 article-title: The protective role of manganese superoxide dismutase against adriamycin-induced acute cardiac toxicity in transgenic mice publication-title: J. Clin. Invest. contributor: fullname: St Clair – start-page: 2851 year: 2006 end-page: 2860 ident: bib21 article-title: Increase in Mrp1 expression and 4-hydroxy-2-nonenal adduction in heart tissue of adriamycin-treated C57BL/6 mice publication-title: Mol. Cancer Ther. contributor: fullname: Vore – start-page: 1017 year: 2000 end-page: 1029 ident: bib70 article-title: Manganese–porphyrin reactions with lipids and lipoproteins publication-title: Free Radic. Biol. Med. contributor: fullname: Freeman – start-page: 1828 year: 2012 end-page: 1834 ident: bib34 article-title: A new SOD mimic, Mn(III) publication-title: Free Radic. Biol. Med. contributor: fullname: Batinic-Haberle – start-page: 1 year: 2002 end-page: 6 ident: bib67 article-title: Inhibition of doxorubicin chronic toxicity in catalase-overexpressing transgenic mouse hearts publication-title: Chem. Res. Toxicol. contributor: fullname: Zhou – start-page: 193 year: 1998 end-page: 198 ident: bib9 article-title: Thymoquinone protects against doxorubicin-induced cardiotoxicity without compromising its antitumor activity publication-title: J. Exp. Clin. Cancer Res. contributor: fullname: al-Bekairi – start-page: 513 year: 2009 end-page: 524 ident: bib48 article-title: Myocardial ischaemia inhibits mitochondrial metabolism of 4-hydroxy-trans-2-nonenal publication-title: Biochem. J. contributor: fullname: Srivastava – start-page: 727 year: 1999 end-page: 741 ident: bib38 article-title: A critical evaluation of the mechanisms of action proposed for the antitumor effects of the anthracycline antibiotics adriamycin and daunorubicin publication-title: Biochem. Pharmacol. contributor: fullname: Gewirtz – start-page: 440 year: 2011 end-page: 446 ident: bib56 article-title: Doxorubicin pathways: pharmacodynamics and adverse effects publication-title: Pharmacogenet. Genomics contributor: fullname: Altman – start-page: 106 year: 2014 end-page: 135 ident: bib16 article-title: Doxorubicin-induced cardiotoxicity: from bioenergetic failure and cell death to cardiomyopathy publication-title: Med. Res. Rev. contributor: fullname: Oliveira – start-page: H2178 year: 2012 end-page: H2189 ident: bib11 article-title: Cardiac mitochondrial network excitability: insights from computational analysis publication-title: Am. J. Physiol. Heart Circ. Physiol. contributor: fullname: O׳Rourke – start-page: 1919 year: 2001 end-page: 1927 ident: bib51 article-title: Role of 4-hydroxynonenal in modification of cytochrome c oxidase in ischemia/reperfused rat heart publication-title: J. Mol. Cell. Cardiol. contributor: fullname: Freeman – start-page: 247 year: 1990 end-page: 257 ident: bib12 article-title: Structure of the adriamycin–cardiolipin complex: role in mitochondrial toxicity publication-title: Biophys. Chem. contributor: fullname: Ruysschaert – start-page: 826 year: 2008 end-page: 838 ident: bib54 article-title: Age-related alterations in oxidatively damaged proteins of mouse skeletal muscle mitochondrial electron transport chain complexes publication-title: Free Radic. Biol. Med. contributor: fullname: Papaconstantinou – start-page: 1656 year: 2009 end-page: 1672 ident: bib63 article-title: New developments in anthracycline-induced cardiotoxicity publication-title: Curr. Med. Chem. contributor: fullname: Giardina – start-page: 21837 year: 2008 end-page: 21841 ident: bib15 article-title: Oxidative stress and covalent modification of protein with bioactive aldehydes publication-title: J. Biol. Chem. contributor: fullname: Bernlohr – start-page: 185 year: 2004 end-page: 229 ident: bib39 article-title: Anthracyclines: molecular advances and pharmacologic developments in antitumor activity and cardiotoxicity publication-title: Pharmacol. Rev. contributor: fullname: Gianni – start-page: 485 year: 1997 end-page: 494 ident: bib6 article-title: Reactive oxygen-mediated protein oxidation in aging and disease publication-title: Chem. Res. Toxicol. contributor: fullname: Berlett – start-page: H935 year: 1999 end-page: H943 ident: bib49 article-title: Formation of 4-hydroxy-2-nonenal-modified proteins in ischemic rat heart publication-title: Am. J. Physiol. contributor: fullname: Shattock – start-page: 288 year: 2011 end-page: 295 ident: bib32 article-title: Bioenergetic function in cardiovascular cells: the importance of the reserve capacity and its biological regulation publication-title: Chem. Biol. Interact. contributor: fullname: Hill – start-page: 147 year: 2007 end-page: 156 ident: bib66 article-title: Collateral damage in cancer chemotherapy: oxidative stress in nontargeted tissues publication-title: Mol. Interv. contributor: fullname: St Clair – start-page: 94 year: 2002 end-page: 101 ident: bib18 article-title: Mitochondrial dysfunction is an early indicator of doxorubicin-induced apoptosis publication-title: Biochim. Biophys. Acta contributor: fullname: Leeuwenburgh – start-page: 125 year: 1983 end-page: 137 ident: bib8 article-title: Acute adriamycin cardiotoxicity in rats publication-title: Res. Commun. Chem. Pathol. Pharmacol. contributor: fullname: Sablan – start-page: 181 year: 1989 end-page: 189 ident: bib4 article-title: Oxidative and non-oxidative mechanisms in the inactivation of cardiac mitochondrial electron transport chain components by doxorubicin publication-title: Biochem. J. contributor: fullname: Davies – start-page: 1 year: 2013 end-page: 14 ident: bib22 article-title: Antisense directed against PS-1 gene decreases brain oxidative markers in aged senescence accelerated mice (SAMP8) and reverses learning and memory impairment: a proteomics study publication-title: Free Radic. Biol. Med. contributor: fullname: Allan Butterfield – start-page: 302 year: 1973 end-page: 314 ident: bib17 article-title: A clinicopathologic analysis of adriamycin cardiotoxicity publication-title: Cancer contributor: fullname: Gottlieb – volume: 6 start-page: CD003917 year: 2011 ident: bib69 article-title: Cardioprotective interventions for cancer patients receiving anthracyclines publication-title: Cochrane Database Syst. Rev. contributor: fullname: Kremer – start-page: 191 year: 1975 end-page: 194 ident: bib43 article-title: Adriamycin-induced cardiac damage in the mouse: a small-animal model of cardiotoxicity publication-title: J. Natl. Cancer Inst. contributor: fullname: Young – start-page: 3777 year: 2008 end-page: 3784 ident: bib40 article-title: Anthracycline cardiotoxicity: from bench to bedside publication-title: J. Clin. Oncol. contributor: fullname: Sawyer – start-page: 2370 year: 2011 end-page: 2379 ident: bib53 article-title: Protein targets for carbonylation by 4-hydroxy-2-nonenal in rat liver mitochondria publication-title: J. Proteomics contributor: fullname: Prokai – start-page: 436 year: 2005 end-page: 444 ident: bib59 article-title: Tissue-specific mtDNA lesions and radical-associated mitochondrial dysfunction in human hearts exposed to doxorubicin publication-title: J. Pathol. contributor: fullname: Walker – start-page: 900 year: 1998 end-page: 905 ident: bib3 article-title: Doxorubicin-induced cardiomyopathy publication-title: N. Engl. J. Med. contributor: fullname: Iliskovic – year: 2006 ident: bib29 article-title: Modifications of proteins by 4-hydroxy-2-nonenal in the ventilatory muscles of rats publication-title: Am. J. Physiol. Lung Cell. Mol. Physiol. contributor: fullname: Vassilakopoulos – start-page: 1590 year: 2012 end-page: 1609 ident: bib10 article-title: 4-Hydroxy-2-nonenal, a reactive product of lipid peroxidation, and neurodegenerative diseases: a toxic combination illuminated by redox proteomics studies publication-title: Antioxid. Redox Signaling contributor: fullname: Butterfield – start-page: 159 year: 1996 end-page: 166 ident: bib65 article-title: Stimulation of mitochondrial oxygen consumption in isolated cardiomyocytes after hypoxia–reoxygenation publication-title: Free Radic. Res. contributor: fullname: Darley-Usmar – start-page: 87 year: 1989 end-page: 94 ident: bib30 article-title: Effects of chronic administration of doxorubicin on myocardial creatine phosphokinase and antioxidant defenses and levels of lipid peroxidation in tissues and plasma of rats publication-title: J. Biochem. Toxicol. contributor: fullname: Wilson – start-page: 794 year: 2012 end-page: 814 ident: bib36 article-title: Manganese superoxide dismutase, MnSOD and its mimics publication-title: Biochim. Biophys. Acta contributor: fullname: Batinic-Haberle – start-page: 649 year: 1961 end-page: 654 ident: bib25 article-title: Biochemistry of dystrophic muscle: mitochondrial succinate-tetrazolium reductase and adenosine triphosphatase publication-title: Biochem. J. contributor: fullname: Pennington – start-page: 3060 year: 1986 end-page: 3067 ident: bib13 article-title: Redox cycling of anthracyclines by cardiac mitochondria. I. Anthracycline radical formation by NADH dehydrogenase publication-title: J. Biol. Chem. contributor: fullname: Doroshow – start-page: e18005 year: 2011 ident: bib19 article-title: p53 regulates oxidative stress-mediated retrograde signaling: a novel mechanism for chemotherapy-induced cardiac injury publication-title: PLoS One contributor: fullname: St Clair – start-page: 536 year: 2004 end-page: 547 ident: bib44 article-title: Oxidative damage precedes nitrative damage in adriamycin-induced cardiac mitochondrial injury publication-title: Toxicol. Pathol. contributor: fullname: Oberley – start-page: 33048 year: 2012 end-page: 33060 ident: bib52 article-title: Electrophilic aldehydes generated by sperm metabolism activate mitochondrial reactive oxygen species generation and apoptosis by targeting succinate dehydrogenase publication-title: J. Biol. Chem. contributor: fullname: Baker – start-page: 541 year: 1998 end-page: 552 ident: bib5 article-title: The secondary alcohol metabolite of doxorubicin irreversibly inactivates aconitase/iron regulatory protein-1 in cytosolic fractions from human myocardium publication-title: FASEB J. contributor: fullname: Cairo – start-page: 99 year: 2009 end-page: 107 ident: bib41 article-title: Importance of the bioenergetic reserve capacity in response to cardiomyocyte stress induced by 4-hydroxynonenal publication-title: Biochem. J. contributor: fullname: Darley-Usmar – start-page: 45154 year: 2003 end-page: 45159 ident: bib50 article-title: Cardiac mitochondrial NADP publication-title: J. Biol. Chem. contributor: fullname: Des Rosiers – year: 2005 ident: bib28 article-title: Ganong׳s Review of Medical Physiology contributor: fullname: Brooks – start-page: 543 year: 2005 end-page: 552 ident: bib64 article-title: Crystal structure of human dihydrolipoamide dehydrogenase: NAD publication-title: J. Mol. Biol. contributor: fullname: Chuang – start-page: 631 year: 1979 end-page: 638 ident: bib46 article-title: Morphometric characterization of left ventricular myocardial cells of male rats during postnatal development publication-title: J. Mol. Cell. Cardiol. contributor: fullname: Wenzelides – start-page: 886 year: 2006 end-page: 896 ident: bib60 article-title: Decreased complex II respiration and HNE-modified SDH subunit in diabetic heart publication-title: Free Radic. Biol. Med. contributor: fullname: Romani – volume: 30 start-page: 107 year: 2008 ident: 10.1016/j.freeradbiomed.2014.03.001_bib20 article-title: Redox proteomic identification of 4-hydroxy-2-nonenal-modified brain proteins in amnestic mild cognitive impairment: insight into the role of lipid peroxidation in the progression and pathogenesis of Alzheimer׳s disease publication-title: Neurobiol. Dis. doi: 10.1016/j.nbd.2007.12.007 contributor: fullname: Reed – volume: 28 start-page: 1017 year: 2000 ident: 10.1016/j.freeradbiomed.2014.03.001_bib70 article-title: Manganese–porphyrin reactions with lipids and lipoproteins publication-title: Free Radic. Biol. Med. doi: 10.1016/S0891-5849(00)00194-5 contributor: fullname: Bloodsworth – volume: 1588 start-page: 94 year: 2002 ident: 10.1016/j.freeradbiomed.2014.03.001_bib18 article-title: Mitochondrial dysfunction is an early indicator of doxorubicin-induced apoptosis publication-title: Biochim. Biophys. Acta doi: 10.1016/S0925-4439(02)00144-8 contributor: fullname: Green – volume: 49 start-page: 798 year: 2001 ident: 10.1016/j.freeradbiomed.2014.03.001_bib31 article-title: Peroxynitrite induced nitration and inactivation of myofibrillar creatine kinase in experimental heart failure publication-title: Cardiovasc. Res. doi: 10.1016/S0008-6363(00)00307-2 contributor: fullname: Mihm – volume: 15 start-page: 237 year: 1990 ident: 10.1016/j.freeradbiomed.2014.03.001_bib26 article-title: Chromogranin A: storage and release in hypertension publication-title: Hypertension doi: 10.1161/01.HYP.15.3.237 contributor: fullname: Takiyyuddin – volume: 53 start-page: 555 year: 1993 ident: 10.1016/j.freeradbiomed.2014.03.001_bib42 article-title: Pharmacokinetics and pharmacodynamics of doxorubicin in patients with small cell lung cancer publication-title: Clin. Pharmacol. Ther. doi: 10.1038/clpt.1993.69 contributor: fullname: Piscitelli – volume: 21 start-page: 440 year: 2011 ident: 10.1016/j.freeradbiomed.2014.03.001_bib56 article-title: Doxorubicin pathways: pharmacodynamics and adverse effects publication-title: Pharmacogenet. Genomics doi: 10.1097/FPC.0b013e32833ffb56 contributor: fullname: Thorn – volume: 41 start-page: 125 year: 1983 ident: 10.1016/j.freeradbiomed.2014.03.001_bib8 article-title: Acute adriamycin cardiotoxicity in rats