Database : MEDLINE
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  1 / 1304 MEDLINE  
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PMID:29289695
Author:Han X; Liu C; Zhang K; Guo M; Shen Z; Liu Y; Zuo Z; Cao M; Li Y
Address:Department of Anesthesiology, Sun Yat-sen Memorial Hospital, Sun Yat-sen University, Guangzhou, 510120, PR China; Laboratory of RNA and Major Diseases of Brain and Heart, Sun Yat-sen Memorial Hospital, Sun Yat-sen University, Guangzhou, 510120, PR China.
Title:Calpain and JNK pathways participate in isoflurane - induced nucleus translocation of apoptosis-inducing factor in the brain of neonatal rats.
Source:Toxicol Lett; 285:60-73, 2018 Mar 15.
ISSN:1879-3169
Country of publication:Netherlands
Language:eng
Abstract:Recent studies have demonstrated that volatile anesthetic causes caspase-dependent neuroapoptosis and persistent cognitive deficits in young animals. Apoptosis-inducing factor (AIF) can trigger apoptosis by caspase-independent pathway. Whether isoflurane induces neuroapoptosis by activation of AIF and its possible mechanism are underdetermined. Rats at postnatal day 7 were exposed to 1.1% isoflurane for 4 h and the expression of AIF, cytochrome c, caspase-3, µ-calpain, m-calpain, Bcl-2 and Bax in the mitochondrial, cytosolic, and nuclear fraction, as well as the number of both AIF and TUNEL positive neurons in the cortices of rats were measured. Moreover, the effects of calpain inhibitor MDL-28170 or JNK inhibitor SP600125 on isoflurane-induced AIF release, caspase activation and cognitive deficits were assessed. We found isoflurane activated CytC-caspase-3 dependent apoptosis pathway mainly in the early phase (0-6 h after exposure). Moreover, isoflurane activated mitochondrial µ-calpain, induced AIF truncation during early phase and activated m-calpain, induced AIF release from the mitochondria to cytosol and translocation into the nucleus in the late phase (6-24 h after exposure). MDL-28170 attenuated the isoflurane-induced mitochondrial AIF truncation, release and nuclear translocation, but did not change the expression of cleaved-caspase-3 and mitochondrial Bax and Bcl-2 proteins. SP600125 attenuated isoflurane-induced neuroapoptosis by inhibiting both AIF and caspase-3 pathways and reduced cognitive impairment in neonatal rats. This is the first study to provide the evidence that isoflurane induced AIF-dependent neuroapoptosis by activation of mitochondrial µ-calpain and m-calpain in neonatal rats. JNK inhibition reversed isoflurane-induced neuroapoptosis and subsequent long-term neurocognitive impairment, acting via inhibiting activation of both AIF and caspase-3 pathways.
Publication type:JOURNAL ARTICLE
Name of substance:0 (Anesthetics, Inhalation); 0 (Apoptosis Inducing Factor); CYS9AKD70P (Isoflurane); EC 2.7.11.24 (JNK Mitogen-Activated Protein Kinases); EC 3.4.22.- (Calpain)


  2 / 1304 MEDLINE  
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PMID:27770267
Author:Nayak VL; Nagesh N; Ravikumar A; Bagul C; Vishnuvardhan MVPS; Srinivasulu V; Kamal A
Address:Medicinal Chemistry and Pharmacology, CSIR-Indian Institute of Chemical Technology, Hyderabad, 500007, India.
Title:2-aryl benzimidazole conjugate induced apoptosis in human breast cancer MCF-7 cells through caspase independent pathway.
Source:Apoptosis; 22(1):118-134, 2017 Jan.
