Database : MEDLINE
Search on : Iodide and Peroxidase [Words]
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[PMID]: 29500802
[Au] Autor:Yaglova NV; Sledneva YP; Nazimova SV; Obernikhin SS; Yaglov VV
[Ad] Address:Research Institute of Human Morphology, Moscow, Russia. yaglova@mail.ru.
[Ti] Title:Sex Differences in the Production of SLC5A5, Thyroid Peroxidase, and Thyroid Hormones in Pubertal Rats Exposed to Endocrine Disruptor Dichlorodiphenyltrichloroethane (DDT) during Postnatal Ontogeny.
[So] Source:Bull Exp Biol Med;, 2018 Mar 03.
[Is] ISSN:1573-8221
[Cp] Country of publication:United States
[La] Language:eng
[Ab] Abstract:Sex differences in the expression of iodide transporter SLC5A5 and thyroid peroxidase in thyroid follicular epithelium and thyroid serum profile were assessed in pubertal rats exposed to endocrine disruptor DDT starting from the first postnatal day. It was found that exposure to DDT reduced expression of SLC5A5 in peripheral regions of thyroid lobes in males and in central regions in females. The most pronounced sex differences were observed in thyroid peroxidase expression that remained sensitive to thyroid stimulating hormone regulation in males and lost sensitivity to pituitary stimulation in females after exposure to disruptor, which determines more pronounced hypothyroidism in females.
[Pt] Publication type:JOURNAL ARTICLE
[Em] Entry month:1803
[Cu] Class update date: 180303
[Lr] Last revision date:180303
[St] Status:Publisher
[do] DOI:10.1007/s10517-018-4005-1

  2 / 5377 MEDLINE  
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[PMID]: 29253128
[Au] Autor:Mohácsik P; Erdélyi F; Baranyi M; Botz B; Szabó G; Tóth M; Haltrich I; Helyes Z; Sperlágh B; Tóth Z; Sinkó R; Lechan RM; Bianco AC; Fekete C; Gereben B
[Ad] Address:Department of Endocrine Neurobiology, Institute of Experimental Medicine, Hungarian Academy of Sciences, Budapest, Hungary.
[Ti] Title:A Transgenic Mouse Model for Detection of Tissue-Specific Thyroid Hormone Action.
[So] Source:Endocrinology;159(2):1159-1171, 2018 02 01.
[Is] ISSN:1945-7170
[Cp] Country of publication:United States
[La] Language:eng
[Ab] Abstract:Thyroid hormone (TH) is present in the systemic circulation and thus should affect all cells similarly in the body. However, tissues have a complex machinery that allows tissue-specific optimization of local TH action that calls for the assessment of TH action in a tissue-specific manner. Here, we report the creation of a TH action indicator (THAI) mouse model to study tissue-specific TH action. The model uses a firefly luciferase reporter readout in the context of an intact transcriptional apparatus and all elements of TH metabolism and transport and signaling. The THAI mouse allows the assessment of the changes of TH signaling in tissue samples or in live animals using bioluminescence, both in hypothyroidism and hyperthyroidism. Beyond pharmacologically manipulated TH levels, the THAI mouse is sufficiently sensitive to detect deiodinase-mediated changes of TH action in the interscapular brown adipose tissue (BAT) that preserves thermal homeostasis during cold stress. The model revealed that in contrast to the cold-induced changes of TH action in the BAT, the TH action in this tissue, at room temperature, is independent of noradrenergic signaling. Our data demonstrate that the THAI mouse can also be used to test TH receptor isoform-specific TH action. Thus, THAI mouse constitutes a unique model to study tissue-specific TH action within a physiological/pathophysiological context and test the performance of thyromimetics. In conclusion, THAI mouse provides an in vivo model to assess a high degree of tissue specificity of TH signaling, allowing alteration of tissue function in health and disease, independently of changes in circulating levels of TH.