publication-title: Res. Commun. Chem. Pathol. Pharmacol. contributor: fullname: Porta – volume: 283 start-page: 21837 year: 2008 ident: 10.1016/j.freeradbiomed.2014.03.001_bib15 article-title: Oxidative stress and covalent modification of protein with bioactive aldehydes publication-title: J. Biol. Chem. doi: 10.1074/jbc.R700019200 contributor: fullname: Grimsrud – volume: 207 start-page: 436 year: 2005 ident: 10.1016/j.freeradbiomed.2014.03.001_bib59 article-title: Tissue-specific mtDNA lesions and radical-associated mitochondrial dysfunction in human hearts exposed to doxorubicin publication-title: J. Pathol. doi: 10.1002/path.1863 contributor: fullname: Lebrecht – volume: 424 start-page: 99 year: 2009 ident: 10.1016/j.freeradbiomed.2014.03.001_bib41 article-title: Importance of the bioenergetic reserve capacity in response to cardiomyocyte stress induced by 4-hydroxynonenal publication-title: Biochem. J. doi: 10.1042/BJ20090934 contributor: fullname: Hill – volume: 259 start-page: 181 year: 1989 ident: 10.1016/j.freeradbiomed.2014.03.001_bib4 article-title: Oxidative and non-oxidative mechanisms in the inactivation of cardiac mitochondrial electron transport chain components by doxorubicin publication-title: Biochem. J. doi: 10.1042/bj2590181 contributor: fullname: Marcillat – volume: 18 start-page: 1639 year: 2012 ident: 10.1016/j.freeradbiomed.2014.03.001_bib68 article-title: Identification of the molecular basis of doxorubicin-induced cardiotoxicity publication-title: Nat. Med. doi: 10.1038/nm.2919 contributor: fullname: Zhang – volume: 17 start-page: 1590 year: 2012 ident: 10.1016/j.freeradbiomed.2014.03.001_bib10 article-title: 4-Hydroxy-2-nonenal, a reactive product of lipid peroxidation, and neurodegenerative diseases: a toxic combination illuminated by redox proteomics studies publication-title: Antioxid. Redox Signaling doi: 10.1089/ars.2011.4406 contributor: fullname: Perluigi – volume: 67 start-page: 1381 year: 2011 ident: 10.1016/j.freeradbiomed.2014.03.001_bib33 article-title: Uncoupling protein downregulation in doxorubicin-induced heart failure improves mitochondrial coupling but increases reactive oxygen species generation publication-title: Cancer Chemother. Pharmacol. doi: 10.1007/s00280-010-1441-7 contributor: fullname: Bugger – volume: 4 start-page: 87 year: 1989 ident: 10.1016/j.freeradbiomed.2014.03.001_bib30 article-title: Effects of chronic administration of doxorubicin on myocardial creatine phosphokinase and antioxidant defenses and levels of lipid peroxidation in tissues and plasma of rats publication-title: J. Biochem. Toxicol. doi: 10.1002/jbt.2570040204 contributor: fullname: Robison – volume: 35 start-page: 247 year: 1990 ident: 10.1016/j.freeradbiomed.2014.03.001_bib12 article-title: Structure of the adriamycin–cardiolipin complex: role in mitochondrial toxicity publication-title: Biophys. Chem. doi: 10.1016/0301-4622(90)80012-V contributor: fullname: Goormaghtigh – volume: 47 start-page: 123 year: 2013 ident: 10.1016/j.freeradbiomed.2014.03.001_bib24 article-title: Reversible inactivation of dihydrolipoamide dehydrogenase by mitochondrial hydrogen peroxide publication-title: Free Radic. Res. doi: 10.3109/10715762.2012.752078 contributor: fullname: Yan – volume: 195 start-page: 945 year: 1993 ident: 10.1016/j.freeradbiomed.2014.03.001_bib35 article-title: A deletion of mitochondrial DNA in murine doxorubicin-induced cardiotoxicity publication-title: Biochem. Biophys. Res. Commun. doi: 10.1006/bbrc.1993.2135 contributor: fullname: Adachi – volume: 15 start-page: 1 year: 2002 ident: 10.1016/j.freeradbiomed.2014.03.001_bib67 article-title: Inhibition of doxorubicin chronic toxicity in catalase-overexpressing transgenic mouse hearts publication-title: Chem. Res. Toxicol. doi: 10.1021/tx015532n contributor: fullname: Kang – volume: 98 start-page: 1253 year: 1996 ident: 10.1016/j.freeradbiomed.2014.03.001_bib45 article-title: The protective role of manganese superoxide dismutase against adriamycin-induced acute cardiac toxicity in transgenic mice publication-title: J. Clin. Invest. doi: 10.1172/JCI118909 contributor: fullname: Yen – volume: 276 start-page: H935 year: 1999 ident: 10.1016/j.freeradbiomed.2014.03.001_bib49 article-title: Formation of 4-hydroxy-2-nonenal-modified proteins in ischemic rat heart publication-title: Am. J. Physiol. contributor: fullname: Eaton – volume: 287 start-page: 33048 year: 2012 ident: 10.1016/j.freeradbiomed.2014.03.001_bib52 article-title: Electrophilic aldehydes generated by sperm metabolism