ISSN:1573-675X
Country of publication:Netherlands
Language:eng
Abstract:Apoptosis is a representative form of programmed cell death, which has been assumed to be critical for cancer prevention. Thus, any agent that can induce apoptosis may be useful for cancer treatment and apoptosis induction is arguably the most potent defense against cancer promotion. In our previous studies, 2-aryl benzimidazole conjugates were synthesized and evaluated for their antiproliferative activity and one of the new molecule (2f) was considered as a potential lead. This lead molecule showed significant antiproliferative activity against human breast cancer cell line, MCF-7. The results of the present study revealed that this compound arrested the cell cycle at G2/M phase. Topoisomerase II inhibition assay and Western blot analysis suggested that this compound effectively inhibits topoisomerase II activity which leads to apoptotic cell death. Apoptosis induction in MCF-7 cells was further confirmed by loss of mitochondrial membrane potential (∆Ψm), release of cytochrome c from mitochondria, an increase in the level of apoptosis inducing factor (AIF), generation of reactive oxygen species (ROS), up regulation of proapoptotic protein Bax and down regulation of anti apoptotic protein Bcl-2. Apoptosis assay using Annexin V-FITC assay also suggested that this compound induced cell death by apoptosis. However, compound 2f induced apoptosis could not be reversed by Z-VAD-FMK (a pan-caspase inhibitor) demonstrated that the 2f induced apoptosis was caspase independent. Further, 2f treatment did not activate caspase-7 and caspase-9 activity, suggesting that this compound induced apoptosis in breast cancer cells via a caspase independent pathway. Most importantly, this compound was less toxic towards non-tumorigenic breast epithelial cells, MCF-10A. Furthermore, docking studies also support the potentiality of this molecule to bind to the DNA topoisomerase II.
Publication type:JOURNAL ARTICLE
Name of substance:0 (AIFM1 protein, human); 0 (Apoptosis Inducing Factor); 0 (BAX protein, human); 0 (Benzimidazoles); 0 (Caspase Inhibitors); 0 (Reactive Oxygen Species); 0 (bcl-2-Associated X Protein); E24GX49LD8 (benzimidazole); EC 3.4.22.- (Caspases); EC 5.99.1.3 (DNA Topoisomerases, Type II)


  3 / 1304 MEDLINE  
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PMID:29227599
Author:Minchenko OH; Kryvdiuk IV; Riabovol OO; Minchenko DO; Danilovskyi SV; Ratushna OO
Title:Inhibition of IRE1 modifies the hypoxic regulation of GADD family gene expressions in U87 glioma cells.
Source:Ukr Biochem J; 88(2):25-34, 2016 Mar-Apr.
ISSN:2409-4943
Country of publication:Ukraine
Language:eng
Abstract:We have studied hypoxic regulation of the expression of genes encoded GADD (growth arrest and DNA damage) family proteins in U87 glioma cells in relation to inhibition of IRE1 (inositol requiring enzyme-1), which controls cell proliferation and tumor growth as a central mediator of endoplasmic reticulum stress. We have shown that hypoxia up-regulates the expression of GADD34, GADD45A, GADD45B, and GADD153 genes, which are related to cell proliferation and apoptosis, in control (transfected by empty vector) glioma cells in gene specific manner. At the same time, the expression level of EIF2AK 1 (eukaryotic translation initiation factor 2-alpha kinase 1) and AI FM1 (apoptosis inducing factor, mitochondria associated 1) genes in these cells is down-regulated upon hypoxic condition. It was also shown that inhibition of ІRE1 signaling enzyme function in U87 glioma cells enhances the effect of hypoxia on these genes expression, except EIF2AK 1 and AI FM1 genes. Furthermore, the expression of all studied genes in ІRE1 knockdown cells is significantly decreased upon normoxic condition, except GADD45B gene, which expression level is strongly up-regulated. Therefore, the expression level of genes encoding GADD34, GADD45A, GADD45B, GADD153, EIF2AK 1, and AI FM1 is affected by hypoxia and by inhibition of IRE1-mediated endoplasmic reticulum stress signaling in gene specific manner and correlates with suppression of glioma cell proliferation upon inhibition of the IRE1 enzyme function.
Publication type:JOURNAL ARTICLE
Name of substance:0 (AIFM1 protein, human); 0 (Antigens, Differentiation); 0 (Apoptosis Inducing Factor); 0 (Cell Cycle Proteins); 0 (DDIT3 protein, human); 0 (GADD45A protein, human); 0 (GADD45B protein, human); 0 (Nuclear Proteins); 147336-12-7 (Transcription Factor CHOP); EC 2.7.11.1 (EIF2AK1 protein, human); EC 2.7.11.1 (ERN1 protein, human); EC 2.7.11.1 (Protein-Serine-Threonine Kinases); EC 2.7.11.1 (eIF-2 Kinase); EC 3.1.- (Endoribonucleases); EC 3.1.3.16 (PPP1R15A protein, human); EC 3.1.3.16 (Protein Phosphatase 1)


  4 / 1304 MEDLINE  
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PMID:29186589
Author:Gal J; Chen J; Katsumata Y; Fardo DW; Wang WX; Artiushin S; Price D; Anderson S; Patel E; Zhu H; Nelson PT
Address:Department of Molecular and Cellular Biochemistry; Department of Biostatistics; Sanders-Brown Center on Aging; Department of Pathology, University of Kentucky, Lexington, Kentucky; and Research and Development, Lexington VA Medical Center, Lexington, Kentucky.
