CISD1 inhibits ferroptosis by protection against mitochondrial lipid peroxidation
Ferroptosis is a form of non-apoptotic cell death originally identified in cancer cells. However, the key regulator of ferroptosis in mitochondria remains unknown. Here, we show that CDGSH iron sulfur domain 1 (CISD1, also termed mitoNEET), an iron-containing outer mitochondrial membrane protein, ne...
Saved in:
| Published in | Biochemical and biophysical research communications Vol. 478; no. 2; pp. 838 - 844 |
|---|---|
| Main Authors | , , , , |
| Format | Journal Article |
| Language | English |
| Published |
United States
Elsevier Inc
16.09.2016
|
| Subjects | |
| Online Access | Get full text |
Cover
Loading…
| Abstract | Ferroptosis is a form of non-apoptotic cell death originally identified in cancer cells. However, the key regulator of ferroptosis in mitochondria remains unknown. Here, we show that CDGSH iron sulfur domain 1 (CISD1, also termed mitoNEET), an iron-containing outer mitochondrial membrane protein, negatively regulates ferroptotic cancer cell death. The classical ferroptosis inducer erastin promotes CISD1 expression in an iron-dependent manner in human hepatocellular carcinoma cells (e.g., HepG2 and Hep3B). Genetic inhibition of CISD1 increased iron-mediated intramitochondrial lipid peroxidation, which contributes to erastin-induced ferroptosis. In contrast, stabilization of the iron sulfur cluster of CISD1 by pioglitazone inhibits mitochondrial iron uptake, lipid peroxidation, and subsequent ferroptosis. These findings indicate a novel role of CISD1 in protecting against mitochondrial injury in ferroptosis. |
|---|---|
| AbstractList | Ferroptosis is a form of non-apoptotic cell death originally identified in cancer cells. However, the key regulator of ferroptosis in mitochondria remains unknown. Here, we show that CDGSH iron sulfur domain 1 (CISD1, also termed mitoNEET), an iron-containing outer mitochondrial membrane protein, negatively regulates ferroptotic cancer cell death. The classical ferroptosis inducer erastin promotes CISD1 expression in an iron-dependent manner in human hepatocellular carcinoma cells (e.g., HepG2 and Hep3B). Genetic inhibition of CISD1 increased iron-mediated intramitochondrial lipid peroxidation, which contributes to erastin-induced ferroptosis. In contrast, stabilization of the iron sulfur cluster of CISD1 by pioglitazone inhibits mitochondrial iron uptake, lipid peroxidation, and subsequent ferroptosis. These findings indicate a novel role of CISD1 in protecting against mitochondrial injury in ferroptosis. |
| Author | Tang, Daolin Kang, Rui Zhang, Xiuying Yuan, Hua Li, Xuemei |
| Author_xml | – sequence: 1 givenname: Hua surname: Yuan fullname: Yuan, Hua organization: School of Nursing, Jilin University, Changchun, Jilin 130021, China – sequence: 2 givenname: Xuemei surname: Li fullname: Li, Xuemei organization: Department of Hematology, Qingdao Municipal Hospital, Qingdao, Shandong 261041, China – sequence: 3 givenname: Xiuying surname: Zhang fullname: Zhang, Xiuying organization: School of Nursing, Jilin University, Changchun, Jilin 130021, China – sequence: 4 givenname: Rui surname: Kang fullname: Kang, Rui organization: Department of Surgery, University of Pittsburgh, Pittsburgh, PA 15213, USA – sequence: 5 givenname: Daolin surname: Tang fullname: Tang, Daolin email: tangd2@upmc.edu organization: School of Nursing, Jilin University, Changchun, Jilin 130021, China |
| BackLink | https://www.ncbi.nlm.nih.gov/pubmed/27510639$$D View this record in MEDLINE/PubMed |
| BookMark | eNqFkU1v1DAQhi1URLeFP8AB5cglYfyRbCxxQUuBSpUQapG4WY49S2eVjYPtRe2_x2HbC4dysiU_78jzvGfsZAoTMvaaQ8OBd-92zTBE14hyb6BvQKpnbMVBQy04qBO2AoCuFpr_OGVnKe0AOFedfsFOxbrl0Em9Yt82l9cfeUXTLQ2UU7XFGMOcQ6JUDffVHENGlylMlf1paUq52lMO7jZMPpIdq5Fm8tWMMdyRtwv4kj3f2jHhq4fznH3_dHGz-VJfff18uflwVTvVtrnWvRKutVYNPbRr2WvNnZWd0FpKIVpnuW5F563A3lnlBynWywN4FFuBYpDn7O1xbvnjrwOmbPaUHI6jnTAckikOuFQtgPovyvvipStSdEHfPKCHYY_ezJH2Nt6bR2MF6I-AiyGliFvjKP9dPEdLo-FglnLMzizlmKUcA70p5ZSo-Cf6OP3J0PtjCIvL34TRJEc4OfQUSzPGB3oq_gesb6ce |
| CitedBy_id | crossref_primary_10_1038_s42255_022_00645_2 crossref_primary_10_2174_0118744710262369231110065230 crossref_primary_10_1016_j_freeradbiomed_2021_09_013 crossref_primary_10_1177_1934578X231220485 crossref_primary_10_1016_j_phrs_2021_105580 crossref_primary_10_1186_s40104_023_00841_4 crossref_primary_10_3389_fcell_2021_616271 crossref_primary_10_3389_fimmu_2024_1511015 crossref_primary_10_1016_j_bbadis_2021_166088 crossref_primary_10_1007_s13577_020_00431_w crossref_primary_10_3390_ph11040113 crossref_primary_10_1016_j_lfs_2022_120868 crossref_primary_10_1186_s41016_024_00357_4 crossref_primary_10_3389_fcvm_2023_1241282 crossref_primary_10_1007_s12011_022_03523_w crossref_primary_10_3389_fphar_2020_00239 crossref_primary_10_1016_j_phrs_2021_105466 crossref_primary_10_3389_fmolb_2022_890766 crossref_primary_10_1016_j_ccell_2019_04_002 crossref_primary_10_1186_s40364_020_00229_w crossref_primary_10_62347_SIGP9279 crossref_primary_10_1002_jnr_25033 crossref_primary_10_1038_s41422_020_00441_1 crossref_primary_10_1007_s40139_017_0139_5 crossref_primary_10_17816_RCF567780 crossref_primary_10_1111_raq_12719 crossref_primary_10_3389_fphar_2024_1290120 crossref_primary_10_3389_fmed_2024_1478153 crossref_primary_10_3390_ijms21186751 crossref_primary_10_1002_jat_4670 crossref_primary_10_1016_j_ejphar_2021_174613 crossref_primary_10_1111_jcmm_15127 crossref_primary_10_3389_fcell_2021_801365 crossref_primary_10_3390_cells9102229 crossref_primary_10_3389_fonc_2024_1394699 crossref_primary_10_3389_fmolb_2023_1203269 crossref_primary_10_1155_2020_9547127 crossref_primary_10_1038_s41416_023_02149_6 crossref_primary_10_1038_s41419_023_05638_x crossref_primary_10_14336_AD_2023_0717 crossref_primary_10_1016_j_envpol_2024_123846 crossref_primary_10_14336_AD_2024_0125_1 crossref_primary_10_1038_s41420_024_01863_1 crossref_primary_10_1093_jxb_eraa425 crossref_primary_10_1002_anie_202300379 crossref_primary_10_1186_s10020_022_00549_7 crossref_primary_10_1042_BSR20210527 crossref_primary_10_2174_0109298665333926240927074528 crossref_primary_10_3389_fmolb_2022_940575 crossref_primary_10_1155_2022_7823191 crossref_primary_10_3389_fphar_2023_1087557 crossref_primary_10_3390_antiox11030501 crossref_primary_10_3390_biom13010037 crossref_primary_10_1016_j_cophys_2022_100483 crossref_primary_10_1166_jnn_2021_18643 crossref_primary_10_1016_j_critrevonc_2022_103887 crossref_primary_10_1080_15548627_2020_1739447 crossref_primary_10_2139_ssrn_4091174 crossref_primary_10_3389_fphar_2023_1286449 crossref_primary_10_3389_fonc_2022_947530 crossref_primary_10_1007_s11684_023_0992_z crossref_primary_10_3390_ijms232415677 crossref_primary_10_1016_j_canlet_2022_215854 crossref_primary_10_1016_j_gendis_2020_09_005 crossref_primary_10_1038_s41418_017_0012_4 crossref_primary_10_3389_fmolb_2022_985571 