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Pesquisa : D08.811.520.241.300.050.500 [Categoria DeCS]
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[PMID]:28939752
[Au] Autor:Outten CE
[Ad] Endereço:From the Department of Chemistry and Biochemistry, University of South Carolina, Columbia, South Carolina 29208 outten@sc.edu.
[Ti] Título:Checks and balances for the iron bank.
[So] Source:J Biol Chem;292(38):15990-15991, 2017 Sep 22.
[Is] ISSN:1083-351X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The RNA-binding iron regulatory proteins IRP1 and IRP2 are inactivated by either Fe-S cluster insertion or protein degradation mediated by the E3 ligase component FBXL5. However, the mechanisms for coordination between Fe-S cluster assembly, FBXL5, and IRP1/IRP2 activity are poorly defined. A new study reveals that FBXL5 plays a critical role in limiting IRP1 and IRP2 overaccumulation when cytosolic Fe-S cluster assembly is impaired in order to maintain optimal iron levels for cell viability.
[Mh] Termos MeSH primário: Ferro/metabolismo
[Mh] Termos MeSH secundário: Sobrevivência Celular
Citosol/metabolismo
Proteínas F-Box/metabolismo
Proteína 1 Reguladora do Ferro/metabolismo
Proteína 2 Reguladora do Ferro/metabolismo
Enxofre/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (F-Box Proteins); 70FD1KFU70 (Sulfur); E1UOL152H7 (Iron); EC 4.2.1.3 (Iron Regulatory Protein 1); EC 4.2.1.3 (Iron Regulatory Protein 2)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171009
[Lr] Data última revisão:
171009
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170924
[St] Status:MEDLINE
[do] DOI:10.1074/jbc.H117.785741


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[PMID]:28768766
[Au] Autor:Johnson NB; Deck KM; Nizzi CP; Eisenstein RS
[Ad] Endereço:From the Department of Nutritional Sciences, University of Wisconsin, Madison, Wisconsin 53706.
[Ti] Título:A synergistic role of IRP1 and FBXL5 proteins in coordinating iron metabolism during cell proliferation.
[So] Source:J Biol Chem;292(38):15976-15989, 2017 Sep 22.
[Is] ISSN:1083-351X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Iron-regulatory protein 1 (IRP1) belongs to a family of RNA-binding proteins that modulate metazoan iron metabolism. Multiple mechanisms are employed to control the action of IRP1 in dictating changes in the uptake and metabolic fate of iron. Inactivation of IRP1 RNA binding by iron primarily involves insertion of a [4Fe-4S] cluster by the cytosolic iron-sulfur cluster assembly (CIA) system, converting it into cytosolic aconitase (c-acon), but can also involve iron-mediated degradation of IRP1 by the E3 ligase FBXL5 that also targets IRP2. How CIA and FBXL5 collaborate to maintain cellular iron homeostasis through IRP1 and other pathways is poorly understood. Because impaired Fe-S cluster biogenesis associates with human disease, we determined the importance of FBXL5 for regulating IRP1 when CIA is impaired. Suppression of FBXL5 expression coupled with induction of an IRP1 mutant (IRP1 ) that cannot insert the Fe-S cluster, or along with knockdown of the CIA factors NUBP2 or FAM96A, reduced cell viability. Iron supplementation reversed this growth defect and was associated with FBXL5-dependent polyubiquitination of IRP1. Phosphorylation of IRP1 at Ser-138 increased when CIA was inhibited and was required for iron rescue. Impaired CIA activity, as noted by reduced c-acon activity, was associated with enhanced FBXL5 expression and a concomitant reduction in IRP1 and IRP2 protein level and RNA-binding activity. Conversely, expression of either IRP induced FBXL5 protein level, demonstrating a negative feedback loop limiting excessive accumulation of iron-response element RNA-binding activity, whose disruption reduces cell growth. We conclude that a regulatory circuit involving FBXL5 and CIA acts through both IRPs to control iron metabolism and promote optimal cell growth.