Title:Detergent Insoluble Proteins and Inclusion Body-Like Structures Immunoreactive for PRKDC/DNA-PK/DNA-PKcs, FTL, NNT, and AIFM1 in the Amygdala of Cognitively Impaired Elderly Persons.
Source:J Neuropathol Exp Neurol; 77(1):21-39, 2018 Jan 01.
ISSN:1554-6578
Country of publication:England
Language:eng
Abstract:Misfolded protein in the amygdala is a neuropathologic feature of Alzheimer disease and many other neurodegenerative disorders. We examined extracts from human amygdala (snap-frozen at autopsy) to investigate whether novel and as yet uncharacterized misfolded proteins would be detectable. Polypeptides from the detergent-insoluble, urea-soluble protein fractions of amygdala were interrogated using liquid chromatography-electrospray ionization-tandem mass spectrometry. Among the detergent-insoluble proteins identified in amygdala of demented subjects but not controls were Tau, TDP-43, Aß, α-synuclein, and ApoE. Additional detergent-insoluble proteins from demented subjects in the high-molecular weight portion of SDS gels included NNT, TNIK, PRKDC (DNA-PK, or DNA-PKcs), ferritin light chain (FTL), AIFM1, SYT11, STX1B, EAA1, COL25A1, M4K4, CLH1, SQSTM, SYNJ1, C3, and C4. In follow-up immunohistochemical experiments, NNT, TNIK, PRKDC, AIFM1, and FTL were observed in inclusion body-like structures in cognitively impaired subjects' amygdalae. Double-label immunofluorescence revealed that FTL and phospho-PRKDC immunoreactivity colocalized partially with TDP-43 and/or Tau inclusion bodies. Western blots showed high-molecular weight "smears", particularly for NNT and PRKDC. A preliminary genetic association study indicated that rare NNT, TNIK, and PRKDC gene variants had nominally significant association with Alzheimer-type dementia risk. In summary, novel detergent-insoluble proteins, with evidence of proteinaceous deposits, were found in amygdalae of elderly, cognitively impaired subjects.
Publication type:JOURNAL ARTICLE
Name of substance:0 (AIFM1 protein, human); 0 (Apoptosis Inducing Factor); 0 (DNA-Binding Proteins); 0 (FTL protein, human); 0 (Mitochondrial Proteins); 0 (Nuclear Proteins); 9013-31-4 (Apoferritins); EC 1.6.1.2 (NADP Transhydrogenase, AB-Specific); EC 1.6.1.2 (NNT protein, human); EC 2.7.11.1 (DNA-Activated Protein Kinase); EC 2.7.11.1 (PRKDC protein, human)


  5 / 1304 MEDLINE  
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PMID:29061809
Author:Maiuthed A; Pinkhien T; Chamni S; Suwanborirux K; Saito N; Petpiroon N; Chanvorachote P
Address:Department of Pharmacology and Physiology, Faculty of Pharmaceutical Sciences, Chulalongkorn University, Bangkok, Thailand.
Title:Apoptosis-inducing Effect of Hydroquinone 5- -Cinnamoyl Ester Analog of Renieramycin M on Non-small Cell Lung Cancer Cells.
Source:Anticancer Res; 37(11):6259-6267, 2017 11.