crossref_primary_10_1016_j_bbrc_2016_10_068 crossref_primary_10_3390_biomedicines9111679 crossref_primary_10_58567_ci03010001 crossref_primary_10_1002_cbin_11443 crossref_primary_10_1016_j_cell_2017_09_021 crossref_primary_10_1007_s00210_025_03927_0 crossref_primary_10_1016_j_cellsig_2023_110654 crossref_primary_10_1016_j_gendis_2020_11_019 crossref_primary_10_1177_17590914211037505 crossref_primary_10_1186_s12943_024_01999_9 crossref_primary_10_1016_j_molcel_2024_04_009 crossref_primary_10_1007_s12094_023_03136_2 crossref_primary_10_1039_D3BM01832F crossref_primary_10_1016_j_canlet_2017_12_025 crossref_primary_10_3390_cells11223653 crossref_primary_10_1016_j_prp_2022_153886 crossref_primary_10_3390_ijms25031518 crossref_primary_10_3389_fonc_2021_579286 crossref_primary_10_3390_antiox11050966 crossref_primary_10_3390_genes14101964 crossref_primary_10_1155_2022_5124553 crossref_primary_10_1016_j_mad_2021_111439 crossref_primary_10_3389_fimmu_2022_1028054 crossref_primary_10_1186_s11658_022_00383_z crossref_primary_10_2174_0929867329666220819112808 crossref_primary_10_3389_fnins_2018_00466 crossref_primary_10_1016_j_jconrel_2022_01_034 crossref_primary_10_1038_s41416_022_01998_x crossref_primary_10_3389_fcell_2021_743046 crossref_primary_10_1053_j_gastro_2024_01_051 crossref_primary_10_3390_cells9061505 crossref_primary_10_1016_j_bcp_2023_115725 crossref_primary_10_1016_j_heliyon_2023_e19799 crossref_primary_10_1007_s13577_023_00890_x crossref_primary_10_3724_abbs_2023120 crossref_primary_10_1016_j_freeradbiomed_2019_01_008 crossref_primary_10_3389_fcell_2021_746696 crossref_primary_10_1038_s41420_021_00660_4 crossref_primary_10_1007_s10495_023_01928_z crossref_primary_10_1089_ars_2022_0203 crossref_primary_10_3390_ijms25053015 crossref_primary_10_1016_j_bbadis_2021_166204 crossref_primary_10_2147_JIR_S307081 crossref_primary_10_7717_peerj_11233 crossref_primary_10_1111_febs_16059 crossref_primary_10_3390_cancers15205043 crossref_primary_10_3390_biom12111702 crossref_primary_10_1515_hsz_2016_0336 crossref_primary_10_1016_j_abb_2023_109644 crossref_primary_10_3390_biom13050820 crossref_primary_10_1038_s41571_020_00462_0 crossref_primary_10_1124_molpharm_122_000607 crossref_primary_10_1016_j_expneurol_2023_114614 crossref_primary_10_32604_biocell_2024_047812 crossref_primary_10_3389_fgene_2021_672904 crossref_primary_10_1002_mc_23533 crossref_primary_10_3389_fmolb_2023_1229710 crossref_primary_10_3390_antiox11081504 crossref_primary_10_1038_s41419_023_06262_5 crossref_primary_10_3892_ol_2019_11159 crossref_primary_10_1007_s12072_021_10248_w crossref_primary_10_3389_fcell_2021_698679 crossref_primary_10_1016_j_bbrc_2024_150683 crossref_primary_10_3390_antiox13030298 crossref_primary_10_3389_fonc_2020_590861 crossref_primary_10_1016_j_expneurol_2022_114100 crossref_primary_10_1016_j_mito_2024_101974 crossref_primary_10_1016_j_bbrc_2016_10_099 crossref_primary_10_1038_s41422_019_0164_5 crossref_primary_10_1016_j_heliyon_2024_e36559 crossref_primary_10_3390_ijms21144908 crossref_primary_10_1097_MD_0000000000029068 crossref_primary_10_1016_j_ejmech_2022_114861 crossref_primary_10_1038_s41392_024_01769_5 crossref_primary_10_1111_liv_15936 crossref_primary_10_1016_j_brainresbull_2022_04_005 crossref_primary_10_1038_s41418_022_00941_0 crossref_primary_10_1038_s41467_024_48695_2 crossref_primary_10_1080_16078454_2022_2132362 crossref_primary_10_1038_s41413_024_00398_6 crossref_primary_10_1186_s12964_025_02121_2 crossref_primary_10_58567_ci02020001 crossref_primary_10_1016_j_ajpath_2019_09_012 crossref_primary_10_1161_CIRCULATIONAHA_122_060257 crossref_primary_10_3390_cancers15102694 crossref_primary_10_1016_j_jare_2024_09_025 crossref_primary_10_1038_s41569_022_00735_4 crossref_primary_10_1016_j_cej_2024_154569 crossref_primary_10_1016_j_cmet_2020_10_011 crossref_primary_10_18632_aging_203140 crossref_primary_10_3389_fonc_2021_738477 crossref_primary_10_3748_wjg_v29_i16_2433 crossref_primary_10_3389_fgene_2021_708699 crossref_primary_10_1002_jat_4613 crossref_primary_10_3892_ijo_2022_5438 crossref_primary_10_3389_fcell_2021_739392 crossref_primary_10_1038_s41419_021_04128_2 crossref_primary_10_7717_peerj_11687 crossref_primary_10_1016_j_canlet_2018_06_018 crossref_primary_10_3389_fimmu_2025_1531577 crossref_primary_10_3390_ijms25010480 crossref_primary_10_3389_fmolb_2022_1051866 crossref_primary_10_1016_j_ejcb_2019_151058 crossref_primary_10_1007_s11010_023_04694_3 crossref_primary_10_1016_j_mehy_2017_02_017 crossref_primary_10_1186_s13045_024_01564_3 crossref_primary_10_1016_j_lfs_2021_119958 crossref_primary_10_1186_s12967_024_05404_3 crossref_primary_10_4103_1673_5374_274344 crossref_primary_10_1002_ijc_34486 crossref_primary_10_1007_s13402_023_00784_y crossref_primary_10_1016_j_yexcr_2021_112678 crossref_primary_10_1152_ajprenal_00016_2021 crossref_primary_10_3389_fendo_2023_1248934 crossref_primary_10_4251_wjgo_v14_i1_1 crossref_primary_10_3389_fcell_2020_590226 crossref_primary_10_1007_s12013_024_01611_3 crossref_primary_10_2147_JIR_S385977 crossref_primary_10_1155_2022_7449941 crossref_primary_10_3390_biology10010035 crossref_primary_10_1146_annurev_cancerbio_030518_055844 crossref_primary_10_1080_14728222_2022_2032651 crossref_primary_10_3724_zdxbyxb_2024_0566 crossref_primary_10_1038_s41418_017_0053_8 crossref_primary_10_1016_j_biopha_2025_117932 crossref_primary_10_1016_j_bbamcr_2023_119535 crossref_primary_10_1016_j_neo_2017_10_005 crossref_primary_10_1038_s41419_022_04770_4 crossref_primary_10_1007_s12094_024_03754_4 crossref_primary_10_1155_dth_1133166 crossref_primary_10_2147_IJGM_S388537 crossref_primary_10_3390_ijms20123000 crossref_primary_10_1155_2022_1792894 crossref_primary_10_1039_c9mt00090a crossref_primary_10_3389_fphar_2020_01061 crossref_primary_10_3390_brainsci13101367 crossref_primary_10_1016_j_prp_2023_154492 crossref_primary_10_3389_fcell_2021_712230 crossref_primary_10_1016_j_ijpharm_2024_124517 crossref_primary_10_1159_000510083 crossref_primary_10_1038_s41419_023_06154_8 crossref_primary_10_1016_j_ymthe_2021_03_022 crossref_primary_10_3389_fcell_2021_735013 crossref_primary_10_1007_s00204_023_03625_x crossref_primary_10_1016_j_arr_2023_102142 crossref_primary_10_1139_bcb_2023_0018 crossref_primary_10_1152_physrev_00031_2024 crossref_primary_10_1038_s44324_024_00045_y crossref_primary_10_1016_j_arres_2022_100059 crossref_primary_10_1038_s41419_023_06045_y crossref_primary_10_3748_wjg_v29_i4_616 crossref_primary_10_1038_s41420_021_00473_5 crossref_primary_10_1016_j_ceramint_2024_01_024 crossref_primary_10_1038_s41418_021_00859_z crossref_primary_10_3390_cells12060867 crossref_primary_10_1016_j_canlet_2023_216147 crossref_primary_10_3389_fgene_2023_1117713 crossref_primary_10_3390_antiox12040918 crossref_primary_10_3389_fcell_2021_728172 crossref_primary_10_1371_journal_pone_0175796 crossref_primary_10_1080_15548627_2020_1810918 