[Mh] MeSH terms primary: Genes, Reporter
Response Elements
Thyroid Hormones/pharmacology
Thyroid Hormones/physiology
[Mh] MeSH terms secundary: Animals
Cells, Cultured
Female
Gene Expression Regulation
HEK293 Cells
Humans
Hyperthyroidism/genetics
Hyperthyroidism/metabolism
Hypothyroidism/genetics
Hypothyroidism/metabolism
Iodide Peroxidase/genetics
Iodide Peroxidase/metabolism
Male
Mice
Mice, Transgenic
Models, Animal
Organ Specificity/drug effects
Organ Specificity/genetics
Signal Transduction/drug effects
Signal Transduction/genetics
[Pt] Publication type:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Name of substance:0 (Thyroid Hormones); EC 1.11.1.8 (Iodide Peroxidase)
[Em] Entry month:1802
[Cu] Class update date: 180215
[Lr] Last revision date:180215
[Js] Journal subset:AIM; IM
[Da] Date of entry for processing:171219
[St] Status:MEDLINE
[do] DOI:10.1210/en.2017-00582

  3 / 5377 MEDLINE  
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[PMID]: 29186449
[Au] Autor:van der Spek AH; Jim KK; Karaczyn A; van Beeren HC; Ackermans MT; Darras VM; Vandenbroucke-Grauls CMJE; Hernandez A; Brouwer MC; Fliers E; van de Beek D; Boelen A
[Ad] Address:Department of Endocrinology and Metabolism, Academic Medical Center, University of Amsterdam, Amsterdam, the Netherlands.
[Ti] Title:The Thyroid Hormone Inactivating Type 3 Deiodinase Is Essential for Optimal Neutrophil Function: Observations From Three Species.
[So] Source:Endocrinology;159(2):826-835, 2018 02 01.
[Is] ISSN:1945-7170
[Cp] Country of publication:United States
[La] Language:eng
[Ab] Abstract:Neutrophils are essential effector cells of the innate immune system that have recently been recognized as thyroid hormone (TH) target cells. Cellular TH bioavailability is regulated by the deiodinase enzymes, which can activate or inactivate TH. We have previously shown that the TH inactivating enzyme type 3 deiodinase (D3) is present in neutrophils. Furthermore, D3 knockout (D3KO) mice show impaired bacterial killing upon infection. We hypothesized that D3 plays a role in neutrophil function during infection by actively regulating local TH availability. We measured TH concentrations in cerebrospinal fluid (CSF) from patients with bacterial meningitis and controls. Bacterial meningitis resulted in marked changes in CSF TH levels, characterized by a strong increase of thyroxine and reverse-triiodothyronine concentrations. This altered TH profile was consistent with elevated D3 activity in infiltrating neutrophils at the site of infection. D3 knockdown in zebrafish embryos with pneumococcal meningitis resulted in increased mortality and reduced neutrophil infiltration during infection. Finally, stimulated neutrophils from female D3KO mice exhibited impaired NADPH-oxidase activity, an important component of the neutrophil bacterial killing machinery. These consistent findings across experimental models strongly support a critical role for reduced intracellular TH concentrations in neutrophil function during infection, for which the TH inactivating enzyme D3 appears essential.
[Mh] MeSH terms primary: Iodide Peroxidase/physiology
Neutrophils/physiology
[Mh] MeSH terms secundary: Animals
Animals, Genetically Modified
Case-Control Studies
Cells, Cultured
Embryo, Nonmammalian
Iodide Peroxidase/genetics
Meningitis, Bacterial/cerebrospinal fluid
Meningitis, Bacterial/immunology
Mice, Knockout
Species Specificity
Thyroid Hormones/cerebrospinal fluid
Thyroid Hormones/metabolism
Triiodothyronine, Reverse/cerebrospinal fluid
Zebrafish/embryology
Zebrafish/genetics
Zebrafish/metabolism
[Pt] Publication type:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Name of substance:0 (Thyroid Hormones); 5817-39-0 (Triiodothyronine, Reverse); EC 1.11.1.- (iodothyronine deiodinase type III); EC 1.11.1.8 (Iodide Peroxidase)
[Em] Entry month:1802
[Cu] Class update date: 180215
[Lr] Last revision date:180215
[Js] Journal subset:AIM; IM
[Da] Date of entry for processing:171130
[St] Status:MEDLINE
[do] DOI:10.1210/en.2017-00666

  4 / 5377 MEDLINE  
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[PMID]: 29320567
[Au] Autor:Gil-Cayuela C; Ortega A; Tarazón E; Martínez-Dolz L; Cinca J; González-Juanatey JR; Lago F; Roselló-Lletí E; Rivera M; Portolés M
[Ad] Address:Cardiocirculatory Unit, Health Research Institute of La Fe University Hospital (IIS La Fe), Valencia, Spain.