ISSN:1791-7530
Country of publication:Greece
Language:eng
Abstract:BACKGROUND: A newly-synthesized derivative of renieramycin M (RM), an anticancer lead compound isolated from the blue sponge Xestospongia sp., hydroquinone 5-O-cinnamoyl ester (CIN-RM), was investigated here for its activity against non-small cell lung cancer cells. MATERIALS AND METHODS: Cytotoxicity effects of CIN-RM and RM on H292 lung cancer cells were determined by the MTT assay. We also investigated the mechanism of CIN-RM-mediated apoptosis and mechanism of action of this compound by western blotting. RESULTS: CIN-RM showed more potent cytotoxicity than its parental compound (RM) against H292 lung cancer cells. At concentrations of 15-60 µM, CIN-RM significantly induced apoptosis by increasing expression of apoptosis-inducing factor (AIF) and activation of caspase-3 and -9. For up-stream mechanism, CIN-RM mediated apoptosis through a p53-dependent mechanism, that consequently down-regulated anti-apoptotic B-cell lymphoma 2 (BCL2), while increasing the level of pro-apoptotic BCL2-associated X (BAX). In addition, phosphorylation of pro-survival protein AKT was found to be dramatically reduced. CONCLUSION: This study revealed the potential of CIN-RM for apoptosis induction and in the development of a novel anticancer agent.
Publication type:JOURNAL ARTICLE
Name of substance:0 (AIFM1 protein, human); 0 (Apoptosis Inducing Factor); 0 (Hydroquinones); 0 (Tetrahydroisoquinolines); 0 (renieramycin M); EC 3.4.22.- (CASP3 protein, human); EC 3.4.22.- (CASP9 protein, human); EC 3.4.22.- (Caspase 3); EC 3.4.22.- (Caspase 9)


  6 / 1304 MEDLINE  
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PMID:28880942
Author:Maes ME; Schlamp CL; Nickells RW
Address:Department of Ophthalmology and Visual Sciences, School of Medicine and Public Health, University of Wisconsin - Madison, Madison, Wisconsin, United States of America.
Title:Live-cell imaging to measure BAX recruitment kinetics to mitochondria during apoptosis.
Source:PLoS One; 12(9):e0184434, 2017.
ISSN:1932-6203
Country of publication:United States
Language:eng
Abstract:The pro-apoptotic BCL2 gene family member, BAX, plays a pivotal role in the intrinsic apoptotic pathway. Under cellular stress, BAX recruitment to the mitochondria occurs when activated BAX forms dimers, then oligomers, to initiate mitochondria outer membrane permeabilization (MOMP), a process critical for apoptotic progression. The activation and recruitment of BAX to form oligomers has been studied for two decades using fusion proteins with a fluorescent reporter attached in-frame to the BAX N-terminus. We applied high-speed live cell imaging to monitor the recruitment of BAX fusion proteins in dying cells. Data from time-lapse imaging was validated against the activity of endogenous BAX in cells, and analyzed using sigmoid mathematical functions to obtain detail of the kinetic parameters of the recruitment process at individual mitochondrial foci. BAX fusion proteins behave like endogenous BAX during apoptosis. Kinetic studies show that fusion protein recruitment is also minimally affected in cells lacking endogenous BAK or BAX genes, but that the kinetics are moderately, but significantly, different with different fluorescent tags in the fusion constructs. In experiments testing BAX recruitment in 3 different cell lines, our results show that regardless of cell type, once activated, BAX recruitment initiates simultaneously within a cell, but exhibits varying rates of recruitment at individual mitochondrial foci. Very early during BAX recruitment, pro-apoptotic molecules are released in the process of MOMP, but different molecules are released at different times and rates relative to the time of BAX recruitment initiation. These results provide a method for BAX kinetic analysis in living cells and yield greater detail of multiple characteristics of BAX-induced MOMP in living cells that were initially observed in cell free studies.
Publication type:JOURNAL ARTICLE
Name of substance:0 (AIFM1 protein, human); 0 (Apoptosis Inducing Factor); 0 (DIABLO protein, human); 0 (Intracellular Signaling Peptides and Proteins); 0 (Mitochondrial Proteins); 0 (bcl-2-Associated X Protein); 9007-43-6 (Cytochromes c)


  7 / 1304 MEDLINE  
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PMID:28666871
Author:Sorrentino L; Cossu F; Milani M; Aliverti A; Mastrangelo E
Address:Biophysics Institute, National Research Council c/o Department of Biosciences, Università degli Studi di Milano, Via Celoria 26, 20133 Milano, Italy; Department of Biosciences, Università degli Studi di Milano, Via Celoria 26, 20133 Milano, Italy.
Title:Structural bases of the altered catalytic properties of a pathogenic variant of apoptosis inducing factor.
Source:Biochem Biophys Res Commun; 490(3):1011-1017, 2017 Aug 26.