activate mitochondrial reactive oxygen species generation and apoptosis by targeting succinate dehydrogenase publication-title: J. Biol. Chem. doi: 10.1074/jbc.M112.366690 contributor: fullname: Aitken – volume: 65C start-page: 1 year: 2013 ident: 10.1016/j.freeradbiomed.2014.03.001_bib22 article-title: Antisense directed against PS-1 gene decreases brain oxidative markers in aged senescence accelerated mice (SAMP8) and reverses learning and memory impairment: a proteomics study publication-title: Free Radic. Biol. Med. doi: 10.1016/j.freeradbiomed.2013.06.017 contributor: fullname: Fiorini – volume: 16 start-page: 1656 year: 2009 ident: 10.1016/j.freeradbiomed.2014.03.001_bib63 article-title: New developments in anthracycline-induced cardiotoxicity publication-title: Curr. Med. Chem. doi: 10.2174/092986709788186228 contributor: fullname: Mordente – volume: 17 start-page: 193 year: 1998 ident: 10.1016/j.freeradbiomed.2014.03.001_bib9 article-title: Thymoquinone protects against doxorubicin-induced cardiotoxicity without compromising its antitumor activity publication-title: J. Exp. Clin. Cancer Res. contributor: fullname: al-Shabanah – volume: 57 start-page: 727 year: 1999 ident: 10.1016/j.freeradbiomed.2014.03.001_bib38 article-title: A critical evaluation of the mechanisms of action proposed for the antitumor effects of the anthracycline antibiotics adriamycin and daunorubicin publication-title: Biochem. Pharmacol. doi: 10.1016/S0006-2952(98)00307-4 contributor: fullname: Gewirtz – volume: 4 start-page: 1908 year: 2013 ident: 10.1016/j.freeradbiomed.2014.03.001_bib1 article-title: Drug-induced histone eviction from open chromatin contributes to the chemotherapeutic effects of doxorubicin publication-title: Nat. Commun. doi: 10.1038/ncomms2921 contributor: fullname: Pang – volume: 55 start-page: 191 year: 1975 ident: 10.1016/j.freeradbiomed.2014.03.001_bib43 article-title: Adriamycin-induced cardiac damage in the mouse: a small-animal model of cardiotoxicity publication-title: J. Natl. Cancer Inst. doi: 10.1093/jnci/55.1.191 contributor: fullname: Rosenoff – volume: 6 start-page: CD003917 year: 2011 ident: 10.1016/j.freeradbiomed.2014.03.001_bib69 article-title: Cardioprotective interventions for cancer patients receiving anthracyclines publication-title: Cochrane Database Syst. Rev. contributor: fullname: van Dalen – volume: 261 start-page: 3060 year: 1986 ident: 10.1016/j.freeradbiomed.2014.03.001_bib13 article-title: Redox cycling of anthracyclines by cardiac mitochondria. I. Anthracycline radical formation by NADH dehydrogenase publication-title: J. Biol. Chem. doi: 10.1016/S0021-9258(17)35746-0 contributor: fullname: Davies – volume: 1822 start-page: 794 year: 2012 ident: 10.1016/j.freeradbiomed.2014.03.001_bib36 article-title: Manganese superoxide dismutase, MnSOD and its mimics publication-title: Biochim. Biophys. Acta doi: 10.1016/j.bbadis.2011.12.002 contributor: fullname: Miriyala – volume: 56 start-page: 377 year: 1985 ident: 10.1016/j.freeradbiomed.2014.03.001_bib47 article-title: Ultrastructural morphometric analysis of myocardium from dogs, rats, hamsters, mice, and from human hearts publication-title: Circ. Res. doi: 10.1161/01.RES.56.3.377 contributor: fullname: Schaper – volume: 417 start-page: 513 year: 2009 ident: 10.1016/j.freeradbiomed.2014.03.001_bib48 article-title: Myocardial ischaemia inhibits mitochondrial metabolism of 4-hydroxy-trans-2-nonenal publication-title: Biochem. J. doi: 10.1042/BJ20081615 contributor: fullname: Hill – volume: 26 start-page: 3777 year: 2008 ident: 10.1016/j.freeradbiomed.2014.03.001_bib40 article-title: Anthracycline cardiotoxicity: from bench to bedside publication-title: J. Clin. Oncol. doi: 10.1200/JCO.2007.14.9401 contributor: fullname: Gianni – volume: 18 start-page: 1160 year: 2010 ident: 10.1016/j.freeradbiomed.2014.03.001_bib61 article-title: Familial neonatal isolated cardiomyopathy caused by a mutation in the flavoprotein subunit of succinate dehydrogenase publication-title: Eur. J. Hum. Genet. doi: 10.1038/ejhg.2010.83 contributor: fullname: Levitas – volume: 6 start-page: e18005 year: 2011 ident: 10.1016/j.freeradbiomed.2014.03.001_bib19 article-title: p53 regulates oxidative stress-mediated retrograde signaling: a novel mechanism for chemotherapy-induced cardiac injury publication-title: PLoS One doi: 10.1371/journal.pone.0018005 contributor: fullname: Velez – volume: 191 start-page: 288 year: 2011 ident: 10.1016/j.freeradbiomed.2014.03.001_bib32 article-title: Bioenergetic function in cardiovascular