[Ti] Title:Myocardium of patients with dilated cardiomyopathy presents altered expression of genes involved in thyroid hormone biosynthesis.
[So] Source:PLoS One;13(1):e0190987, 2018.
[Is] ISSN:1932-6203
[Cp] Country of publication:United States
[La] Language:eng
[Ab] Abstract:BACKGROUND: The association between dilated cardiomyopathy (DCM) and low thyroid hormone (TH) levels has been previously described. In these patients abnormal thyroid function is significantly related to impaired left ventricular (LV) function and increased risk of death. Although TH was originally thought to be produced exclusively by the thyroid gland, we recently reported TH biosynthesis in the human ischemic heart. OBJECTIVES: Based on these findings, we evaluated whether the genes required for TH production are also altered in patients with DCM. METHODS: Twenty-three LV tissue samples were obtained from patients with DCM (n = 13) undergoing heart transplantation and control donors (n = 10), and used for RNA sequencing analysis. The number of LV DCM samples was increased to 23 to determine total T4 and T3 tissue levels by ELISA. RESULTS: We found that all components of TH biosynthesis are expressed in human dilated heart tissue. Expression of genes encoding thyroperoxidase (-2.57-fold, P < 0.05) and dual oxidase 2 (2.64-fold, P < 0.01), the main enzymatic system of TH production, was significantly altered in patients with DCM and significantly associated with LV remodeling parameters. Thyroxine (T4) cardiac tissue levels were significantly increased (P < 0.01), whilst triiodothyronine (T3) levels were significantly diminished (P < 0.05) in the patients. CONCLUSIONS: Expression of TH biosynthesis machinery in the heart and total tissue levels of T4 and T3, are altered in patients with DCM. Given the relevance of TH in cardiac pathology, our results provide a basis for new gene-based therapeutic strategies for treating DCM.
[Mh] MeSH terms primary: Autoantigens/genetics
Cardiomyopathy, Dilated/genetics
Dual Oxidases/genetics
Iodide Peroxidase/genetics
Iron-Binding Proteins/genetics
Myocardium/metabolism
Receptors, Thyrotropin/genetics
Thyroid Hormones/biosynthesis
[Mh] MeSH terms secundary: Autoantigens/metabolism
Biomarkers/metabolism
Cardiomyopathy, Dilated/pathology
Case-Control Studies
Dual Oxidases/metabolism
Female
Gene Expression Profiling
Gene Expression Regulation
High-Throughput Nucleotide Sequencing/methods
Humans
Iodide Peroxidase/metabolism
Iron-Binding Proteins/metabolism
Male
Middle Aged
Receptors, Thyrotropin/metabolism
Ventricular Remodeling
[Pt] Publication type:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Name of substance:0 (Autoantigens); 0 (Biomarkers); 0 (Iron-Binding Proteins); 0 (Receptors, Thyrotropin); 0 (Thyroid Hormones); EC 1.11.1.- (Dual Oxidases); EC 1.11.1.7 (TPO protein, human); EC 1.11.1.8 (Iodide Peroxidase); EC 1.6.3.1 (DUOX2 protein, human)
[Em] Entry month:1802
[Cu] Class update date: 180212
[Lr] Last revision date:180212
[Js] Journal subset:IM
[Da] Date of entry for processing:180111
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0190987

  5 / 5377 MEDLINE  
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[PMID]: 29242189
[Au] Autor:Nicolussi A; Dunn JD; Mlynek G; Bellei M; Zamocky M; Battistuzzi G; Djinovic-Carugo K; Furtmüller PG; Soldati T; Obinger C
[Ad] Address:From the Department of Chemistry, Division of Biochemistry, BOKU-University of Natural Resources and Life Sciences, 1190 Vienna, Austria.
[Ti] Title:Secreted heme peroxidase from : Insights into catalysis, structure, and biological role.
[So] Source:J Biol Chem;293(4):1330-1345, 2018 Jan 26.