[Mh] Termos MeSH primário: Proteínas F-Box/metabolismo
Proteína 1 Reguladora do Ferro/metabolismo
Ferro/metabolismo
Complexos Ubiquitina-Proteína Ligase/metabolismo
[Mh] Termos MeSH secundário: Proteínas F-Box/genética
Ferritinas/metabolismo
Técnicas de Silenciamento de Genes
Células HEK293
Seres Humanos
Proteína 1 Reguladora do Ferro/química
Proteína 2 Reguladora do Ferro/metabolismo
Fosforilação
Complexo de Endopeptidases do Proteassoma/metabolismo
Proteólise
RNA/metabolismo
Serina/metabolismo
Enxofre/metabolismo
Complexos Ubiquitina-Proteína Ligase/deficiência
Complexos Ubiquitina-Proteína Ligase/genética
Ubiquitinação
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (F-Box Proteins); 0 (FBXL5 protein, human); 452VLY9402 (Serine); 63231-63-0 (RNA); 70FD1KFU70 (Sulfur); 9007-73-2 (Ferritins); E1UOL152H7 (Iron); EC 2.3.2.23 (Ubiquitin-Protein Ligase Complexes); EC 3.4.25.1 (Proteasome Endopeptidase Complex); EC 4.2.1.3 (Iron Regulatory Protein 1); EC 4.2.1.3 (Iron Regulatory Protein 2)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171009
[Lr] Data última revisão:
171009
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170804
[St] Status:MEDLINE
[do] DOI:10.1074/jbc.M117.785741


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[PMID]:28672025
[Au] Autor:Zhou S; Du X; Xie J; Wang J
[Ad] Endereço:Department of Physiology, Shandong Provincial Key Laboratory of Pathogenesis and Prevention of Neurological Disorders and State Key Disciplines: Physiology, Medical College of Qingdao University, Qingdao, China.
[Ti] Título:Interleukin-6 regulates iron-related proteins through c-Jun N-terminal kinase activation in BV2 microglial cell lines.
[So] Source:PLoS One;12(7):e0180464, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Parkinson's disease (PD) is a common neurodegenerative disorder characterized by the loss of dopaminergic (DA) neurons in the substantia nigra (SN) and subsequent DA depletion in the striatum. Microglia activation and nigral iron accumulation play important roles in the pathogenesis of PD. Activated microglia show increased iron deposits. However, the relationship between microglia activation and iron accumulation remains unclear. In the present study, we aimed to determine how iron levels affect interleukin-6 (IL-6) synthesis, and the effect of IL-6 on cellular iron metabolism in BV2 microglial cells.IL-6 mRNA was up-regulated after FAC treatment for 12 h in BV2 cells. Iron regulatory protein 1 (IRP1) and divalent metal transporter 1 (DMT1) were up-regulated and iron exporter ferroportin 1 (FPN1) was down-regulated in BV2 cells after 24 h of IL-6 treatment. Phosphorylated JNK increased significantly compared to the control after BV2 cells were treated with IL-6 for 1 h. Pretreatment with SP600125 attenuated the up-regulation of IRP1 and DMT1 and down-regulation of FPN1 (compared to IL-6-treated group). These results suggest that iron load could increase IL-6 mRNA expression in BV2 cells. Further, IL-6 likely up-regulates IRP1 and DMT1 expression and down-regulates FPN1 expression in BV2 microglial cells through JNK signaling pathways.
[Mh] Termos MeSH primário: Proteínas de Transporte de Cátions/metabolismo
Interleucina-6/fisiologia
Proteína 1 Reguladora do Ferro/metabolismo
Proteínas Quinases JNK Ativadas por Mitógeno/metabolismo
Microglia/metabolismo
[Mh] Termos MeSH secundário: Animais
Western Blotting
Linhagem Celular
Ativação Enzimática
Compostos Férricos/farmacologia
Interleucina-6/genética
Camundongos
Microglia/citologia
Microglia/efeitos dos fármacos
Microglia/enzimologia
Compostos de Amônio Quaternário/farmacologia
RNA Mensageiro/genética
Reação em Cadeia da Polimerase em Tempo Real
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Cation Transport Proteins); 0 (Ferric Compounds); 0 (Interleukin-6); 0 (Quaternary Ammonium Compounds); 0 (RNA, Messenger); 0 (solute carrier family 11- (proton-coupled divalent metal ion transporters), member 2); EC 2.7.11.24 (JNK Mitogen-Activated Protein Kinases); EC 4.2.1.3 (Iron Regulatory Protein 1); UVP74NG1C5 (ferric ammonium citrate)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171006
[Lr] Data última revisão:
171006
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170704
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0180464


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[PMID]:28615439
[Au] Autor:Rouault TA; Maio N
[Ad] Endereço:From the Molecular Medicine Branch, Eunice Kennedy Shriver NICHD, National Institutes of Health, Bethesda, Maryland 20892 rouault@mail.nih.gov.