cells: the importance of the reserve capacity and its biological regulation publication-title: Chem. Biol. Interact. doi: 10.1016/j.cbi.2010.12.002 contributor: fullname: Sansbury – volume: 10 start-page: 485 year: 1997 ident: 10.1016/j.freeradbiomed.2014.03.001_bib6 article-title: Reactive oxygen-mediated protein oxidation in aging and disease publication-title: Chem. Res. Toxicol. doi: 10.1021/tx960133r contributor: fullname: Stadtman – volume: 7 start-page: 147 year: 2007 ident: 10.1016/j.freeradbiomed.2014.03.001_bib66 article-title: Collateral damage in cancer chemotherapy: oxidative stress in nontargeted tissues publication-title: Mol. Interv. doi: 10.1124/mi.7.3.6 contributor: fullname: Chen – volume: 302 start-page: H2178 year: 2012 ident: 10.1016/j.freeradbiomed.2014.03.001_bib11 article-title: Cardiac mitochondrial network excitability: insights from computational analysis publication-title: Am. J. Physiol. Heart Circ. Physiol. doi: 10.1152/ajpheart.01073.2011 contributor: fullname: Zhou – year: 2005 ident: 10.1016/j.freeradbiomed.2014.03.001_bib28 contributor: fullname: Barret – volume: 52 start-page: 1828 year: 2012 ident: 10.1016/j.freeradbiomed.2014.03.001_bib34 article-title: A new SOD mimic, Mn(III) ortho N-butoxyethylpyridylporphyrin, combines superb potency and lipophilicity with low toxicity publication-title: Free Radic. Biol. Med. doi: 10.1016/j.freeradbiomed.2012.02.006 contributor: fullname: Rajic – volume: 12 start-page: 541 year: 1998 ident: 10.1016/j.freeradbiomed.2014.03.001_bib5 article-title: The secondary alcohol metabolite of doxorubicin irreversibly inactivates aconitase/iron regulatory protein-1 in cytosolic fractions from human myocardium publication-title: FASEB J. doi: 10.1096/fasebj.12.7.541 contributor: fullname: Minotti – ident: 10.1016/j.freeradbiomed.2014.03.001_bib37 doi: 10.1089/ars.2012.5147 – volume: 34 start-page: 106 year: 2014 ident: 10.1016/j.freeradbiomed.2014.03.001_bib16 article-title: Doxorubicin-induced cardiotoxicity: from bioenergetic failure and cell death to cardiomyopathy publication-title: Med. Res. Rev. doi: 10.1002/med.21280 contributor: fullname: Carvalho – volume: 24 start-page: 159 year: 1996 ident: 10.1016/j.freeradbiomed.2014.03.001_bib65 article-title: Stimulation of mitochondrial oxygen consumption in isolated cardiomyocytes after hypoxia–reoxygenation publication-title: Free Radic. Res. doi: 10.3109/10715769609088013 contributor: fullname: Smith – volume: 13 start-page: 245 year: 2003 ident: 10.1016/j.freeradbiomed.2014.03.001_bib57 article-title: Differential ability of cytostatics from anthraquinone group to generate free radicals in three enzymatic systems: NADH dehydrogenase, NADPH cytochrome P450 reductase, and xanthine oxidase publication-title: Oncol. Res. doi: 10.3727/096504003108748294 contributor: fullname: Pawlowska – volume: 74 start-page: 2370 year: 2011 ident: 10.1016/j.freeradbiomed.2014.03.001_bib53 article-title: Protein targets for carbonylation by 4-hydroxy-2-nonenal in rat liver mitochondria publication-title: J. Proteomics doi: 10.1016/j.jprot.2011.07.009 contributor: fullname: Guo – volume: 892 start-page: 320 year: 1987 ident: 10.1016/j.freeradbiomed.2014.03.001_bib58 article-title: Effects of adriamycin on respiratory chain activities in mitochondria from rat liver, rat heart and bovine heart: evidence for a preferential inhibition of complex III and IV publication-title: Biochim. Biophys. Acta doi: 10.1016/0005-2728(87)90236-2 contributor: fullname: Nicolay – volume: 23 start-page: 15 year: 2007 ident: 10.1016/j.freeradbiomed.2014.03.001_bib14 article-title: Adriamycin-induced oxidative mitochondrial cardiotoxicity publication-title: Cell Biol. Toxicol. doi: 10.1007/s10565-006-0140-y contributor: fullname: Berthiaume – volume: 278 start-page: 45154 year: 2003 ident: 10.1016/j.freeradbiomed.2014.03.001_bib50 article-title: Cardiac mitochondrial NADP+-isocitrate dehydrogenase is inactivated through 4-hydroxynonenal adduct formation: an event that precedes hypertrophy development publication-title: J. Biol. Chem. doi: 10.1074/jbc.M306285200 contributor: fullname: Benderdour – volume: 33 start-page: 1919 year: 2001 ident: 10.1016/j.freeradbiomed.2014.03.001_bib51 article-title: Role of 4-hydroxynonenal in modification of cytochrome c oxidase in ischemia/reperfused rat heart publication-title: J. Mol. Cell. Cardiol. doi: 10.1006/jmcc.2001.1454 contributor: fullname: Chen – volume: 80 start-page: 649 year: 1961 ident: 10.1016/j.freeradbiomed.2014.03.001_bib25 