[Is] ISSN:1083-351X
[Cp] Country of publication:United States
[La] Language:eng
[Ab] Abstract:Oxidation of halides and thiocyanate by heme peroxidases to antimicrobial oxidants is an important cornerstone in the innate immune system of mammals. Interestingly, phylogenetic and physiological studies suggest that homologous peroxidases are already present in mycetozoan eukaryotes such as This social amoeba kills bacteria via phagocytosis for nutrient acquisition at its single-cell stage and for antibacterial defense at its multicellular stages. Here, we demonstrate that peroxidase A from (DdPoxA) is a stable, monomeric, glycosylated, and secreted heme peroxidase with homology to mammalian peroxidases. The first crystal structure (2.5 Å resolution) of a mycetozoan peroxidase of this superfamily shows the presence of a post-translationally-modified heme with one single covalent ester bond between the 1-methyl heme substituent and Glu-236. The metalloprotein follows the halogenation cycle, whereby compound I oxidizes iodide and thiocyanate at high rates (>10 m s ) and bromide at very low rates. It is demonstrated that DdPoxA is up-regulated and likely secreted at late multicellular development stages of when migrating slugs differentiate into fruiting bodies that contain persistent spores on top of a cellular stalk. Expression of DdPoxA is shown to restrict bacterial contamination of fruiting bodies. Structure and function of DdPoxA are compared with evolutionary-related mammalian peroxidases in the context of non-specific immune defense.
[Pt] Publication type:JOURNAL ARTICLE
[Em] Entry month:1712
[Cu] Class update date: 180201
[Lr] Last revision date:180201
[St] Status:In-Data-Review
[do] DOI:10.1074/jbc.RA117.000463

  6 / 5377 MEDLINE  
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[PMID]: 28970022
[Au] Autor:Chang J; Hao W; Xu Y; Xu P; Li W; Li J; Wang H
[Ad] Address:Research Center for Eco-Environmental Science, Chinese Academy of Sciences, Shuangqing RD 18, Beijing 100085, China; University of Chinese Academy of Sciences, Yuquan RD 19 a, Beijing 100049, China.
[Ti] Title:Stereoselective degradation and thyroid endocrine disruption of lambda-cyhalothrin in lizards (Eremias argus) following oral exposure.
[So] Source:Environ Pollut;232:300-309, 2018 Jan.
[Is] ISSN:1873-6424
[Cp] Country of publication:England
[La] Language:eng
[Ab] Abstract:The disturbance of the thyroid system and elimination of chiral pyrethroid pesticides with respect to enantioselectivity in reptiles have so far received limited attention by research. In this study, bioaccumulation, thyroid gland lesions, thyroid hormone levels, and hypothalamus-pituitary-thyroid axis-related gene expression in male Eremias argus were investigated after three weeks oral administration of lambda-cyhalothrin (LCT) enantiomers. In the lizard liver, the concentration of LCT was negatively correlated with the metabolite-3-phenoxybenzoic acid (PBA) level during 21 days of exposure. (+)-LCT exposure induced a higher thyroid follicular epithelium height than (-)-LCT exposure. The thyroxine levels were increased in both treated groups while only (+)-LCT exposure induced a significant change in the triiodothyronine (T3) level. In addition, the expressions of hypothalamus-pituitary-thyroid axis-related genes including thyroid hormone receptors (trs), deiodinases (dios), uridinediphosphate glucuronosyltransferase (udp), and sulfotransferase (sult) were up-regulated after exposure to the two enantiomers. (+)-LCT treatment resulted in higher expression of trs and (-)-LCT exposure led to greater stimulation of dios in the liver, which indicated PBA-induced antagonism on thyroid hormone receptors and LCT-induced disruption of thyroxine (T4) deiodination. The results suggest the (-)-LCT exposure causes higher residual level in lizard liver while induces less disruption on lizard thyroid activity than (+)-LCT.