[Ti] Título:Biogenesis and functions of mammalian iron-sulfur proteins in the regulation of iron homeostasis and pivotal metabolic pathways.
[So] Source:J Biol Chem;292(31):12744-12753, 2017 Aug 04.
[Is] ISSN:1083-351X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Fe-S cofactors are composed of iron and inorganic sulfur in various stoichiometries. A complex assembly pathway conducts their initial synthesis and subsequent binding to recipient proteins. In this minireview, we discuss how discovery of the role of the mammalian cytosolic aconitase, known as iron regulatory protein 1 (IRP1), led to the characterization of the function of its Fe-S cluster in sensing and regulating cellular iron homeostasis. Moreover, we present an overview of recent studies that have provided insights into the mechanism of Fe-S cluster transfer to recipient Fe-S proteins.
[Mh] Termos MeSH primário: Homeostase
Proteína 1 Reguladora do Ferro/fisiologia
Ferro/fisiologia
Modelos Moleculares
[Mh] Termos MeSH secundário: Animais
Apoenzimas/química
Apoenzimas/metabolismo
Liases de Carbono-Enxofre/biossíntese
Liases de Carbono-Enxofre/química
Liases de Carbono-Enxofre/fisiologia
Transporte de Elétrons
Regulação Enzimológica da Expressão Gênica
Proteínas de Choque Térmico HSP70/biossíntese
Proteínas de Choque Térmico HSP70/química
Proteínas de Choque Térmico HSP70/fisiologia
Seres Humanos
Proteína 1 Reguladora do Ferro/biossíntese
Proteína 1 Reguladora do Ferro/química
Proteínas de Ligação ao Ferro/biossíntese
Proteínas de Ligação ao Ferro/química
Proteínas de Ligação ao Ferro/fisiologia
Proteínas Reguladoras do Ferro/biossíntese
Proteínas Reguladoras do Ferro/química
Proteínas Reguladoras do Ferro/fisiologia
Proteínas com Ferro-Enxofre/biossíntese
Proteínas com Ferro-Enxofre/química
Proteínas com Ferro-Enxofre/fisiologia
Proteínas Mitocondriais/biossíntese
Proteínas Mitocondriais/química
Proteínas Mitocondriais/fisiologia
Chaperonas Moleculares/biossíntese
Chaperonas Moleculares/química
Chaperonas Moleculares/fisiologia
Dobramento de Proteína
Domínios e Motivos de Interação entre Proteínas
Multimerização Proteica
Elementos de Resposta
Succinato Desidrogenase/biossíntese
Succinato Desidrogenase/química
Succinato Desidrogenase/fisiologia
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Apoenzymes); 0 (HSCB protein, human); 0 (HSP70 Heat-Shock Proteins); 0 (HSPA9 protein, human); 0 (ISCU protein, human); 0 (ISD11 protein, human); 0 (Iron-Binding Proteins); 0 (Iron-Regulatory Proteins); 0 (Iron-Sulfur Proteins); 0 (Mitochondrial Proteins); 0 (Molecular Chaperones); 0 (frataxin); E1UOL152H7 (Iron); EC 1.3.5.1 (SDHB protein, human); EC 1.3.99.1 (Succinate Dehydrogenase); EC 4.2.1.3 (IRP1 protein, human); EC 4.2.1.3 (Iron Regulatory Protein 1); EC 4.4.- (Carbon-Sulfur Lyases); EC 4.4.1.- (NFS1 protein, human)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170825
[Lr] Data última revisão:
170825
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170616
[St] Status:MEDLINE
[do] DOI:10.1074/jbc.R117.789537


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[PMID]:28542246
[Au] Autor:Milczarek A; Starzynski RR; Stys A; Jonczy A; Staron R; Grzelak A; Lipinski P
[Ad] Endereço:Department of Molecular Biology, Institute of Genetics and Animal Breeding, Polish Academy of Sciences, Jastrzebiec, Poland.