article-title: Biochemistry of dystrophic muscle: mitochondrial succinate-tetrazolium reductase and adenosine triphosphatase publication-title: Biochem. J. doi: 10.1042/bj0800649 contributor: fullname: Pennington – volume: 11 start-page: 631 year: 1979 ident: 10.1016/j.freeradbiomed.2014.03.001_bib46 article-title: Morphometric characterization of left ventricular myocardial cells of male rats during postnatal development publication-title: J. Mol. Cell. Cardiol. doi: 10.1016/0022-2828(79)90377-8 contributor: fullname: David – volume: 85 start-page: 3585 year: 1988 ident: 10.1016/j.freeradbiomed.2014.03.001_bib62 article-title: Doxorubicin cardiotoxicity may be caused by its metabolite, doxorubicinol publication-title: Proc. Natl. Acad. Sci. USA doi: 10.1073/pnas.85.10.3585 contributor: fullname: Olson – volume: 115 start-page: 155 year: 2010 ident: 10.1016/j.freeradbiomed.2014.03.001_bib2 article-title: Doxorubicin cardiomyopathy publication-title: Cardiology doi: 10.1159/000265166 contributor: fullname: Chatterjee – volume: 45 start-page: 826 year: 2008 ident: 10.1016/j.freeradbiomed.2014.03.001_bib54 article-title: Age-related alterations in oxidatively damaged proteins of mouse skeletal muscle mitochondrial electron transport chain complexes publication-title: Free Radic. Biol. Med. doi: 10.1016/j.freeradbiomed.2008.06.006 contributor: fullname: Choksi – volume: 40 start-page: 886 year: 2006 ident: 10.1016/j.freeradbiomed.2014.03.001_bib60 article-title: Decreased complex II respiration and HNE-modified SDH subunit in diabetic heart publication-title: Free Radic. Biol. Med. doi: 10.1016/j.freeradbiomed.2005.10.040 contributor: fullname: Lashin – volume: 339 start-page: 900 year: 1998 ident: 10.1016/j.freeradbiomed.2014.03.001_bib3 article-title: Doxorubicin-induced cardiomyopathy publication-title: N. Engl. J. Med. doi: 10.1056/NEJM199809243391307 contributor: fullname: Singal – volume: 56 start-page: 185 year: 2004 ident: 10.1016/j.freeradbiomed.2014.03.001_bib39 article-title: Anthracyclines: molecular advances and pharmacologic developments in antitumor activity and cardiotoxicity publication-title: Pharmacol. Rev. doi: 10.1124/pr.56.2.6 contributor: fullname: Minotti – volume: 5 start-page: 2851 year: 2006 ident: 10.1016/j.freeradbiomed.2014.03.001_bib21 article-title: Increase in Mrp1 expression and 4-hydroxy-2-nonenal adduction in heart tissue of adriamycin-treated C57BL/6 mice publication-title: Mol. Cancer Ther. doi: 10.1158/1535-7163.MCT-06-0297 contributor: fullname: Jungsuwadee – volume: 32 start-page: 302 year: 1973 ident: 10.1016/j.freeradbiomed.2014.03.001_bib17 article-title: A clinicopathologic analysis of adriamycin cardiotoxicity publication-title: Cancer doi: 10.1002/1097-0142(197308)32:2<302::AID-CNCR2820320205>3.0.CO;2-2 contributor: fullname: Lefrak – volume: 70 start-page: 2880 year: 2010 ident: 10.1016/j.freeradbiomed.2014.03.001_bib27 article-title: A NADPH oxidase-dependent redox signaling pathway mediates the selective radiosensitization effect of parthenolide in prostate cancer cells publication-title: Cancer Res. doi: 10.1158/0008-5472.CAN-09-4572 contributor: fullname: Sun – volume: 350 start-page: 543 year: 2005 ident: 10.1016/j.freeradbiomed.2014.03.001_bib64 article-title: Crystal structure of human dihydrolipoamide dehydrogenase: NAD+/NADH binding and the structural basis of disease-causing mutations publication-title: J. Mol. Biol. doi: 10.1016/j.jmb.2005.05.014 contributor: fullname: Brautigam – volume: 50 start-page: 319 year: 2003 ident: 10.1016/j.freeradbiomed.2014.03.001_bib7 article-title: Lipid peroxidation and cell cycle signaling: 4-hydroxynonenal, a key molecule in stress mediated signaling publication-title: Acta Biochim. Pol. doi: 10.18388/abp.2003_3689 contributor: fullname: Yang – volume: 32 start-page: 536 year: 2004 ident: 10.1016/j.freeradbiomed.2014.03.001_bib44 article-title: Oxidative damage precedes nitrative damage in adriamycin-induced cardiac mitochondrial injury publication-title: Toxicol. Pathol. doi: 10.1080/01926230490502601 contributor: fullname: Chaiswing – volume: 41 start-page: 1470 year: 2006 ident: 10.1016/j.freeradbiomed.2014.03.001_bib23 article-title: Redox proteomic identification of oxidized cardiac proteins in adriamycin-treated mice publication-title: Free Radic. Biol. Med. doi: 10.1016/j.freeradbiomed.2006.08.006 contributor: fullname: Chen – volume: 290 year: 2006 ident: 10.1016/j.freeradbiomed.2014.03.001_bib29 article-title: Modifications of proteins by 4-hydroxy-2-nonenal in the ventilatory muscles of rats publication-title: Am. J. Physiol. Lung Cell. Mol. Physiol. doi: 10.1152/ajplung.00337.2005 contributor: fullname: Hussain – volume: 49 start-page: 195 year: 2001 ident: 10.1016/j.freeradbiomed.2014.03.001_bib55 article-title: Mutations in the complex I NDUFS2 gene of patients with cardiomyopathy and encephalomyopathy publication-title: Ann. Neurol. doi: 10.1002/1531-8249(20010201)49:2<195::AID-ANA39>3.0.CO;2-M contributor: fullname: Loeffen |