[Mh] MeSH terms primary: Lizards/physiology
Nitriles/toxicity
Pesticides/toxicity
Pyrethrins/toxicity
Thyroid Gland/drug effects
[Mh] MeSH terms secundary: Animals
Benzoates
Endocrine Disruptors/metabolism
Iodide Peroxidase/metabolism
Liver/metabolism
Lizards/metabolism
Male
Pesticides/metabolism
Receptors, Thyroid Hormone/metabolism
Stereoisomerism
Thyroid Gland/metabolism
Thyroid Hormones/metabolism
Thyroxine
[Pt] Publication type:JOURNAL ARTICLE
[Nm] Name of substance:0 (Benzoates); 0 (Endocrine Disruptors); 0 (Nitriles); 0 (Pesticides); 0 (Pyrethrins); 0 (Receptors, Thyroid Hormone); 0 (Thyroid Hormones); 69DC2655VH (3-phenoxybenzoic acid); EC 1.11.1.8 (Iodide Peroxidase); Q51BO43MG4 (Thyroxine); V0V73PEB8M (cyhalothrin)
[Em] Entry month:1801
[Cu] Class update date: 180122
[Lr] Last revision date:180122
[Js] Journal subset:IM
[Da] Date of entry for processing:171004
[St] Status:MEDLINE

  7 / 5377 MEDLINE  
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[PMID]: 29272308
[Au] Autor:Poplawski P; Wisniewski JR; Rijntjes E; Richards K; Rybicka B; Köhrle J; Piekielko-Witkowska A
[Ad] Address:Department of Biochemistry and Molecular Biology, Centre of Postgraduate Medical Education, Warsaw, Poland.
[Ti] Title:Restoration of type 1 iodothyronine deiodinase expression in renal cancer cells downregulates oncoproteins and affects key metabolic pathways as well as anti-oxidative system.
[So] Source:PLoS One;12(12):e0190179, 2017.
[Is] ISSN:1932-6203
[Cp] Country of publication:United States
[La] Language:eng
[Ab] Abstract:Type 1 iodothyronine deiodinase (DIO1) contributes to deiodination of 3,5,3',5'-tetraiodo-L-thyronine (thyroxine, T4) yielding of 3,5,3'-triiodothyronine (T3), a powerful regulator of cell differentiation, proliferation, and metabolism. Our previous work showed that loss of DIO1 enhances proliferation and migration of renal cancer cells. However, the global effects of DIO1 expression in various tissues affected by cancer remain unknown. Here, the effects of stable DIO1 re-expression were analyzed on the proteome of renal cancer cells, followed by quantitative real-time PCR validation in two renal cancer-derived cell lines. DIO1-induced changes in intracellular concentrations of thyroid hormones were quantified by L-MS/MS and correlations between expression of DIO1 and potential target genes were determined in tissue samples from renal cancer patients. Stable re-expression of DIO1, resulted in 26 downregulated proteins while 59 proteins were overexpressed in renal cancer cells. The 'downregulated' group consisted mainly of oncoproteins (e.g. STAT3, ANPEP, TGFBI, TGM2) that promote proliferation, migration and invasion. Furthermore, DIO1 re-expression enhanced concentrations of two subunits of thyroid hormone transporter (SLC7A5, SLC3A2), enzymes of key pathways of cellular energy metabolism (e.g. TKT, NAMPT, IDH2), sex steroid metabolism and anti-oxidative response (AKR1C2, AKR1B10). DIO1 expression resulted in elevated intracellular concentration of T4. Expression of DIO1-affected genes strongly correlated with DIO1 transcript levels in tissue samples from renal cancer patients as well as with their poor survival. This first study addressing effects of deiodinase re-expression on proteome of cancer cells demonstrates that induced DIO1 re-expression in renal cancer robustly downregulates oncoproteins, affects key metabolic pathways, and triggers proteins involved in anti-oxidative protection. This data supports the notion that suppressed DIO1 expression and changes in local availability of thyroid hormones might favor a shift from a differentiated to a more proliferation-prone state of cancer tissues and cell lines.
[Mh] MeSH terms primary: Antioxidants/metabolism
Down-Regulation
Iodide Peroxidase/metabolism
Kidney Neoplasms/enzymology
Oncogene Proteins/metabolism
[Mh] MeSH terms secundary: Cell Line, Tumor
Humans
Kidney Neoplasms/metabolism
Kidney Neoplasms/pathology
Proteomics
Real-Time Polymerase Chain Reaction
Thyroxine/metabolism
[Pt] Publication type:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T; VALIDATION STUDIES
[Nm] Name of substance:0 (Antioxidants); 0 (Oncogene Proteins); EC 1.11.1.- (iodothyronine deiodinase type I); EC 1.11.1.8 (Iodide Peroxidase); Q51BO43MG4 (Thyroxine)
[Em] Entry month:1801
[Cu] Class update date: 180116
[Lr] Last revision date:180116
[Js] Journal subset:IM
[Da] Date of entry for processing:171223
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0190179

  8 / 5377 MEDLINE  
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[PMID]: 28743556
[Au] Autor:Martinez B; Scheibner M; Soñanez-Organis JG; Jaques JT; Crocker DE; Ortiz RM
[Ad] Address:Department of Molecular and Cellular Biology, University of California Merced, 5200 North Lake Road, Merced, CA 95343, USA. Electronic address: bmartinez26@ucmerced.edu.