[Ti] Título:A drastic superoxide-dependent oxidative stress is prerequisite for the down-regulation of IRP1: Insights from studies on SOD1-deficient mice and macrophages treated with paraquat.
[So] Source:PLoS One;12(5):e0176800, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Iron regulatory protein 1 (IRP1) is a cytosolic bifunctional [4Fe-4S] protein which exhibits aconitase activity or binds iron responsive elements (IREs) in untranslated regions of specific mRNA encoding proteins involved in cellular iron metabolism. Superoxide radical (O2.-) converts IRP1 from a [4Fe-4S] aconitase to a [3Fe-4S] "null" form possessing neither aconitase nor trans-regulatory activity. Genetic ablation of superoxide dismutase 1 (SOD1), an antioxidant enzyme that acts to reduce O2.- concentration, revealed a new O2.--dependent regulation of IRP1 leading to the reduction of IRP1 protein level and in consequence to the diminution of IRP1 enzymatic and IRE-binding activities. Here, we attempted to establish whether developmental changes in SOD1 activity occurring in the mouse liver, impact IRP1 expression. We show no correlation between hepatic SOD1 activity and IRP1 protein level neither in pre- nor postnatal period probably because the magnitude of developmental fluctuations in SOD1 activity is relatively small. The comparison of SOD1 activity in regards to IRP1 protein level in the liver of threeSOD1 genotypes (Sod1+/+, Sod1+/- and Sod1-/-) demonstrates that only drastic SOD1 deficiency leads to the reduction of IRP1 protein level. Importantly, we found that in the liver of fetuses lacking SOD1, IRP1 is not down-regulated. To investigate O2.--dependent regulation of IRP1 in a cellular model, we exposed murine RAW 264.7 and bone marrow-derived macrophages to paraquat, widely used as a redox cycler to stimulate O2.-production in cells. We showed that IRP1 protein level as well as aconitase and IRE-binding activities are strongly reduced in macrophages treated with paraquat. The analysis of the expression of IRP1-target genes revealed the increase in L-ferritin protein level resulting from the enhanced transcriptional regulation of the LFt gene and diminished translational repression of L-ferritin mRNA by IRP1. We propose that O2.--dependent up-regulation of this cellular protectant in paraquat-treated macrophages may counterbalance iron-related toxic effects of O2.-.
[Mh] Termos MeSH primário: Regulação para Baixo/efeitos dos fármacos
Proteína 1 Reguladora do Ferro/metabolismo
Macrófagos/efeitos dos fármacos
Estresse Oxidativo/efeitos dos fármacos
Paraquat/farmacologia
Superóxido Dismutase-1/deficiência
Superóxidos/metabolismo
[Mh] Termos MeSH secundário: Animais
Apoferritinas/genética
Relação Dose-Resposta a Droga
Regulação da Expressão Gênica/efeitos dos fármacos
Proteína 1 Reguladora do Ferro/genética
Rim/efeitos dos fármacos
Rim/metabolismo
Fígado/efeitos dos fármacos
Fígado/metabolismo
Macrófagos/citologia
Macrófagos/metabolismo
Camundongos
Células RAW 264.7
RNA Mensageiro/genética
RNA Mensageiro/metabolismo
Receptores de LDL/deficiência
Receptores de LDL/metabolismo
Proteínas Supressoras de Tumor/deficiência
Proteínas Supressoras de Tumor/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Lrp1 protein, mouse); 0 (RNA, Messenger); 0 (Receptors, LDL); 0 (Tumor Suppressor Proteins); 11062-77-4 (Superoxides); 9013-31-4 (Apoferritins); EC 1.15.1.1 (Superoxide Dismutase-1); EC 4.2.1.3 (Iron Regulatory Protein 1); PLG39H7695 (Paraquat)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170919
[Lr] Data última revisão:
170919
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170526
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0176800


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[PMID]:28178997
[Au] Autor:Meng FX; Hou JM; Sun TS
[Ad] Endereço:Third Military Medical University, No. 30 Gaotanyan Street, 400038, Chongqing, China.
[Ti] Título:Effect of oxidative stress induced by intracranial iron overload on central pain after spinal cord injury.
[So] Source:J Orthop Surg Res;12(1):24, 2017 Feb 08.