crossref_primary_10_1016_j_chembiol_2020_02_005 crossref_primary_10_1038_s41420_023_01606_8 crossref_primary_10_2174_1566524023666230913105735 crossref_primary_10_1016_j_arres_2022_100048 crossref_primary_10_3389_fonc_2023_999688 crossref_primary_10_1016_j_bbamcr_2020_118805 crossref_primary_10_3389_fphys_2024_1450656 crossref_primary_10_1039_D0RA04896H crossref_primary_10_3390_cells12071050 crossref_primary_10_3390_ph14101045 crossref_primary_10_3390_ijms241713336 crossref_primary_10_1016_j_biopha_2024_117407 crossref_primary_10_3389_fphar_2022_1020918 crossref_primary_10_1016_j_biopha_2023_114993 crossref_primary_10_3389_fnins_2020_00267 crossref_primary_10_1016_j_semcancer_2019_03_002 crossref_primary_10_1016_j_jtcme_2022_10_007 crossref_primary_10_1089_ars_2018_7502 crossref_primary_10_1158_1078_0432_CCR_22_0470 crossref_primary_10_3390_life11030222 crossref_primary_10_1073_pnas_1908271116 crossref_primary_10_1016_j_biopha_2022_113516 crossref_primary_10_1093_lifemeta_loac035 crossref_primary_10_3389_fonc_2022_861834 crossref_primary_10_1016_j_expneurol_2024_114961 crossref_primary_10_3389_fonc_2021_713721 crossref_primary_10_3390_antiox9030205 crossref_primary_10_1038_s41401_021_00814_1 crossref_primary_10_1158_1541_7786_MCR_22_0163 crossref_primary_10_1038_s41598_018_23305_6 crossref_primary_10_1155_2020_9738143 crossref_primary_10_3390_biology10020083 crossref_primary_10_1007_s10522_025_10211_4 crossref_primary_10_1093_cvr_cvae270 crossref_primary_10_15212_bioi_2020_0039 crossref_primary_10_1016_j_jhazmat_2023_131908 crossref_primary_10_1074_jbc_M117_789800 crossref_primary_10_1080_10715762_2019_1666983 crossref_primary_10_1038_s41419_023_05978_8 crossref_primary_10_1152_ajpcell_00148_2022 crossref_primary_10_1016_j_bbrc_2019_10_006 crossref_primary_10_1038_s41419_021_04490_1 crossref_primary_10_1016_j_lfs_2022_120704 crossref_primary_10_1186_s12943_020_01157_x crossref_primary_10_1002_ange_202300379 crossref_primary_10_51755_turkvetj_1078397 crossref_primary_10_3389_fcell_2021_649045 crossref_primary_10_1089_ars_2022_0179 crossref_primary_10_1016_j_biopha_2021_111472 crossref_primary_10_1080_1040841X_2024_2340643 crossref_primary_10_3390_cells11203301 crossref_primary_10_3892_ijmm_2024_5457 crossref_primary_10_7717_peerj_11627 crossref_primary_10_1007_s00775_018_1538_8 crossref_primary_10_1158_0008_5472_CAN_20_2017 crossref_primary_10_3390_biology10020151 crossref_primary_10_1002_cbin_11705 crossref_primary_10_1007_s10495_023_01890_w crossref_primary_10_1038_s41419_021_03559_1 crossref_primary_10_3389_fcell_2021_719187 crossref_primary_10_1186_s12890_023_02410_x crossref_primary_10_1016_j_aca_2024_342811 crossref_primary_10_3389_fphar_2022_879317 crossref_primary_10_1016_j_biopha_2021_112423 crossref_primary_10_1016_j_biopha_2023_115419 crossref_primary_10_1021_acscentsci_0c01592 crossref_primary_10_1089_ars_2020_8175 crossref_primary_10_1007_s12551_023_01126_w crossref_primary_10_1186_s40001_024_01822_7 crossref_primary_10_1016_j_abb_2022_109199 crossref_primary_10_1007_s12265_024_10539_1 crossref_primary_10_1016_j_bbrc_2019_11_187 crossref_primary_10_1080_10715762_2020_1780229 crossref_primary_10_3390_cancers13184576 crossref_primary_10_1097_MD_0000000000041218 crossref_primary_10_12677_ACM_2023_13122860 crossref_primary_10_3390_antiox10081160 crossref_primary_10_1016_j_arr_2023_102063 crossref_primary_10_3389_fonc_2020_586530 crossref_primary_10_3390_cancers12010164 crossref_primary_10_3390_ijms22115652 crossref_primary_10_1016_j_bbrc_2016_08_124 crossref_primary_10_3389_fonc_2022_948389 crossref_primary_10_3390_ijms24032887 crossref_primary_10_3389_fonc_2022_1023040 crossref_primary_10_1016_j_chembiol_2020_03_011 crossref_primary_10_1002_adma_201704007 crossref_primary_10_1007_s00432_018_2740_3 crossref_primary_10_1016_j_acuroe_2022_06_001 crossref_primary_10_1016_j_taap_2023_116440 crossref_primary_10_1097_HEP_0000000000000390 crossref_primary_10_1016_j_biopha_2021_112223 crossref_primary_10_1021_acs_jafc_4c00931 crossref_primary_10_1017_S0954422421000226 crossref_primary_10_1016_j_bcp_2021_114584 crossref_primary_10_1016_j_freeradbiomed_2018_10_426 crossref_primary_10_3389_fmolb_2022_917602 crossref_primary_10_2174_1386207325666220823122942 crossref_primary_10_1039_C8BM01525B crossref_primary_10_1002_1873_3468_14277 crossref_primary_10_1016_j_bmc_2023_117564 crossref_primary_10_3390_cells13181541 crossref_primary_10_1038_s41420_021_00468_2 crossref_primary_10_31083_j_jin2306113 crossref_primary_10_1002_cbin_11804 crossref_primary_10_1016_j_acuro_2021_12_006 crossref_primary_10_3389_fcvm_2021_710963 crossref_primary_10_1016_j_isci_2024_110622 crossref_primary_10_1038_s41388_023_02703_9 crossref_primary_10_1038_s41419_020_2298_2 crossref_primary_10_3892_ol_2019_10568 crossref_primary_10_3390_ijms25189947 crossref_primary_10_1016_j_biopha_2022_112747 crossref_primary_10_1016_j_ejphar_2021_174319 crossref_primary_10_1016_j_canlet_2018_04_021 crossref_primary_10_1186_s12943_024_02132_6 crossref_primary_10_3389_fcell_2021_637162 crossref_primary_10_3389_fcell_2021_670184 crossref_primary_10_2217_fon_2020_0362 crossref_primary_10_1155_2023_6653202 crossref_primary_10_1016_j_lfs_2021_119799 crossref_primary_10_1161_ATVBAHA_123_319518 crossref_primary_10_1016_j_freeradbiomed_2018_04_569 crossref_primary_10_3389_fimmu_2023_1140791 crossref_primary_10_1038_s41419_022_04628_9 crossref_primary_10_3892_mmr_2022_12773 crossref_primary_10_7717_peerj_7435 |
| Cites_doi | 10.1038/nchembio.2079 10.1016/j.drudis.2014.05.001 10.4161/cc.22376 10.1038/nature14344 10.1074/jbc.C700107200 10.1038/cdd.2016.25 10.1083/jcb.200911078 10.1016/j.tcb.2015.10.014 10.1016/j.cmet.2008.07.005 10.1016/j.bbrc.2016.03.052 10.1084/jem.20140857 10.1038/cdd.2015.158 10.1073/pnas.1313198110 10.1016/j.freeradbiomed.2015.03.014 10.1038/nrm3909 10.1080/23723556.2015.1054549 10.1038/nature05859 10.1038/ncomms4962 10.1002/hep.28251 10.1146/annurev.nutr.28.061807.155521 10.1038/nature04512 10.1016/j.cell.2012.03.042 10.1152/ajpendo.00424.2003 10.1038/nm.2899 10.1073/pnas.1502960112 10.1038/onc.2015.32 10.1073/pnas.0701078104 10.1021/ja411006a 10.1002/hep.28574 10.1182/blood-2015-06-654194 10.1073/pnas.1109986108 10.1016/j.bbamcr.2014.10.014 10.1074/jbc.M109.032839 10.2174/092986711796504600 10.1016/j.cell.2013.12.010 10.1073/pnas.0707189104 10.2337/db15-1323 10.3390/biom5020808 10.1016/j.neuint.2011.05.006 10.1038/ncb3064 10.1038/nchembio.1416 10.1371/journal.pone.0139699 |
| ContentType | Journal Article |
| Copyright | 2016 Elsevier Inc. Copyright © 2016 Elsevier Inc. All rights reserved. |
| Copyright_xml | – notice: 2016 Elsevier Inc. – notice: Copyright © 2016 Elsevier Inc. All rights reserved. |
| DBID | AAYXX CITATION CGR CUY CVF ECM EIF NPM 7X8 7S9 L.6 |
| DOI | 10.1016/j.bbrc.2016.08.034 |
| DatabaseName | CrossRef Medline MEDLINE MEDLINE (Ovid) MEDLINE MEDLINE PubMed MEDLINE - Academic AGRICOLA AGRICOLA - Academic |