[Ti] Title:Increased sensitivity of thyroid hormone-mediated signaling despite prolonged fasting.
[So] Source:Gen Comp Endocrinol;252:36-47, 2017 Oct 01.
[Is] ISSN:1095-6840
[Cp] Country of publication:United States
[La] Language:eng
[Ab] Abstract:Thyroid hormones (TH) can increase cellular metabolism. Food deprivation in mammals is typically associated with reduced thyroid gland responsiveness, in an effort to suppress cellular metabolism and abate starvation. However, in prolonged-fasted, elephant seal pups, cellular TH-mediated proteins are up-regulated and TH levels are maintained with fasting duration. The function and contribution of the thyroid gland to this apparent paradox is unknown and physiologically perplexing. Here we show that the thyroid gland remains responsive during prolonged food deprivation, and that its function and production of TH increase with fasting duration in elephant seals. We discovered that our modeled plasma TH data in response to exogenous thyroid stimulating hormone predicted cellular signaling, which was corroborated independently by the enzyme expression data. The data suggest that the regulation and function of the thyroid gland in the northern elephant seal is atypical for a fasted animal, and can be better described as, "adaptive fasting". Furthermore, the modeling data help substantiate the in vivo responses measured, providing unique insight on hormone clearance, production rates, and thyroid gland responsiveness. Because these unique endocrine responses occur simultaneously with a nearly strict reliance on the oxidation of lipid, these findings provide an intriguing model to better understand the TH-mediated reliance on lipid metabolism that is not otherwise present in morbidly obese humans. When coupled with cellular, tissue-specific responses, these data provide a more integrated assessment of thyroidal status that can be extrapolated for many fasting/food deprived mammals.
[Mh] MeSH terms primary: Fasting/metabolism
Seals, Earless/metabolism
Signal Transduction
Thyroid Hormones/metabolism
[Mh] MeSH terms secundary: Animals
Fasting/blood
Iodide Peroxidase/metabolism
Models, Biological
RNA, Messenger/genetics
RNA, Messenger/metabolism
Receptors, Thyroid Hormone/metabolism
Seals, Earless/blood
Thyroid Hormones/blood
Thyroid Hormones/genetics
[Pt] Publication type:JOURNAL ARTICLE
[Nm] Name of substance:0 (RNA, Messenger); 0 (Receptors, Thyroid Hormone); 0 (Thyroid Hormones); EC 1.11.1.8 (Iodide Peroxidase)
[Em] Entry month:1712
[Cu] Class update date: 171222
[Lr] Last revision date:171222
[Js] Journal subset:IM
[Da] Date of entry for processing:170727
[St] Status:MEDLINE

  9 / 5377 MEDLINE  
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[PMID]: 29183601
[Au] Autor:Luo X; Liu Z; Sunohara Y; Matsumoto H; Li P
[Ad] Address:College of Agronomy and Plant Protection, Qingdao Agricultural University, Key Lab of Integrated Crop Pest Management of Shandong Province, Qingdao, Shandong, 266109, China. Electronic address: luo-xiaoyong@163.com.
[Ti] Title:Involvement of H O in fluazifop-P-butyl-induced cell death in bristly starbur seedlings.
[So] Source:Pestic Biochem Physiol;143:258-264, 2017 Nov.