[Is] ISSN:1749-799X
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: Central pain (CP) is a common clinical problem in patients with spinal cord injury (SCI). Recent studies found the pathogenesis of CP was related to the remodeling of the brain. We investigate the roles of iron overload and subsequent oxidative stress in the remodeling of the brain after SCI. METHODS: We established a rat model of central pain after SCI. Rats were divided randomly into four groups: SCI, sham operation, SCI plus deferoxamine (DFX) intervention, and SCI plus nitric oxide synthase (NOS) inhibitor treatment. Pain behavior was observed and thermal pain threshold was measured regularly, and brain levels of iron, transferrin receptor 1 (TfR1), ferritin (Fn), and lactoferrin (Lf), were detected in the different groups 12 weeks after establishment of the model. RESULTS: Rats demonstrated self-biting behavior after SCI. Furthermore, the latent period of thermal pain was reduced and iron levels in the hind limb sensory area, hippocampus, and thalamus increased after SCI. Iron-regulatory protein (IRP) 1 levels increased in the hind limb sensory area, while Fn levels decreased. TfR1 mRNA levels were also increased and oxidative stress was activated. Oxidative stress could be inhibited by ferric iron chelators and NOS inhibitors. CONCLUSIONS: SCI may cause intracranial iron overload through the NOS-iron-responsive element/IRP pathway, resulting in central pain mediated by the oxidative stress response. Iron chelators and oxidative stress inhibitors can effectively relieve SCI-associated central pain.
[Mh] Termos MeSH primário: Sobrecarga de Ferro/complicações
Estresse Oxidativo/fisiologia
Dor/etiologia
Traumatismos da Medula Espinal/complicações
[Mh] Termos MeSH secundário: Animais
Encéfalo/metabolismo
Feminino
Ferritinas/metabolismo
Ferro/metabolismo
Sobrecarga de Ferro/metabolismo
Sobrecarga de Ferro/fisiopatologia
Proteína 1 Reguladora do Ferro/metabolismo
Lactoferrina/metabolismo
Malondialdeído/metabolismo
Dor/metabolismo
Dor/fisiopatologia
Medição da Dor/métodos
Limiar da Dor/fisiologia
Ratos Sprague-Dawley
Receptores da Transferrina/metabolismo
Traumatismos da Medula Espinal/metabolismo
Traumatismos da Medula Espinal/fisiopatologia
Superóxido Dismutase/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Receptors, Transferrin); 0 (Tfr1 protein, rat); 4Y8F71G49Q (Malondialdehyde); 9007-73-2 (Ferritins); E1UOL152H7 (Iron); EC 1.15.1.1 (Superoxide Dismutase); EC 3.4.21.- (Lactoferrin); EC 4.2.1.3 (Iron Regulatory Protein 1)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:170612
[Lr] Data última revisão:
170612
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170210
[St] Status:MEDLINE
[do] DOI:10.1186/s13018-017-0526-y


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[PMID]:27816562
[Au] Autor:Villafuerte BC; Barati MT; Rane MJ; Isaacs S; Li M; Wilkey DW; Merchant ML
[Ad] Endereço:Department of Medicine, University of Louisville, Louisville, KY, United States.
[Ti] Título:Over-expression of insulin-response element binding protein-1 (IRE-BP1) in mouse pancreatic islets increases expression of RACK1 and TCTP: Beta cell markers of high glucose sensitivity.
[So] Source:Biochim Biophys Acta;1865(2):186-194, 2017 02.
[Is] ISSN:0006-3002
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: A targeted analysis of the 50kDa C-terminal fragment of insulin-response element binding protein-1 (IRE-BP1) activation of target genes through the insulin receptor substrate receptor/PI-3 kinase/Akt pathway has been demonstrated for the insulin growth factor-1 receptor. The broader effects of 50kDa C-terminal IRE-BP1 fragment over-expression on protein abundance in pancreatic islet beta cells have not been determined. RESULTS: Liquid-chromatography coupled to tandem mass spectrometry (LC-MS/MS) analyses of replicate lysates of pancreatic islets isolated from background strain animals and transgenic animals, overexpressing IRE-BP1 in pancreatic islet beta cells, demonstrated statistically significant increases in the expression of proteins involved in protein synthesis, endoplasmic reticulum (ER) stress and scaffolding proteins important for protein kinase C signaling; some of which were confirmed by immunoblot analyses. Bioinformatic analysis of protein expression network patterns suggested IRE-BP1 over-expression leads to protein expression patterns indicative of activation of functional protein networks utilized for protein post-translational modification, protein folding, and protein synthesis. Co-immunoprecipitation experiments demonstrate a novel interaction between two differentially regulated proteins receptor for activated protein kinase C (RACK1) and translationally controlled tumor protein (TCTP). CONCLUSIONS: Proteomic analysis of IRE-BP1 over-expression in pancreatic islet beta cells suggest IRE-BP1 (a) directly or indirectly through establishing hyperglycemia results in increased expression of ribosomal proteins and markers of ER stress and (b) leads to the enhanced and previously un-described interaction of RACK1 and TCTP. SIGNIFICANCE: This study identified C-terminal 50kDa domain of IRE-BP1 over-expression results in increased markers of ER-stress and a novel interaction between the scaffolding proteins RACK1 and TCTP.