ISSN:1090-2104
Country of publication:United States
Language:eng
Abstract:The apoptosis-inducing factor (AIF) is a FAD-containing protein playing critical roles in caspase-independent apoptosis and mitochondrial respiratory chain biogenesis and maintenance. While its lethal role is well known, the details of its mitochondrial function remain elusive. So far, nineteen allelic variants of AIF have been associated to human diseases, mainly affecting the nervous system. A strict correlation is emerging between the degree of impairment of its ability to stabilize the charge-transfer (CT) complex between FAD and NAD and the severity of the resulting pathology. Recently, we demonstrated that the G307E replacement in murine AIF (equivalent to the pathogenic G308E in the human protein) dramatically decreases the rate of CT complex formation through the destabilization of the flavoprotein interaction with NAD(H). To provide further insights into the structural bases of its altered functional properties, here we report the first crystal structure of an AIF pathogenic mutant variant in complex with NAD (murine AIF-G307E ) in comparison with its oxidized form. With respect to wild type AIF, the mutation leads to an altered positioning of NAD adenylate moiety, which slows down CT complex formation. Moreover, the altered balance between the binding of the adenine/nicotinamide portions of the coenzyme determines a large drop in AIF-G307E ability to discriminate between NADH and NADPH.
Publication type:JOURNAL ARTICLE
Name of substance:0 (Apoptosis Inducing Factor); 0U46U6E8UK (NAD); 53-59-8 (NADP)


  8 / 1304 MEDLINE  
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PMID:28526682
Author:Chan TK; Tan WSD; Peh HY; Wong WSF
Address:Department of Pharmacology, Yong Loo Lin School of Medicine, National University Health System, Singapore 117600, Singapore.
Title:Aeroallergens Induce Reactive Oxygen Species Production and DNA Damage and Dampen Antioxidant Responses in Bronchial Epithelial Cells.
Source:J Immunol; 199(1):39-47, 2017 Jul 01.
ISSN:1550-6606
Country of publication:United States
Language:eng
Abstract:Exposure to environmental allergens is a major risk factor for asthma development. Allergens possess proteolytic activity that is capable of disrupting the airway epithelium. Although there is increasing evidence pointing to asthma as an epithelial disease, the underlying mechanism that drives asthma has not been fully elucidated. In this study, we investigated the direct DNA damage potential of aeroallergens on human bronchial epithelial cells and elucidated the mechanisms mediating the damage. Human bronchial epithelial cells, BEAS-2B, directly exposed to house dust mites (HDM) resulted in enhanced DNA damage, as measured by the CometChip and the staining of DNA double-strand break marker, γH2AX. HDM stimulated cellular reactive oxygen species production, increased mitochondrial oxidative stress, and promoted nitrosative stress. Notably, expression of nuclear factor erythroid 2-related factor 2-dependent antioxidant genes was reduced immediately after HDM exposure, suggesting that HDM altered antioxidant responses. HDM exposure also reduced cell proliferation and induced cell death. Importantly, HDM-induced DNA damage can be prevented by the antioxidants glutathione and catalase, suggesting that HDM-induced reactive oxygen and nitrogen species can be neutralized by antioxidants. Mechanistic studies revealed that HDM-induced cellular injury is NADPH oxidase (NOX)-dependent, and apocynin, a NOX inhibitor, protected cells from double-strand breaks induced by HDM. Our results show that direct exposure of bronchial epithelial cells to HDM leads to the production of reactive oxygen and nitrogen species that damage DNA and induce cytotoxicity. Antioxidants and NOX inhibitors can prevent HDM-induced DNA damage, revealing a novel role for antioxidants and NOX inhibitors in mitigating allergic airway disease.
Publication type:JOURNAL ARTICLE
Name of substance:0 (Acetophenones); 0 (Allergens); 0 (Antioxidants); 0 (Apoptosis Inducing Factor); 0 (Membrane Glycoproteins); 0 (Reactive Oxygen Species); B6J7B9UDTR (acetovanillone); EC 1.11.1.6 (Catalase); EC 1.6.3.- (CYBB protein, human); EC 1.6.3.- (NADPH Oxidase 2); EC 1.6.3.- (NADPH Oxidase 4); EC 1.6.3.- (NADPH Oxidases); EC 1.6.3.- (NOX4 protein, human); GAN16C9B8O (Glutathione)


  9 / 1304 MEDLINE  
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PMID:28367082
Author:Aldasoro M; Jorda A; Aldasoro C; Marchio P; Guerra-Ojeda S; Gimeno-Raga M; Mauricio MD; Iradi A; Obrador E; Vila JM; Valles SL
Address:Department of Physiology, School of Medicine, University of Valencia, Valencia, Spain.