| DatabaseTitle | CrossRef MEDLINE Medline Complete MEDLINE with Full Text PubMed MEDLINE (Ovid) MEDLINE - Academic AGRICOLA AGRICOLA - Academic |
| DatabaseTitleList | MEDLINE AGRICOLA MEDLINE - Academic |
| 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 Chemistry Biology |
| EISSN | 1090-2104 |
| EndPage | 844 |
| ExternalDocumentID | 27510639 10_1016_j_bbrc_2016_08_034 S0006291X1631289X |
| Genre | Research Support, Non-U.S. Gov't Journal Article Research Support, N.I.H., Extramural |
| GrantInformation_xml | – fundername: NIGMS NIH HHS grantid: R01 GM115366 – fundername: NCI NIH HHS grantid: R01 CA160417 |
| GroupedDBID | --- --K --M -~X .~1 0R~ 1B1 1RT 1~. 1~5 23N 4.4 457 4G. 53G 5GY 5VS 6J9 7-5 71M 8P~ 9JM AABNK AACTN AAEDT AAEDW AAIAV AAIKJ AAKOC AALRI AAOAW AAQFI AAXUO ABFNM ABFRF ABGSF ABJNI ABMAC ABUDA ABYKQ ACDAQ ACGFO ACGFS ACNCT ACRLP ADBBV ADEZE ADUVX AEBSH AEFWE AEHWI AEKER AENEX AFFNX AFKWA AFTJW AFXIZ AGHFR AGUBO AGYEJ AIEXJ AIKHN AITUG AJBFU AJOXV ALMA_UNASSIGNED_HOLDINGS AMFUW AMRAJ AXJTR BKOJK BLXMC CS3 D0L DM4 DOVZS EBS EFBJH EFLBG EJD EO8 EO9 EP2 EP3 F5P FDB FIRID FNPLU FYGXN G-Q GBLVA IHE J1W K-O KOM L7B LG5 LX2 M41 MO0 N9A O-L O9- OAUVE OZT P-8 P-9 P2P PC. Q38 RIG RNS ROL RPZ SCC SDF SDG SDP SES SPCBC SSU SSZ T5K TWZ WH7 XPP XSW ZA5 ZMT ~02 ~G- .55 .GJ .HR 1CY 3O- 9M8 AAHBH AAQXK AATTM AAXKI AAYJJ AAYWO AAYXX ABDPE ABEFU ABWVN ABXDB ACKIV ACRPL ACVFH ADCNI ADFGL ADIYS ADMUD ADNMO AEIPS AEUPX AFJKZ AFPUW AGCQF AGQPQ AGRDE AGRNS AHHHB AIGII AIIUN AKBMS AKRWK AKYEP ANKPU APXCP ASPBG AVWKF AZFZN BNPGV CAG CITATION COF FEDTE FGOYB G-2 HLW HVGLF HZ~ MVM OHT R2- SBG SEW SSH UQL WUQ X7M Y6R ZGI ZKB ~KM CGR CUY CVF ECM EIF NPM 7X8 7S9 L.6 |
| ID | FETCH-LOGICAL-c455t-9842c5aa4b805738991ca3629933225ca19526da2e8ca4db32733220de2f2e2b3 |
| IEDL.DBID | .~1 |
| ISSN | 0006-291X |
| IngestDate | Thu Jul 10 22:22:35 EDT 2025 Thu Jul 10 18:06:16 EDT 2025 Wed Feb 19 02:40:52 EST 2025 Tue Jul 01 03:10:14 EDT 2025 Thu Apr 24 23:05:18 EDT 2025 Fri Feb 23 02:30:56 EST 2024 |
| IsPeerReviewed | true |
| IsScholarly | true |
| Issue | 2 |
| Keywords | Iron-sulfur proteins GPX4 IRP CISD1 Lipid peroxidation Q-PCR Ferroptosis HCC MDA DFO Mitochondria Fe2 NRF2 ΔΨm ROS VDACs CCK-8 GSH |
| Language | English |
| License | Copyright © 2016 Elsevier Inc. All rights reserved. |
| LinkModel | DirectLink |
| MergedId | FETCHMERGED-LOGICAL-c455t-9842c5aa4b805738991ca3629933225ca19526da2e8ca4db32733220de2f2e2b3 |
| Notes | ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 |
| PMID | 27510639 |
| PQID | 1814662759 |
| PQPubID | 23479 |
| PageCount | 7 |
| ParticipantIDs | proquest_miscellaneous_2101345004 proquest_miscellaneous_1814662759 pubmed_primary_27510639 crossref_citationtrail_10_1016_j_bbrc_2016_08_034 crossref_primary_10_1016_j_bbrc_2016_08_034 elsevier_sciencedirect_doi_10_1016_j_bbrc_2016_08_034 |
| ProviderPackageCode | CITATION AAYXX |
| PublicationCentury | 2000 |
| PublicationDate | 2016-09-16 |
| PublicationDateYYYYMMDD | 2016-09-16 |
| PublicationDate_xml | – month: 09 year: 2016 text: 2016-09-16 day: 16 |
| PublicationDecade | 2010 |
| PublicationPlace | United States |
| PublicationPlace_xml | – name: United States |
| PublicationTitle | Biochemical and biophysical research communications |
| PublicationTitleAlternate | Biochem Biophys Res Commun |
| PublicationYear | 2016 |
| Publisher | Elsevier Inc |
| Publisher_xml | – name: Elsevier Inc |
| References | Wiley, Murphy, Ross, van der Geer, Dixon (bib13) 2007; 104 Kusminski, Chen, Ye, Sun, Wang, Spurgin, Sanders, Brozinick, Geldenhuys, Li, Unger, Scherer (bib18) 2016; 65 Faine, Rudnicki, Cesar, Heras, Bosca, Souza, Hernandes, Galdino, Lima, Pitta, Abdalla (bib46) 2011; 18 Xie, Hou, Song, Yu, Huang, Sun, Kang, Tang (bib3) 2016; 23 Dixon, Stockwell (bib30) 2014; 10 Xie, Hou, Song, Yu, Huang, Sun, Kang, Tang (bib27) 2016; 23 Bai, Morcos, Sohn, Darash-Yahana, Rezende, Lipper, Paddock, Song, Luo, Holt, Tamir, Theodorakis, Jennings, Onuchic, Mittler, Nechushtai (bib20) 2015; 112 Hou, Xie, Song, Sun, Lotze, Zeh, Kang, Tang (bib45) 2016 Wiley, Paddock, Abresch, Gross, van der Geer, Nechushtai, Murphy, Jennings, Dixon (bib15) 2007; 282 Rouault (bib29) 2015; 16 Yagoda, von Rechenberg, Zaganjor, Bauer, Yang, Fridman, Wolpaw, Smukste, Peltier, Boniface, Smith, Lessnick, Sahasrabudhe, Stockwell (bib38) 2007; 447 Navarro, Botella, Metzendorf, Lind, Schneuwly (bib35) 2015; 85 Skouta, Dixon, Wang, Dunn, Orman, Shimada, Rosenberg, Lo, Weinberg, Linkermann, Stockwell (bib37) 2014; 136 Shaw, Cope, Li, Corson, Hersey, Ackermann, Gwynn, Lambert, Wingert, Traver, Trede, Barut, Zhou, Minet, Donovan, Brownlie, Balzan, Weiss, Peters, Kaplan, Zon, Paw (bib33) 2006; 440 Xie, Song, Sun, Huang, Zhong, Lotze, Zeh, Kang, Tang (bib25) 2016; 473 Stehling, Lill (bib32) 2013; 3 Sohn, Tamir, Song, Michaeli, Matouk, Conlan, Harir, Holt, Shulaev, Paddock, Hochberg, Cabanchick, Onuchic, Jennings, Nechushtai, Mittler (bib21) 2013; 110 Yang, Stockwell (bib26) 2016; 26 Friedmann Angeli, Schneider, Proneth, Tyurina, Tyurin, Hammond, Herbach, Aichler, Walch, Eggenhofer, Basavarajappa, Radmark, Kobayashi, Seibt, Beck, Neff, Esposito, Wanke, Forster, Yefremova, Heinrichmeyer, Bornkamm, Geissler, Thomas, Stockwell, O'Donnell, Kagan, Schick, Conrad (bib6) 2014; 16 Tamir, Paddock, Darash-Yahana-Baram, Holt, Sohn, Agranat, Michaeli, Stofleth, Lipper, Morcos, Cabantchik, Onuchic, Jennings, Mittler, Nechushtai (bib16) 2015; 1853 Sun, Ou, Chen, Niu, Chen, Kang, Tang (bib44) 2016; 63 Yang, Stockwell (bib4) 2016; 26 Kusminski, Holland, Sun, Park, Spurgin, Lin, Askew, Simcox, McClain, Li, Scherer (bib17) 2012; 18 Kusminski, Park, Scherer (bib19) 2014; 5 Seiler, Schneider, Forster, Roth, Wirth, Culmsee, Plesnila, Kremmer, Radmark, Wurst, Bornkamm, Schweizer, Conrad (bib41) 2008; 8 Sun, Niu, Chen, He, Chen, Kang, Tang (bib43) 2016; 64 Yang, SriRamaratnam, Welsch, Shimada, Skouta, Viswanathan, Cheah, Clemons, Shamji, Clish, Brown, Girotti, Cornish, Schreiber, Stockwell (bib5) 2014; 156 Shimada, Skouta, Kaplan, Yang, Hayano, Dixon, Brown, Valenzuela, Wolpaw, Stockwell (bib9) 2016; 12 Carroll, Zeissler, Chadborn, Gibson, Williams, Zajicek, Morrison, Hanemann (bib36) 2011; 59 Liang, Yoo, Na, Walter, Richardson, Ran (bib40) 2009; 284 Lipper, Paddock, Onuchic, Mittler, Nechushtai, Jennings (bib22) 2015; 10 Yu, Xie, Cao, Yang, Yang, Lotze, Zeh, Kang, Tang (bib8) 2015; 2 Zuris, Harir, Conlan, Shvartsman, Michaeli, Tamir, Paddock, Onuchic, Mittler, Cabantchik, Jennings, Nechushtai (bib28) 2011; 108 Sun, Ou, Xie, Kang, Fan, Niu, Wang, Cao, Tang (bib10) 2015; 34 Salem, Whitaker-Menezes, Howell, Sotgia, Lisanti (bib23) 2012; 11 Canli, Alankus, Grootjans, Vegi, Hultner, Hoppe, Schroeder, Vandenabeele, Bornkamm, Greten (bib42) 2016; 127 Paddock, Wiley, Axelrod, Cohen, Roy, Abresch, Capraro, Murphy, Nechushtai, Dixon, Jennings (bib14) 