[Mh] Termos MeSH primário: Biomarcadores Tumorais/metabolismo
Biomarcadores/metabolismo
Glucose/metabolismo
Células Secretoras de Insulina/metabolismo
Proteína 1 Reguladora do Ferro/metabolismo
Ilhotas Pancreáticas/metabolismo
Neuropeptídeos/metabolismo
[Mh] Termos MeSH secundário: Animais
Estresse do Retículo Endoplasmático/fisiologia
Hiperglicemia
Insulina/metabolismo
Camundongos
Proteína Quinase C/metabolismo
Processamento de Proteína Pós-Traducional/fisiologia
Proteômica/métodos
Receptores de Quinase C Ativada
Elementos de Resposta/fisiologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Biomarkers); 0 (Biomarkers, Tumor); 0 (Insulin); 0 (Neuropeptides); 0 (RACK1 protein, mouse); 0 (Receptors for Activated C Kinase); 0 (tumor protein, translationally-controlled 1); EC 2.7.11.13 (Protein Kinase C); EC 4.2.1.3 (Iron Regulatory Protein 1); IY9XDZ35W2 (Glucose)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161107
[St] Status:MEDLINE


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[PMID]:27999284
[Au] Autor:Li WY; Li FM; Zhou YF; Wen ZM; Ma J; Ya K; Qian ZM
[Ad] Endereço:Laboratory of Neuropharmacology, Fudan University School of Pharmacy, Shanghai 201203, China. lj19840208@126.com.
[Ti] Título:Aspirin down Regulates Hepcidin by Inhibiting NF-κB and IL6/JAK2/STAT3 Pathways in BV-2 Microglial Cells Treated with Lipopolysaccharide.
[So] Source:Int J Mol Sci;17(12), 2016 Dec 16.
[Is] ISSN:1422-0067
[Cp] País de publicação:Switzerland
[La] Idioma:eng
[Ab] Resumo:Aspirin down regulates transferrin receptor 1 (TfR1) and up regulates ferroportin 1 (Fpn1) and ferritin expression in BV-2 microglial cells treated without lipopolysaccharides (LPS), as well as down regulates hepcidin and interleukin 6 (IL-6) in cells treated with LPS. However, the relevant mechanisms are unknown. Here, we investigate the effects of aspirin on expression of hepcidin and iron regulatory protein 1 (IRP1), phosphorylation of Janus kinase 2 (JAK2), signal transducer and activator of transcription 3 (STAT3) and P65 (nuclear factor-κB), and the production of nitric oxide (NO) in BV-2 microglial cells treated with and without LPS. We demonstrated that aspirin inhibited hepcidin mRNA as well as NO production in cells treated with LPS, but not in cells without LPS, suppresses IL-6, JAK2, STAT3, and P65 (nuclear factor-κB) phosphorylation and has no effect on IRP1 in cells treated with or without LPS. These findings provide evidence that aspirin down regulates hepcidin by inhibiting IL6/JAK2/STAT3 and P65 (nuclear factor-κB) pathways in the cells under inflammatory conditions, and imply that an aspirin-induced reduction in TfR1 and an increase in ferritin are not associated with IRP1 and NO.