Title:Neuronal Effects of Sugammadex in combination with Rocuronium or Vecuronium.
Source:Int J Med Sci; 14(3):224-230, 2017.
ISSN:1449-1907
Country of publication:Australia
Language:eng
Abstract:Rocuronium (ROC) and Vecuronium (VEC) are the most currently used steroidal non-depolarizing neuromuscular blocking (MNB) agents. Sugammadex (SUG) rapidly reverses steroidal NMB agents after anaesthesia. The present study was conducted in order to evaluate neuronal effects of SUG alone and in combination with both ROC and VEC. Using MTT, CASP-3 activity and Western-blot we determined the toxicity of SUG, ROC or VEC in neurons in primary culture. SUG induces apoptosis/necrosis in neurons in primary culture and increases cytochrome C (CytC), apoptosis-inducing factor (AIF), Smac/Diablo and Caspase 3 (CASP-3) protein expression. Our results also demonstrated that both ROC and VEC prevent these SUG effects. The protective role of both ROC and VEC could be explained by the fact that SUG encapsulates NMB drugs. In BBB impaired conditions it would be desirable to control SUG doses to prevent the excess of free SUG in plasma that may induce neuronal damage. A balance between SUG, ROC or VEC would be necessary to prevent the risk of cell damage.
Publication type:JOURNAL ARTICLE
Name of substance:0 (Androstanols); 0 (Apoptosis Inducing Factor); 0 (Drug Combinations); 0 (Neuromuscular Blocking Agents); 0 (Pdcd8 protein, rat); 0 (gamma-Cyclodextrins); 361LPM2T56 (Sugammadex); 7E4PHP5N1D (Vecuronium Bromide); 9007-43-6 (Cytochromes c); EC 3.4.22.- (Caspase 3); WRE554RFEZ (rocuronium)


  10 / 1304 MEDLINE  
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PMID:28350112
Author:Zhang L; Yan J; Liu Y; Zhao Q; Di C; Chao S; Jie L; Liu Y; Zhang H
Address:Department of Heavy Ion Radiation Medicine, Institute of Modern Physics, Chinese Academy of Sciences, Lanzhou, Gansu 730000, P.R. China.
Title:Contribution of caspase-independent pathway to apoptosis in malignant glioma induced by carbon ion beams.
Source:Oncol Rep; 37(5):2994-3000, 2017 May.
ISSN:1791-2431
Country of publication:Greece
Language:eng
Abstract:High linear energy transfer (LET) carbon ion beam (CIB) is becoming the best tool for external radiotherapy of inoperable tumors because of its greater cell killing than conventional low LET gamma or X-rays. In the present study, whether the caspase-independent pathway exerts the important contribution in CIB-induced cell apoptosis was explored. Herein we showed, despite the absence of caspase activity using a pan caspase inhibitor Z-VAD-FMK, that apoptosis induced by high LET CIB were clearly observed in the glioma cells. Simultaneously, the increased 8-OHdG level, PARP-1 activity and AIF translocation occurred in response to CIB irradiation. Moreover, it was distinctly higher in the nuclear translocation frequency along with PARP-1 activation when the caspase protease cascade was suppressed in the irradiated glioma cells. Nuclear colocalization between PARP-1 and AIF as well as a positive association of the PARP-1 mRNA expression with AIF translocation frequency indicated that PARP-1 activation controlled the translocation of AIF to the nucleus. Our findings strongly demonstrated that caspase-independent cell apoptosis provided a prominent compensation in the glioma cell death involving the PARP-1/AIF signaling pathway at 24 h after CIB exposure, and likely triggered by oxidative damage to DNA. The knowledge on the molecular mechanism of AIF-mediated cell death may be very useful for the improvement of the therapeutic efficacy of malignant gliomas with heavy charged particles.
Publication type:JOURNAL ARTICLE
Name of substance:0 (AIFM1 protein, human); 0 (Apoptosis Inducing Factor); EC 2.4.2.30 (PARP1 protein, human); EC 2.4.2.30 (Poly (ADP-Ribose) Polymerase-1); EC 3.4.22.- (Caspases)



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