[Is] ISSN:1095-9939
[Cp] Country of publication:United States
[La] Language:eng
[Ab] Abstract:In order to understand the action mechanism of fluazifop-P-butyl (FB) in bristly starbur (Acanthospermum hispidum D.C.), a susceptible plant, the role of active oxygen species (ROS) in herbicide-induced cell death in shoots was investigated. FB-induced phytotoxicity was not reduced by the antioxidants, 1,4-diazabicyclooctane (dabaco), sodium azide, l-tryptophan, d-tryptophan, hydroquinone and dimethyl pyridine N-oxide (DMPO). The activities of superoxide dismutase (SOD) and catalase (CAT), in bristly starbur seedlings were significantly increased by FB at 12 HAT and 24 HAT, while ascorbate peroxidase (APX) and glutathione reductase (GR) activities increased only at 12 HAT. The contents of H O in FB-treated bristly starbur seedlings were significantly higher to that of control between 8 and 24 HAT. According to the analysis of potassium iodide - starch or 3,3-diaminobenzidine, the accumulation of hydrogen peroxide was observed in the apical growing point, stem, petiole and veins of FB-treated bristly starbur seedlings at 24 HAT. The cell viability of bristly starbur seedlings treated by 10µM FB decreased at 18 HAT. These results suggested that FB-induced cell death in bristly starbur shoots may be caused by ROS (O and H O ) generation and lipid peroxidation.
[Pt] Publication type:JOURNAL ARTICLE
[Em] Entry month:1711
[Cu] Class update date: 171129
[Lr] Last revision date:171129
[St] Status:In-Process

  10 / 5377 MEDLINE  
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[PMID]: 29152653
[Au] Autor:Ma WW; Zhao L; Yuan LH; Yu HL; Wang H; Gong XY; Wei F; Xiao R
[Ad] Address:Department of Nutrition and Food Hygiene, School of Public Health, Beijing Key Laboratory of Environmental Toxicology, Capital Medical University, Beijing 100069, P.R. China.
[Ti] Title:Elaidic acid induces cell apoptosis through induction of ROS accumulation and endoplasmic reticulum stress in SH­SY5Y cells.
[So] Source:Mol Med Rep;, 2017 Oct 19.
[Is] ISSN:1791-3004
[Cp] Country of publication:Greece
[La] Language:eng
[Ab] Abstract:Elaidic acid, which is a major trans fatty acid, has been reported to be involved in neurotoxicity; however, the underlying molecular mechanisms underlying its neurotoxic effects remain largely unknown. Therefore, the present study aimed to investigate the potential mechanisms underlying elaidic acid­induced neuronal damage in vitro. The SH­SY5Y neuroblastoma cell line was used as a model in the present study. Following treatment of cells with various concentrations of elaidic acid or with vehicle for 24 h, cell viability was measured using the MTT assay. Mitochondrial membrane potential (MMP) and reactive oxygen species (ROS) release were measured using flow cytometry. Cell apoptosis was measured by Annexin V­fluorescein isothiocyanate/propidium iodide double staining, and cellular redox status was determined using ELISA analysis. Furthermore, western blotting was used to detect the protein expression levels of factors associated with oxidative damage and components of the endoplasmic reticulum (ER) stress/unfolded protein response (UPR) signaling pathways. The results demonstrated that elaidic acid treatment inhibited cell viability, elevated cell apoptosis and resulted in a loss of MMP. In addition, elaidic acid induced marked alterations in cellular redox status. Treatment with high doses of elaidic acid treatment also enhanced the release of ROS, and upregulated lipid peroxide and malondialdehyde levels; however, it reduced superoxide dismutase and glutathione peroxidase activities. Furthermore, elaidic acid resulted in upregulation of nuclear factor erythroid 2­related factor 2 and downregulation of heme oxygenase 1, which are two key antioxidative factors. Elaidic acid treatment also induced or inhibited the expression of numerous ER stress/UPR­associated molecules. It induced glucose­regulated protein 78 (GRP78) expression, whereas the expression levels of activating transcription factor 4 (ATF4) and CCAAT/enhancer­binding protein homologous protein (CHOP) were upregulated and then downregulated following treatment with various doses of elaidic acid. These results indicated that elaidic acid inhibited SH­SY5Y cell growth and induced apoptosis by enhancing oxidative stress and activating the ER stress/UPR signaling pathway and the GRP78/ATF4/CHOP pathway.
[Pt] Publication type:JOURNAL ARTICLE
[Em] Entry month:1711
[Cu] Class update date: 171120
[Lr] Last revision date:171120
[St] Status:Publisher
[do] DOI:10.3892/mmr.2017.7830


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BIREME/PAHO/WHO - Latin American and Caribbean Center on Health Sciences Information