[Mh] Termos MeSH primário: Aspirina/farmacologia
Hepcidinas/biossíntese
Interleucina-6/antagonistas & inibidores
Janus Quinase 2/antagonistas & inibidores
Lipopolissacarídeos/toxicidade
Microglia/efeitos dos fármacos
Fator de Transcrição STAT3/antagonistas & inibidores
Fator de Transcrição RelA/antagonistas & inibidores
[Mh] Termos MeSH secundário: Animais
Linhagem Celular
Hepcidinas/genética
Inflamação/patologia
Proteína 1 Reguladora do Ferro/biossíntese
Janus Quinase 2/metabolismo
Camundongos
Óxido Nítrico/biossíntese
Fosforilação/efeitos dos fármacos
RNA Mensageiro/biossíntese
Fator de Transcrição STAT3/metabolismo
Transdução de Sinais/efeitos dos fármacos
Fator de Transcrição RelA/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Hepcidins); 0 (Interleukin-6); 0 (Lipopolysaccharides); 0 (RNA, Messenger); 0 (Rela protein, mouse); 0 (STAT3 Transcription Factor); 0 (Stat3 protein, mouse); 0 (Transcription Factor RelA); 0 (interleukin-6, mouse); 31C4KY9ESH (Nitric Oxide); EC 2.7.10.2 (Jak2 protein, mouse); EC 2.7.10.2 (Janus Kinase 2); EC 4.2.1.3 (Iron Regulatory Protein 1); R16CO5Y76E (Aspirin)
[Em] Mês de entrada:1704
[Cu] Atualização por classe:170407
[Lr] Data última revisão:
170407
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161222
[St] Status:MEDLINE


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[PMID]:27766034
[Au] Autor:Luo QQ; Qian ZM; Zhou YF; Zhang MW; Wang D; Zhu L; Ke Y
[Ad] Endereço:Department of Biochemistry, Institute for Nautical Medicine, Nantong University, Nantong, 226001, China; Laboratory of Neuropharmacology, FudanUniversity School of Pharmacy,826 Zhang Heng Road, Pu Dong, Shanghai201203, China.
[Ti] Título:Expression of Iron Regulatory Protein 1 Is Regulated not only by HIF-1 but also pCREB under Hypoxia.
[So] Source:Int J Biol Sci;12(10):1191-1202, 2016.
[Is] ISSN:1449-2288
[Cp] País de publicação:Australia
[La] Idioma:eng
[Ab] Resumo:The inconsistent of responses of IRP1 and HIF-1 alpha to hypoxia and the similar tendencies in the changes of IRP1 and pCREB contents led us to hypothesize that pCREB might be involved in the regulation of IRP1 under hypoxia. Here, we investigated the role of pCREB in IRP1 expression in HepG2 cells under hypoxia using quantitative PCR, western blot, immunofluorescence, electrophoretic mobility shift assay (EMSA) and chromatin immunoprecipitation (ChIP). We demonstrated that 1) Hypoxia increased pCREB levels inside of the nucleus; 2) Putative CREs were found in the IRP1 gene; 3) Nuclear extracts of HepG2 cells treated with hypoxia could bind to CRE1 and CRE3, and 100-fold competitor of putative CREs could abolish the binding activity to varying degrees; 4) pCREB was found in the CRE1 and CRE3 DNA-protein complexes of EMSA; 5) CRE1 and CRE3 binding activity of IRP1 depended on CREB activation but not on HIF-1; 6) Increased IRP1 expression under hypoxia could be prevented by LY294002; 7) ChIP assays demonstrated that pCREB binds to IRP1 promoter; and 8) HIF-1 and/or HIF-2 siRNA had no effect on the expression of pCREB and IRP1 proteins in cells treated with hypoxia for 8 hours. Our findings evidenced for the involvement of pCREB in IRP1 expression and revealed a dominant role of PI3K/Akt pathway in CREB activation under hypoxia and also suggested that dual-regulation of IRP1 expression by HIF-1 and pCERB or other transcription factor(s) under hypoxia might be a common mechanism in most if not all of hypoxia-inducible genes.