2007; 104 Dixon, Lemberg, Lamprecht, Skouta, Zaitsev, Gleason, Patel, Bauer, Cantley, Yang, Morrison, Stockwell (bib1) 2012; 149 Muckenthaler, Galy, Hentze (bib31) 2008; 28 Jiang, Kon, Li, Wang, Su, Hibshoosh, Baer, Gu (bib2) 2015; 520 Geldenhuys, Leeper, Carroll (bib11) 2014; 19 Tang, Kang, Livesey, Cheh, Farkas, Loughran, Hoppe, Bianchi, Tracey, Zeh, Lotze (bib24) 2010; 190 Bresgen, Eckl (bib34) 2015; 5 Magtanong, Ko, Dixon (bib39) 2016; 23 Matsushita, Freigang, Schneider, Conrad, Bornkamm, Kopf (bib7) 2015; 212 Colca, McDonald, Waldon, Leone, Lull, Bannow, Lund, Mathews (bib12) 2004; 286 Yu (10.1016/j.bbrc.2016.08.034_bib8) 2015; 2 Geldenhuys (10.1016/j.bbrc.2016.08.034_bib11) 2014; 19 Lipper (10.1016/j.bbrc.2016.08.034_bib22) 2015; 10 Tang (10.1016/j.bbrc.2016.08.034_bib24) 2010; 190 Xie (10.1016/j.bbrc.2016.08.034_bib27) 2016; 23 Sun (10.1016/j.bbrc.2016.08.034_bib43) 2016; 64 Bresgen (10.1016/j.bbrc.2016.08.034_bib34) 2015; 5 Muckenthaler (10.1016/j.bbrc.2016.08.034_bib31) 2008; 28 Tamir (10.1016/j.bbrc.2016.08.034_bib16) 2015; 1853 Faine (10.1016/j.bbrc.2016.08.034_bib46) 2011; 18 Yang (10.1016/j.bbrc.2016.08.034_bib26) 2016; 26 Shimada (10.1016/j.bbrc.2016.08.034_bib9) 2016; 12 Kusminski (10.1016/j.bbrc.2016.08.034_bib19) 2014; 5 Zuris (10.1016/j.bbrc.2016.08.034_bib28) 2011; 108 Sohn (10.1016/j.bbrc.2016.08.034_bib21) 2013; 110 Matsushita (10.1016/j.bbrc.2016.08.034_bib7) 2015; 212 Colca (10.1016/j.bbrc.2016.08.034_bib12) 2004; 286 Bai (10.1016/j.bbrc.2016.08.034_bib20) 2015; 112 Carroll (10.1016/j.bbrc.2016.08.034_bib36) 2011; 59 Yagoda (10.1016/j.bbrc.2016.08.034_bib38) 2007; 447 Xie (10.1016/j.bbrc.2016.08.034_bib3) 2016; 23 Friedmann Angeli (10.1016/j.bbrc.2016.08.034_bib6) 2014; 16 Xie (10.1016/j.bbrc.2016.08.034_bib25) 2016; 473 Yang (10.1016/j.bbrc.2016.08.034_bib4) 2016; 26 Navarro (10.1016/j.bbrc.2016.08.034_bib35) 2015; 85 Seiler (10.1016/j.bbrc.2016.08.034_bib41) 2008; 8 Hou (10.1016/j.bbrc.2016.08.034_bib45) 2016 Kusminski (10.1016/j.bbrc.2016.08.034_bib18) 2016; 65 Paddock (10.1016/j.bbrc.2016.08.034_bib14) 2007; 104 Wiley (10.1016/j.bbrc.2016.08.034_bib13) 2007; 104 Kusminski (10.1016/j.bbrc.2016.08.034_bib17) 2012; 18 Dixon (10.1016/j.bbrc.2016.08.034_bib30) 2014; 10 Yang (10.1016/j.bbrc.2016.08.034_bib5) 2014; 156 Skouta (10.1016/j.bbrc.2016.08.034_bib37) 2014; 136 Dixon (10.1016/j.bbrc.2016.08.034_bib1) 2012; 149 Sun (10.1016/j.bbrc.2016.08.034_bib44) 2016; 63 Sun (10.1016/j.bbrc.2016.08.034_bib10) 2015; 34 Shaw (10.1016/j.bbrc.2016.08.034_bib33) 2006; 440 Jiang (10.1016/j.bbrc.2016.08.034_bib2) 2015; 520 Liang (10.1016/j.bbrc.2016.08.034_bib40) 2009; 284 Wiley (10.1016/j.bbrc.2016.08.034_bib15) 2007; 282 Magtanong (10.1016/j.bbrc.2016.08.034_bib39) 2016; 23 Stehling (10.1016/j.bbrc.2016.08.034_bib32) 2013; 3 Salem (10.1016/j.bbrc.2016.08.034_bib23) 2012; 11 Canli (10.1016/j.bbrc.2016.08.034_bib42) 2016; 127 Rouault (10.1016/j.bbrc.2016.08.034_bib29) 2015; 16 |
| References_xml | – volume: 19 start-page: 1601 year: 2014 end-page: 1606 ident: bib11 article-title: mitoNEET as a novel drug target for mitochondrial dysfunction publication-title: Drug Discov. Today – volume: 34 start-page: 5617 year: 2015 end-page: 5625 ident: bib10 article-title: HSPB1 as a novel regulator of ferroptotic cancer cell death publication-title: Oncogene – volume: 85 start-page: 71 year: 2015 end-page: 82 ident: bib35 article-title: Mitoferrin modulates iron toxicity in a Drosophila model of Friedreich's ataxia publication-title: Free Radic. Biol. Med. – volume: 26 start-page: 165 year: 2016 end-page: 176 ident: bib4 article-title: Ferroptosis: death by lipid peroxidation publication-title: Trends Cell Biol. – volume: 18 start-page: 3351 year: 2011 end-page: 3360 ident: bib46 article-title: Anti-inflammatory and antioxidant properties of a new arylidene-thiazolidinedione in macrophages publication-title: Curr. Med. Chem. – volume: 149 start-page: 1060 year: 2012 end-page: 1072 ident: bib1 article-title: Ferroptosis: an iron-dependent form of nonapoptotic cell death publication-title: Cell – volume: 282 start-page: 23745 year: 2007 end-page: 23749 ident: bib15 article-title: The outer mitochondrial membrane protein mitoNEET contains a novel redox-active 2Fe-2S cluster publication-title: J. Biol. Chem. – volume: 26 start-page: 165 year: 2016 end-page: 176 ident: bib26 article-title: Ferroptosis: Death by Lipid Peroxidation publication-title: Trends Cell Biol. – volume: 23 start-page: 369 year: 2016 end-page: 379 ident: bib27 article-title: Ferroptosis: process and function publication-title: Cell Death Differ. – start-page: 1 year: 2016 end-page: 4 ident: bib45 article-title: Autophagy promotes ferroptosis by degradation of ferritin publication-title: Autophagy – volume: 28 start-page: 197 year: 2008 end-page: 213 ident: bib31 article-title: Systemic iron homeostasis and the iron-responsive element/iron-regulatory protein (IRE/IRP) regulatory network publication-title: Annu. Rev. Nutr. – volume: 104 start-page: 14342 year: 2007 end-page: 14347 ident: bib14 article-title: MitoNEET is a uniquely folded 2Fe 2S outer mitochondrial membrane protein stabilized by pioglitazone publication-title: Proc. Natl. Acad. Sci. U. S. A. – volume: 104 start-page: 5318 year: 2007 end-page: 5323 ident: bib13 article-title: MitoNEET is an iron-containing outer mitochondrial membrane protein that regulates oxidative capacity publication-title: Proc. Natl. Acad. Sci. U. S. A. – volume: 156 start-page: 317 year: 2014 end-page: 331 ident: bib5 article-title: Regulation of ferroptotic cancer cell death by GPX4 publication-title: Cell – volume: 447 start-page: 864 year: 2007 end-page: 868 ident: bib38 article-title: RAS-RAF-MEK-dependent oxidative cell death involving voltage-dependent anion channels publication-title: Nature – volume: 1853 start-page: 1294 year: 2015 end-page: 1315 ident: bib16 article-title: Structure-function analysis of NEET proteins uncovers their role as key regulators of iron and ROS homeostasis in health and disease publication-title: Biochim. Biophys. Acta – volume: 136 start-page: 4551 year: 2014 end-page: 4556 ident: bib37 article-title: Ferrostatins inhibit oxidative lipid damage and cell death in diverse disease models publication-title: J. Am. Chem. Soc. – volume: 8 start-page: 237 year: 2008 end-page: 248 ident: bib41 article-title: Glutathione peroxidase 4 senses and translates oxidative stress into 12/15-lipoxygenase dependent- and AIF-mediated cell death publication-title: Cell Metab. – volume: 108 start-page: 13047 year: 2011 end-page: 13052 ident: bib28 article-title: Facile transfer of [2Fe-2S] clusters from the diabetes drug target mitoNEET to an apo-acceptor protein publication-title: Proc. Natl. Acad. Sci. U. S. A. – volume: 5 start-page: 808 year: 2015 end-page: 847 ident: bib34 article-title: Oxidative stress and the homeodynamics of iron