SSID | ssj0004538 |
Score | 2.4929342 |
Snippet | Doxorubicin (DOX), one of the most effective anticancer drugs, is known to generate progressive cardiac damage, which is due, in part, to DOX-induced reactive... |
SourceID | pubmedcentral proquest crossref pubmed elsevier |
SourceType | Open Access Repository Aggregation Database Index Database Publisher |
StartPage | 55 |
SubjectTerms | Aldehydes - metabolism Animals Antibiotics, Antineoplastic - toxicity ATP synthase Cardiac injury Dihydrolipoyl dehydrogenase Doxorubicin Doxorubicin - toxicity Electrophoresis, Gel, Two-Dimensional Energy Metabolism - drug effects Free radicals Immunoblotting Immunoprecipitation Lipid Peroxidation - drug effects Male Metabolism Mice Mice, Inbred C57BL Mitochondria, Heart - drug effects Mitochondria, Heart - metabolism NADH dehydrogenase [ubiquinone] iron–sulfur protein 2 Oxidation-Reduction Oxidative stress Proteomics Redox proteomics Succinate dehydrogenase [ubiquinone] flavoprotein |
Title | Redox proteomic identification of HNE-bound mitochondrial proteins in cardiac tissues reveals a systemic effect on energy metabolism after doxorubicin treatment |
URI | https://dx.doi.org/10.1016/j.freeradbiomed.2014.03.001 https://www.ncbi.nlm.nih.gov/pubmed/24632380 https://search.proquest.com/docview/1687685312 https://pubmed.ncbi.nlm.nih.gov/PMC4053505 |
Volume | 72 |
hasFullText | 1 |
inHoldings | 1 |
isFullTextHit | |
isPrint | |
link | http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwpV1Li9RAEC72geJFdNfH-FhKFG9xknQnmVyEYdllVJyDurC3kE66MeJ0lpkM7F72t_hTrepOxh1FECSQkFfTpKq7qtJffQXwSgihaUvIc9N5IJXUgeJkH4qGjMlDHUUu6_3jPJ2dyffnyfkOHA-5MAyr7Od-P6e72bq_Mu6_5viiacafw0kekfnMKUSgoCJLdmGfzBGv1e5P332YzW-QhruC1vx8wC_chpe_YF5mqTWvWrtkd4Z6SU96Gv3NUP3piP6Op7xhoE7vwd3es8Sp7_x92NH2AA6nlqLqxRW-Rof1dD_RD-CWL0F5dQg_Pum6vURH18AJytjUPX7IiQxbg7P5SaC4-hIuaPjTdGlr1lr_TmNX2FisnKJV2Dk5rpCJoUixsURPFU0Ne-QIUpva5RviQnekgd-b1QJdpXKkjrTLteK1ftwA4B_A2enJl-NZ0FdtCKokD7uAk2FDXaaiJstXGnIAyiqSdRlPqiwPVanZJaSrWmo6ZEmt4iwxItImNdmkrMVD2LOt1Y8BM8P0drQjr08KqVRCemRUJbKYgmldjUAOIiouPDlHMaDWvhVbki1YskUoGMM3greDOIstXSvIjPxbAy8GJShoNPISS2l1u14VUUrWhTygKB7BI68Um57FMhXkIIUjyLbUZfMAM31v37HNV8f4LZmFJ0ye_G_Hn8IdPvNw42ew1y3X-jk5VZ06gt0319FRP3R-Akq1KEU |
link.rule.ids | 230,314,780,784,885,4502,24116,27924,27925,45585,45679 |
linkProvider | Elsevier |
linkToHtml | http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwpV3db9MwED-NIT5eEGx8lM9DIN6yJrGTNC9I07SpwNYH2KS9WXFiiyCaTG0qsRf-Fv5U7uykrCAkJFQplRLHsno_--7q3_0M8FoIYeiTUORm8kBqaQLNxT6UDVmbhyaKXNX7ySydnsn358n5FhwMtTBMq-zXfr-mu9W6vzPuf83xRV2PP4WTPCL3mVOKQElFllyD6zKh6JdAvfc9uiIZ7o6z5tYBN78Jr36RvOzCGN6zdqXuTPSSXvI0-pub-jMM_Z1NecU9Hd2FO31cift-6PdgyzQ7sLvfUE49v8Q36Jie7i_0HbjhD6C83IUfH03VfkMn1sDlyVhXPXvIGQxbi9PZYaD57CWc0-SnxbKpGLP-nbpZYt1g6WBWYuesuESWhSJYY4FeKJo69rwRpD6NqzbEuekIf1_r5RzdOeVIA2kXK807_bimv9-Hs6PD04Np0J_ZEJRJHnYBl8KGpkhFRX6vsOT-izKSVRFPyiwPdWE4IKS7Rhr6ypJKx1liRWRsarNJUYkHsN20jXkEmFkWt6MLxXxSSK0TQpHVpchiSqVNOQI5mEhdeGkONXDWvqgNyyq2rAoFM_hG8HYwp9pAmiIn8m8dvBxAoGgu8gZL0Zh2tVRRSr6F4p8oHsFDD4r1yGKZCgqPwhFkG3BZN2Cd780nTf3Z6X1L1uAJk8f_O_AXcGt6enKsjt_NPjyB2_zEE4-fwna3WJlnFF51-rmbPj8BDgkpHg |
openUrl | ctx_ver=Z39.88-2004&ctx_enc=info%3Aofi%2Fenc%3AUTF-8&rfr_id=info%3Asid%2Fsummon.serialssolutions.com&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.atitle=Redox+proteomic+identification+of+HNE-bound+mitochondrial+proteins+in+cardiac+tissues+reveals+a+systemic+effect+on+energy+metabolism+after+doxorubicin+treatment&rft.jtitle=Free+radical+biology+%26+medicine&rft.au=Zhao%2C+Y&rft.au=Miriyala%2C+S&rft.au=Miao%2C+L&rft.au=Mitov%2C+M&rft.date=2014-07-01&rft.issn=0891-5849&rft.volume=72&rft.spage=55&rft.epage=65&rft_id=info:doi/10.1016%2Fj.freeradbiomed.2014.03.001&rft.externalDBID=NO_FULL_TEXT |
thumbnail_l | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/lc.gif&issn=0891-5849&client=summon |
thumbnail_m | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/mc.gif&issn=0891-5849&client=summon |
thumbnail_s | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/sc.gif&issn=0891-5849&client=summon |