[Mh] Termos MeSH primário: Proteína de Ligação ao Elemento de Resposta ao AMP Cíclico/metabolismo
Subunidade alfa do Fator 1 Induzível por Hipóxia/metabolismo
Proteína 1 Reguladora do Ferro/metabolismo
[Mh] Termos MeSH secundário: Fatores de Transcrição Hélice-Alça-Hélice Básicos/genética
Fatores de Transcrição Hélice-Alça-Hélice Básicos/metabolismo
Western Blotting
Hipóxia Celular/genética
Hipóxia Celular/fisiologia
Sobrevivência Celular/genética
Sobrevivência Celular/fisiologia
Imunoprecipitação da Cromatina
Proteína de Ligação ao Elemento de Resposta ao AMP Cíclico/genética
Ensaio de Desvio de Mobilidade Eletroforética
Imunofluorescência
Células Hep G2
Seres Humanos
Subunidade alfa do Fator 1 Induzível por Hipóxia/genética
Proteína 1 Reguladora do Ferro/genética
RNA Interferente Pequeno
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Basic Helix-Loop-Helix Transcription Factors); 0 (Cyclic AMP Response Element-Binding Protein); 0 (Hypoxia-Inducible Factor 1, alpha Subunit); 0 (RNA, Small Interfering); 0 (endothelial PAS domain-containing protein 1); EC 4.2.1.3 (Iron Regulatory Protein 1)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171020
[Lr] Data última revisão:
171020
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161022
[St] Status:MEDLINE


  10 / 368 MEDLINE  
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Texto completo
[PMID]:27380194
[Au] Autor:Yamamoto M; Tanaka H; Toki Y; Hatayama M; Ito S; Addo L; Shindo M; Sasaki K; Ikuta K; Ohtake T; Fujiya M; Torimoto Y; Kohgo Y
[Ad] Endereço:Division of Gastroenterology and Hematology/Oncology, Asahikawa Medical University, Asahikawa, Hokkaido, Japan.
[Ti] Título:Iron-induced epigenetic abnormalities of mouse bone marrow through aberrant activation of aconitase and isocitrate dehydrogenase.
[So] Source:Int J Hematol;104(4):491-501, 2016 Oct.
[Is] ISSN:1865-3774
[Cp] País de publicação:Japan
[La] Idioma:eng
[Ab] Resumo:Iron overload remains a concern in myelodysplastic syndrome (MDS) patients. Iron chelation therapy (ICT) thus plays an integral role in the management of these patients. Moreover, ICT has been shown to prolong leukemia-free survival in MDS patients; however, the mechanisms responsible for this effect are unclear. Iron is a key molecule for regulating cytosolic aconitase 1 (ACO1). Additionally, the mutation of isocitrate dehydrogenase (IDH), the enzyme downstream of ACO1 in the TCA cycle, is associated with epigenetic abnormalities secondary to 2-hydroxyglutarate (2-HG) and DNA methylation. However, epigenetic abnormalities observed in many MDS patients occur without IDH mutation. We hypothesized that iron itself activates the ACO1-IDH pathway, which may increase 2-HG and DNA methylation, and eventually contribute to leukemogenesis without IDH mutation. Using whole RNA sequencing of bone marrow cells in iron-overloaded mice, we observed that the enzymes, phosphoglucomutase 1, glycogen debranching enzyme, and isocitrate dehydrogenase 1 (Idh1), which are involved in glycogen and glucose metabolism, were increased. Digital PCR further showed that Idh1 and Aco1, enzymes involved in the TCA cycle, were also elevated. Additionally, enzymatic activities of TCA cycle and methylated DNA were increased. Iron chelation reversed these phenomena. In conclusion, iron activation of glucose metabolism causes an increase of 2-HG and DNA methylation.
[Mh] Termos MeSH primário: Medula Óssea/metabolismo
Metilação de DNA/efeitos dos fármacos
Proteína 1 Reguladora do Ferro/metabolismo
Ferro/farmacologia
Isocitrato Desidrogenase/metabolismo
[Mh] Termos MeSH secundário: Animais
Carcinogênese/induzido quimicamente
Glucose/metabolismo
Glutaratos/sangue
Proteína 1 Reguladora do Ferro/efeitos dos fármacos
Isocitrato Desidrogenase/efeitos dos fármacos
Camundongos
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Glutarates); 2889-31-8 (alpha-hydroxyglutarate); E1UOL152H7 (Iron); EC 1.1.1.41 (Isocitrate Dehydrogenase); EC 4.2.1.3 (Iron Regulatory Protein 1); IY9XDZ35W2 (Glucose)
[Em] Mês de entrada:1703
[Cu] Atualização por classe:171109
[Lr] Data última revisão:
171109
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160706
[St] Status:MEDLINE
[do] DOI:10.1007/s12185-016-2054-7



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