metabolism publication-title: Biomolecules – volume: 18 start-page: 1539 year: 2012 end-page: 1549 ident: bib17 article-title: MitoNEET-driven alterations in adipocyte mitochondrial activity reveal a crucial adaptive process that preserves insulin sensitivity in obesity publication-title: Nat. Med. – volume: 16 start-page: 1180 year: 2014 end-page: 1191 ident: bib6 article-title: Inactivation of the ferroptosis regulator Gpx4 triggers acute renal failure in mice publication-title: Nat. Cell Biol. – volume: 212 start-page: 555 year: 2015 end-page: 568 ident: bib7 article-title: T cell lipid peroxidation induces ferroptosis and prevents immunity to infection publication-title: J. Exp. Med. – volume: 10 start-page: e0139699 year: 2015 ident: bib22 article-title: Cancer-Related NEET proteins transfer 2Fe-2S clusters to anamorsin, a protein required for cytosolic iron-sulfur cluster biogenesis publication-title: PLoS One – volume: 23 start-page: 369 year: 2016 end-page: 379 ident: bib3 article-title: Ferroptosis: process and function publication-title: Cell Death Differ. – volume: 127 start-page: 139 year: 2016 end-page: 148 ident: bib42 article-title: Glutathione peroxidase 4 prevents necroptosis in mouse erythroid precursors publication-title: Blood – volume: 11 start-page: 4174 year: 2012 end-page: 4180 ident: bib23 article-title: Mitochondrial biogenesis in epithelial cancer cells promotes breast cancer tumor growth and confers autophagy resistance publication-title: Cell Cycle – volume: 59 start-page: 73 year: 2011 end-page: 80 ident: bib36 article-title: Changes in iron-regulatory gene expression occur in human cell culture models of Parkinson's disease publication-title: Neurochem. Int. – volume: 64 start-page: 488 year: 2016 end-page: 500 ident: bib43 article-title: Metallothionein-1G facilitates sorafenib resistance through inhibition of ferroptosis publication-title: Hepatology – volume: 440 start-page: 96 year: 2006 end-page: 100 ident: bib33 article-title: Mitoferrin is essential for erythroid iron assimilation publication-title: Nature – volume: 190 start-page: 881 year: 2010 end-page: 892 ident: bib24 article-title: Endogenous HMGB1 regulates autophagy publication-title: J. Cell Biol. – volume: 473 start-page: 775 year: 2016 end-page: 780 ident: bib25 article-title: Identification of baicalein as a ferroptosis inhibitor by natural product library screening publication-title: Biochem. Biophys. Res. Commun. – volume: 110 start-page: 14676 year: 2013 end-page: 14681 ident: bib21 article-title: NAF-1 and mitoNEET are central to human breast cancer proliferation by maintaining mitochondrial homeostasis and promoting tumor growth publication-title: Proc. Natl. Acad. Sci. U. S. A. – volume: 12 start-page: 497 year: 2016 end-page: 503 ident: bib9 article-title: Global survey of cell death mechanisms reveals metabolic regulation of ferroptosis publication-title: Nat. Chem. Biol. – volume: 65 start-page: 1534 year: 2016 end-page: 1555 ident: bib18 article-title: MitoNEET-parkin effects in pancreatic alpha- and beta-cells, cellular survival, and intrainsular cross talk publication-title: Diabetes – volume: 23 start-page: 1099 year: 2016 end-page: 1109 ident: bib39 article-title: Emerging roles for lipids in non-apoptotic cell death publication-title: Cell Death Differ. – volume: 284 start-page: 30836 year: 2009 end-page: 30844 ident: bib40 article-title: Short form glutathione peroxidase 4 is the essential isoform required for survival and somatic mitochondrial functions publication-title: J. Biol. Chem. – volume: 112 start-page: 3698 year: 2015 end-page: 3703 ident: bib20 article-title: The Fe-S cluster-containing NEET proteins mitoNEET and NAF-1 as chemotherapeutic targets in breast cancer publication-title: Proc. Natl. Acad. Sci. U. S. A. – volume: 520 start-page: 57 year: 2015 end-page: 62 ident: bib2 article-title: Ferroptosis as a p53-mediated activity during tumour suppression publication-title: Nature – volume: 2 start-page: e1054549 year: 2015 ident: bib8 article-title: The ferroptosis inducer erastin enhances sensitivity of acute myeloid leukemia cells to chemotherapeutic agents publication-title: Mol. Cell Oncol. – volume: 286 start-page: E252 year: 2004 end-page: E260 ident: bib12 article-title: Identification of a novel mitochondrial protein (“mitoNEET”) cross-linked specifically by a thiazolidinedione photoprobe publication-title: Am. J. Physiol. Endocrinol. Metab. – volume: 16 start-page: 45 year: 2015 end-page: 55 ident: bib29 article-title: Mammalian iron-sulphur proteins: novel insights into biogenesis and function publication-title: Nat. Rev. Mol. Cell Biol. – volume: 10 start-page: 9 year: 2014 end-page: 17 ident: bib30 article-title: The role of iron and reactive oxygen species in cell death publication-title: Nat. Chem. Biol. – volume: 63 start-page: 173 year: 2016 end-page: 184 ident: bib44 article-title: Activation of the p62-Keap1-NRF2 pathway protects against ferroptosis in hepatocellular carcinoma cells publication-title: Hepatology – volume: 3 start-page: 1 year: 2013 end-page: 17 ident: bib32 article-title: The role of mitochondria in cellular iron-sulfur protein biogenesis: mechanisms, connected processes, and diseases publication-title: Cold Spring Harb. Perspect. Med. – volume: 5 start-page: 3962 year: 2014 ident: bib19 article-title: MitoNEET-mediated effects on browning of white adipose tissue publication-title: Nat. Commun. – volume: 12 start-page: 497 year: 2016 ident: 10.1016/j.bbrc.2016.08.034_bib9 article-title: Global survey of cell death mechanisms reveals metabolic regulation of ferroptosis publication-title: Nat. Chem. Biol. doi: 10.1038/nchembio.2079 – volume: 19 start-page: 1601 year: 2014 ident: 10.1016/j.bbrc.2016.08.034_bib11 article-title: mitoNEET as a novel drug target for mitochondrial dysfunction publication-title: Drug Discov. Today doi: 10.1016/j.drudis.2014.05.001 – volume: 11 start-page: 4174 year: 2012 ident: 10.1016/j.bbrc.2016.08.034_bib23 article-title: Mitochondrial biogenesis in epithelial cancer cells promotes breast cancer tumor growth and confers autophagy resistance publication-title: Cell Cycle doi: 10.4161/cc.22376 – volume: 520 start-page: 57 year: 2015 ident: 10.1016/j.bbrc.2016.08.034_bib2 article-title: Ferroptosis as a p53-mediated activity during tumour suppression publication-title: Nature doi: 10.1038/nature14344 – volume: 282 start-page: 23745 year: 2007 ident: 10.1016/j.bbrc.2016.08.034_bib15 article-title: The outer mitochondrial membrane protein mitoNEET contains a novel redox-active 2Fe-2S cluster publication-title: J. Biol. Chem. doi: 10.1074/jbc.C700107200 – volume: 23 start-page: 1099 year: 2016 ident: 10.1016/j.bbrc.2016.08.034_bib39 article-title: Emerging roles for lipids in non-apoptotic cell death publication-title: Cell Death Differ. doi: 10.1038/cdd.2016.25 – volume: 190 start-page: 881 year: 2010 ident: 10.1016/j.bbrc.2016.08.034_bib24 article-title: Endogenous HMGB1 regulates autophagy publication-title: J. Cell Biol. doi: 10.1083/jcb.200911078 – volume: 26 start-page: 165 year: 2016 ident: 10.1016/j.bbrc.2016.08.034_bib26 article-title: Ferroptosis: Death by Lipid Peroxidation publication-title: Trends Cell Biol. doi: 10.1016/j.tcb.2015.10.014 – volume: 8 start-page: 237 year: 2008 ident: 10.1016/j.bbrc.2016.08.034_bib41 article-title: Glutathione peroxidase 4 senses and translates oxidative stress into 12/15-lipoxygenase dependent- and AIF-mediated cell death publication-title: Cell Metab. doi: 10.1016/j.cmet.2008.07.005 – start-page: 1 year: 2016 ident: 10.1016/j.bbrc.2016.08.034_bib45 article-title: Autophagy promotes ferroptosis by degradation of ferritin publication-title: Autophagy – volume: 473 start-page: 775 year: 2016 ident: 10.1016/j.bbrc.2016.08.034_bib25 article-title: Identification of baicalein as a ferroptosis inhibitor by natural product library screening publication-title: Biochem. Biophys. Res. Commun. doi: 10.1016/j.bbrc.2016.03.052 – volume: 212 start-page: 555 year: 2015 ident: 10.1016/j.bbrc.2016.08.034_bib7 article-title: T cell lipid peroxidation induces ferroptosis and prevents immunity to infection publication-title: J. Exp. Med. doi: 10.1084/jem.20140857 – volume: 23 start-page: 369 year: 2016 ident: 10.1016/j.bbrc.2016.08.034_bib3 article-title: Ferroptosis: process and function publication-title: Cell Death Differ. doi: 10.1038/cdd.2015.158 – volume: 110 start-page: 14676 year: 2013 ident: 10.1016/j.bbrc.2016.08.034_bib21 article-title: NAF-1 and mitoNEET are central to human breast cancer proliferation by maintaining mitochondrial homeostasis and promoting tumor growth publication-title: Proc. Natl. Acad. Sci. U. S. A. doi: 10.1073/pnas.1313198110 – volume: 85 start-page: 71 year: 2015 ident: 10.1016/j.bbrc.2016.08.034_bib35 article-title: Mitoferrin modulates iron toxicity in a Drosophila model of Friedreich's ataxia publication-title: Free Radic. Biol. Med. doi: 10.1016/j.freeradbiomed.2015.03.014 – volume: 16 start-page: 45 year: 2015 ident: 10.1016/j.bbrc.2016.08.034_bib29 article-title: Mammalian iron-sulphur proteins: novel insights into biogenesis and function publication-title: Nat. Rev. Mol. Cell Biol. doi: 10.1038/nrm3909 – volume: 2 start-page: e1054549 year: 2015 ident: 10.1016/j.bbrc.2016.08.034_bib8 article-title: The ferroptosis inducer erastin enhances sensitivity of acute myeloid leukemia cells to chemotherapeutic agents publication-title: Mol. Cell Oncol. doi: 10.1080/23723556.2015.1054549 – volume: 447 start-page: 864 year: 2007 ident: 10.1016/j.bbrc.2016.08.034_bib38 article-title: RAS-RAF-MEK-dependent oxidative cell death involving voltage-dependent anion channels publication-title: Nature doi: 10.1038/nature05859 – volume: 5 start-page: 3962 year: 2014 ident: 10.1016/j.bbrc.2016.08.034_bib19 article-title: MitoNEET-mediated effects on browning of white adipose tissue publication-title: Nat. Commun. doi: 10.1038/ncomms4962 – volume: 63 start-page: 173 year: 2016 ident: 10.1016/j.bbrc.2016.08.034_bib44 article-title: Activation of the p62-Keap1-NRF2 pathway protects against ferroptosis in hepatocellular carcinoma cells publication-title: Hepatology doi: 10.1002/hep.28251 – volume: 28 start-page: 197 year: 2008 ident: 10.1016/j.bbrc.2016.08.034_bib31 article-title: Systemic iron homeostasis and the iron-responsive element/iron-regulatory protein (IRE/IRP) regulatory network publication-title: Annu. Rev. Nutr. doi: 10.1146/annurev.nutr.28.061807.155521 – volume: 440 start-page: 96 year: 2006 ident: 10.1016/j.bbrc.2016.08.034_bib33 article-title: Mitoferrin is essential for erythroid iron assimilation publication-title: Nature doi: 10.1038/nature04512 – volume: 149 start-page: 1060 year: 2012 ident: 10.1016/j.bbrc.2016.08.034_bib1 article-title: Ferroptosis: an iron-dependent form of nonapoptotic cell death publication-title: Cell doi: 10.1016/j.cell.2012.03.042 – volume: 286 start-page: E252 year: 2004 ident: 10.1016/j.bbrc.2016.08.034_bib12 article-title: Identification of a novel mitochondrial protein (“mitoNEET”) cross-linked specifically by a thiazolidinedione photoprobe publication-title: Am. J. Physiol. Endocrinol. Metab. doi: 10.1152/ajpendo.00424.2003 – volume: 18 start-page: 1539 year: 2012 ident: 10.1016/j.bbrc.2016.08.034_bib17 article-title: MitoNEET-driven alterations in adipocyte mitochondrial activity reveal a crucial adaptive process that preserves insulin sensitivity in obesity publication-title: Nat. Med. doi: 10.1038/nm.2899 – volume: 112 start-page: 3698 year: 2015 ident: 10.1016/j.bbrc.2016.08.034_bib20 article-title: The Fe-S cluster-containing NEET proteins mitoNEET and NAF-1 as chemotherapeutic targets in breast cancer publication-title: Proc. Natl. Acad. Sci. U. S. A. doi: 10.1073/pnas.1502960112 – volume: 34 start-page: 5617 year: 2015 ident: 10.1016/j.bbrc.2016.08.034_bib10 article-title: HSPB1 as a novel regulator of ferroptotic cancer cell death publication-title: Oncogene doi: 10.1038/onc.2015.32 – volume: 104 start-page: 5318 year: 2007 ident: 10.1016/j.bbrc.2016.08.034_bib13 article-title: MitoNEET is an iron-containing outer mitochondrial membrane protein that regulates oxidative capacity publication-title: Proc. Natl. Acad. Sci. U. S. A. doi: 10.1073/pnas.0701078104 – volume: 136 start-page: 4551 year: 2014 ident: 10.1016/j.bbrc.2016.08.034_bib37 article-title: Ferrostatins inhibit oxidative lipid damage and cell death in diverse disease models publication-title: J. Am. Chem. Soc. doi: 10.1021/ja411006a – volume: 64 start-page: 488 year: 2016 ident: 10.1016/j.bbrc.2016.08.034_bib43 article-title: Metallothionein-1G facilitates sorafenib resistance through inhibition of ferroptosis publication-title: Hepatology doi: 10.1002/hep.28574 – volume: 127 start-page: 139 year: 2016 ident: 10.1016/j.bbrc.2016.08.034_bib42 article-title: Glutathione peroxidase 4 prevents necroptosis in mouse erythroid precursors publication-title: Blood doi: 10.1182/blood-2015-06-654194 – volume: 26 start-page: 165 year: 2016 ident: 10.1016/j.bbrc.2016.08.034_bib4 article-title: Ferroptosis: death by lipid peroxidation publication-title: Trends Cell Biol. doi: 10.1016/j.tcb.2015.10.014 – volume: 108 start-page: 13047 year: 2011 ident: 10.1016/j.bbrc.2016.08.034_bib28 article-title: Facile transfer of [2Fe-2S] clusters from the diabetes drug target mitoNEET to an apo-acceptor protein publication-title: Proc. Natl. Acad. Sci. U. S. A. doi: 10.1073/pnas.1109986108 – volume: 1853 start-page: 1294 year: 2015 ident: 10.1016/j.bbrc.2016.08.034_bib16 article-title: Structure-function analysis of NEET proteins uncovers their role as key regulators of iron and ROS homeostasis in health and disease publication-title: Biochim. Biophys. Acta doi: 10.1016/j.bbamcr.2014.10.014 – volume: 284 start-page: 30836 year: 2009 ident: 10.1016/j.bbrc.2016.08.034_bib40 article-title: Short form glutathione peroxidase 4 is the essential isoform required for survival and somatic mitochondrial functions publication-title: J. Biol. Chem. doi: 10.1074/jbc.M109.032839 – volume: 18 start-page: 3351 year: 2011 ident: 10.1016/j.bbrc.2016.08.034_bib46 article-title: Anti-inflammatory and antioxidant properties of a new arylidene-thiazolidinedione in macrophages publication-title: Curr. Med. Chem. doi: 10.2174/092986711796504600 – volume: 156 start-page: 317 year: 2014 ident: 10.1016/j.bbrc.2016.08.034_bib5 article-title: Regulation of ferroptotic cancer cell death by GPX4 publication-title: Cell doi: 10.1016/j.cell.2013.12.010 – volume: 104 start-page: 14342 year: 2007 ident: 10.1016/j.bbrc.2016.08.034_bib14 article-title: MitoNEET is a uniquely folded 2Fe 2S outer mitochondrial membrane protein stabilized by pioglitazone publication-title: Proc. Natl. Acad. Sci. U. S. A. doi: 10.1073/pnas.0707189104 – volume: 23 start-page: 369 year: 2016 ident: 10.1016/j.bbrc.2016.08.034_bib27 article-title: Ferroptosis: process and function publication-title: Cell Death Differ. doi: 10.1038/cdd.2015.158 – volume: 65 start-page: 1534 year: 2016 ident: 10.1016/j.bbrc.2016.08.034_bib18 article-title: MitoNEET-parkin effects in pancreatic alpha- and beta-cells, cellular survival, and intrainsular cross talk publication-title: Diabetes doi: 10.2337/db15-1323 – volume: 5 start-page: 808 year: 2015 ident: 10.1016/j.bbrc.2016.08.034_bib34 article-title: Oxidative stress and the homeodynamics of iron metabolism publication-title: Biomolecules doi: 10.3390/biom5020808 – volume: 59 start-page: 73 year: 2011 ident: 10.1016/j.bbrc.2016.08.034_bib36 article-title: Changes in iron-regulatory gene expression occur in human cell culture models of Parkinson's disease publication-title: Neurochem. Int. doi: 10.1016/j.neuint.2011.05.006 – volume: 16 start-page: 1180 year: 2014 ident: 10.1016/j.bbrc.2016.08.034_bib6 article-title: Inactivation of the ferroptosis regulator Gpx4 triggers acute renal failure in mice publication-title: Nat. Cell Biol. doi: 10.1038/ncb3064 – volume: 10 start-page: 9 year: 2014 ident: 10.1016/j.bbrc.2016.08.034_bib30 article-title: The role of iron and reactive oxygen species in cell death publication-title: Nat. Chem. Biol. doi: 10.1038/nchembio.1416 – volume: 3 start-page: 1 year: 2013 ident: 10.1016/j.bbrc.2016.08.034_bib32 article-title: The role of mitochondria in cellular iron-sulfur protein biogenesis: mechanisms, connected processes, and diseases publication-title: Cold Spring Harb. Perspect. Med. – volume: 10 start-page: e0139699 year: 2015 ident: 10.1016/j.bbrc.2016.08.034_bib22 article-title: Cancer-Related NEET proteins transfer 2Fe-2S clusters to anamorsin, a protein required for cytosolic iron-sulfur cluster biogenesis publication-title: PLoS One doi: 10.1371/journal.pone.0139699 |
| SSID | ssj0011469 |
| Score | 2.6446047 |
| Snippet | Ferroptosis is a form of non-apoptotic cell death originally identified in cancer cells. However, the key regulator of ferroptosis in mitochondria remains... |
| SourceID | proquest pubmed crossref elsevier |
| SourceType | Aggregation Database Index Database Enrichment Source Publisher |
| StartPage | 838 |
| SubjectTerms | Apoptosis - drug effects Apoptosis - genetics Apoptosis Regulatory Proteins - agonists Apoptosis Regulatory Proteins - antagonists & inhibitors Apoptosis Regulatory Proteins - genetics Apoptosis Regulatory Proteins - metabolism cell death CISD1 Deferoxamine - pharmacology Ferroptosis Gene Expression Regulation, Neoplastic Hep G2 Cells hepatoma Humans iron Iron - metabolism Iron Chelating Agents - pharmacology Iron-sulfur proteins Lipid peroxidation Lipid Peroxidation - drug effects membrane proteins Mitochondria Mitochondria - drug effects Mitochondria - metabolism mitochondrial membrane Mitochondrial Proteins - agonists Mitochondrial Proteins - antagonists & inhibitors Mitochondrial Proteins - genetics Mitochondrial Proteins - metabolism neoplasm cells Oxidative Stress Piperazines - antagonists & inhibitors Piperazines - pharmacology sulfur Thiazolidinediones - pharmacology |
| Title | CISD1 inhibits ferroptosis by protection against mitochondrial lipid peroxidation |
| URI | https://dx.doi.org/10.1016/j.bbrc.2016.08.034 https://www.ncbi.nlm.nih.gov/pubmed/27510639 https://www.proquest.com/docview/1814662759 https://www.proquest.com/docview/2101345004 |
| Volume | 478 |
| hasFullText | 1 |
| inHoldings | 1 |
| isFullTextHit | |
| isPrint | |
| link | http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwnV3daxQxEB9KpeiL2NbqqS0RxBfZ9rL56O3jeVquFQqihXsLSTbbRtq9424L9sW_3Znd7IEP1wff9iNZQmYy80t25jcAHyrvymEpVaaFdpm0vMistlXmc-UR8geEIG2A7KWeXsmLmZptwaTPhaGwymT7O5veWuv05CTN5skiRsrxHeq84DNEFGhkixllsMtT0vLjP-swD0q6TRBYZ9Q6Jc50MV7OLYnGkOuWxlPITc5pE_hsndDZC3ie0CMbdwPcha1Q78H-uMad890D-8jaeM72oHwPdj73V08nfVW3ffg-Of_xhbNY30QXmxWrwnI5XzTzVVwx98ASbQMKi9lrGxE7sjtc82gj65JUld3GRSwZsYv_jl05ppdwdfb152SapbIKmZdKNVkxkrlX1ko3IjZE3HBxb9GPIVKh1e1RXirXpc3DyFtZOoEIB18My5BXecidOIDtel6H18CKEEIlTq0XgqOXw90ifti7go8q6b20A-D9fBqfOMep9MWt6YPLfhmSgSEZGKqHKeQAPq37LDrGjUdbq15M5h-9MegSHu33vpepQQnQXxJbh_n9ynA6FCXu5mJzG9wncyEVGpgBvOoUYj1W7MkJ9735z5G9hWd0RzEpXL-D7WZ5Hw4R-DTuqNXsI3gyPv82vfwLiQgBPQ |
| linkProvider | Elsevier |
| linkToHtml | http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwnV3fb9MwED6NTmi8oLHxo7CBkRAvKFod26F5LB1Ty0YlxCb1zbIdZxhtadVmEvvvuUucSjx0D7xFiS-yfOe7z_b5O4APpbPFoJAqyURmE2l4npjMlIlLlUPI7xGCNAmys2xyJb_N1XwHxt1dGEqrjL6_9emNt45vTuJonixDoDu-gyzN-RwRBTrZfP4IdomdSvVgdzQ9n8w2hwnoDCIKzhISiHdn2jQva1fEZMizhslTyG3xaRv-bOLQ2T48jQCSjdo-PoMdXx3A4ajCxfPtPfvImpTOZq_8AB5_6Z72xl1ht0P4MZ7-POUsVL-CDfWalX61WizrxTqsmb1nkbkB9cXMtQkIH9ktTnt0k1VB1spuwjIUjAjG_4S2ItNzuDr7ejmeJLGyQuKkUnWSD2XqlDHSDokQEddc3BkMZQhWaII7VJlKs8KkfuiMLKxAkIMfBoVPy9SnVryAXrWo_Ctgufe-FJ-NE4JjoMMFI_7Y2ZwPS-mcNH3g3XhqF2nHqfrFje7yy35r0oEmHWgqiSlkHz5tZJYt6caDrVWnJv2P6WiMCg_Kve90qlEDdFBiKr-4W2tO-6JE35xvb4NLZS6kQh_Th5etQWz6ipKcoN_r_-zZO9ibXH6_0BfT2fkbeEJfKEWFZ0fQq1d3_hhxUG3fRjv_C1dHA-4 |
| 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=CISD1+inhibits+ferroptosis+by+protection+against+mitochondrial+lipid+peroxidation&rft.jtitle=Biochemical+and+biophysical+research+communications&rft.au=Yuan%2C+Hua&rft.au=Li%2C+Xuemei&rft.au=Zhang%2C+Xiuying&rft.au=Kang%2C+Rui&rft.date=2016-09-16&rft.eissn=1090-2104&rft.volume=478&rft.issue=2&rft.spage=838&rft_id=info:doi/10.1016%2Fj.bbrc.2016.08.034&rft_id=info%3Apmid%2F27510639&rft.externalDocID=27510639 |
| thumbnail_l | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/lc.gif&issn=0006-291X&client=summon |
| thumbnail_m | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/mc.gif&issn=0006-291X&client=summon |
| thumbnail_s | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/sc.gif&issn=0006-291X&client=summon |