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[PMID]:27771699
[Au] Autor:van Breda GF; Bongartz LG; Zhuang W; van Swelm RP; Pertijs J; Braam B; Cramer MJ; Swinkels DW; Doevendans PA; Verhaar MC; Masereeuw R; Joles JA; Gaillard CA
[Ad] Endereço:Department of Nephrology and Immunology, University of Alberta, Edmonton, Alta., Canada.
[Ti] Título:Cardiac Hepcidin Expression Associates with Injury Independent of Iron.
[So] Source:Am J Nephrol;44(5):368-378, 2016.
[Is] ISSN:1421-9670
[Cp] País de publicação:Switzerland
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: Hepcidin regulates systemic iron homeostasis by downregulating the iron exporter ferroportin. Circulating hepcidin is mainly derived from the liver but hepcidin is also produced in the heart. We studied the differential and local regulation of hepcidin gene expression in response to myocardial infarction (MI) and/or chronic kidney disease (CKD). We hypothesized that cardiac hepcidin gene expression is induced by and regulated to severity of cardiac injury, either through direct (MI) or remote (CKD) stimuli, as well as through increased local iron content. METHODS: Nine weeks after subtotal nephrectomy (SNX) or sham surgery (CON), rats were subjected to coronary ligation (CL) or sham surgery to realize 4 groups: CON, SNX, CL and SNX + CL. In week 16, the gene expression of hepcidin, iron and damage markers in cardiac and liver tissues was assessed by quantitative polymerase chain reaction and ferritin protein expression was studied by immunohistochemistry. RESULTS: Cardiac hepcidin messenger RNA (mRNA) expression was increased 2-fold in CL (p = 0.03) and 3-fold in SNX (p = 0.01). Cardiac ferritin staining was not different among groups. Cardiac hepcidin mRNA expression correlated with mRNA expression levels of brain natriuretic peptide (ß = 0.734, p < 0.001) and connective tissue growth factor (ß = 0.431, p = 0.02). In contrast, liver hepcidin expression was unaffected by SNX and CL alone, while it had decreased 50% in SNX + CL (p < 0.05). Hepatic ferritin immunostaining was not different among groups. CONCLUSIONS: Our data indicate differences in hepcidin regulation in liver and heart and suggest a role for injury rather than iron as the driving force for cardiac hepcidin expression in renocardiac failure.
[Mh] Termos MeSH primário: Hepcidinas/metabolismo
Ferro/metabolismo
Fígado/metabolismo
Infarto do Miocárdio/metabolismo
Miocárdio/metabolismo
Insuficiência Renal Crônica/metabolismo
[Mh] Termos MeSH secundário: Animais
Proteína Morfogenética Óssea 6/metabolismo
Proteína alfa Estimuladora de Ligação a CCAAT/metabolismo
Proteínas de Transporte de Cátions/metabolismo
Fator de Crescimento do Tecido Conjuntivo/metabolismo
Citocinas/metabolismo
Regulação da Expressão Gênica
Heme Oxigenase (Desciclizante)/metabolismo
Masculino
Peptídeo Natriurético Encefálico/metabolismo
Ratos Endogâmicos Lew
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Bmp6 protein, rat); 0 (Bone Morphogenetic Protein 6); 0 (CCAAT-Enhancer-Binding Protein-alpha); 0 (Cation Transport Proteins); 0 (Ctgf protein, rat); 0 (Cytokines); 0 (Hepcidins); 0 (metal transporting protein 1); 114471-18-0 (Natriuretic Peptide, Brain); 139568-91-5 (Connective Tissue Growth Factor); E1UOL152H7 (Iron); EC 1.14.14.18 (Heme Oxygenase (Decyclizing)); EC 1.14.14.18 (Hmox1 protein, rat)
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180118
[Lr] Data última revisão:
180118
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161025
[St] Status:MEDLINE


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[PMID]:28771589
[Au] Autor:Soldano A; Klinke S; Otero LH; Rivera M; Catalano-Dupuy DL; Ceccarelli EA
[Ad] Endereço:Instituto de Biología Molecular y Celular de Rosario (IBR), CONICET, Facultad de Ciencias Bioquímicas y Farmacéuticas, Universidad Nacional de Rosario, Rosario, Argentina.
[Ti] Título:Structural and mutational analyses of the Leptospira interrogans virulence-related heme oxygenase provide insights into its catalytic mechanism.
[So] Source:PLoS One;12(8):e0182535, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Heme oxygenase from Leptospira interrogans is an important virulence factor. During catalysis, redox equivalents are provided to this enzyme by the plastidic-type ferredoxin-NADP+ reductase also found in L. interrogans. This process may have evolved to aid this bacterial pathogen to obtain heme-iron from their host and enable successful colonization. Herein we report the crystal structure of the heme oxygenase-heme complex at 1.73 Å resolution. The structure reveals several distinctive features related to its function. A hydrogen bonded network of structural water molecules that extends from the catalytic site to the protein surface was cleared observed. A depression on the surface appears to be the H+ network entrance from the aqueous environment to the catalytic site for O2 activation, a key step in the heme oxygenase reaction. We have performed a mutational analysis of the F157, located at the above-mentioned depression. The mutant enzymes were unable to carry out the complete degradation of heme to biliverdin since the reaction was arrested at the verdoheme stage. We also observed that the stability of the oxyferrous complex, the efficiency of heme hydroxylation and the subsequent conversion to verdoheme was adversely affected. These findings underscore a long-range communication between the outer fringes of the hydrogen-bonded network of structural waters and the heme active site during catalysis. Finally, by analyzing the crystal structures of ferredoxin-NADP+ reductase and heme oxygenase, we propose a model for the productive association of these proteins.
[Mh] Termos MeSH primário: Heme Oxigenase (Desciclizante)/química
Heme Oxigenase (Desciclizante)/genética
Leptospira interrogans/patogenicidade
Mutagênese Sítio-Dirigida/métodos
[Mh] Termos MeSH secundário: Proteínas de Bactérias/química
Proteínas de Bactérias/genética
Domínio Catalítico
Cristalografia por Raios X
Ativação Enzimática
Ligações de Hidrogênio
Leptospira interrogans/enzimologia
Leptospira interrogans/genética
Modelos Moleculares
Conformação Proteica
Estabilidade Proteica
Fatores de Virulência/química
Fatores de Virulência/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Bacterial Proteins); 0 (Virulence Factors); EC 1.14.14.18 (Heme Oxygenase (Decyclizing))
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170829
[Lr] Data última revisão:
170829
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170804
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0182535


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[PMID]:28704479
[Au] Autor:Yamaoka M; Shimizu H; Takahashi T; Omori E; Morimatsu H
[Ad] Endereço:Department of Anesthesiology and Resuscitology, Okayama University Medical School, Okayama, Japan.
[Ti] Título:Dynamic changes in Bach1 expression in the kidney of rhabdomyolysis-associated acute kidney injury.
[So] Source:PLoS One;12(7):e0180934, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Free heme, a pro-oxidant released from myoglobin, is thought to contribute to the pathogenesis of rhabdomyolysis-associated acute kidney injury (RM-AKI), because renal overexpression of heme oxygenase-1 (HO-1), the rate-limiting enzyme in heme catabolism, confers protection against RM-AKI. BTB and CNC homology 1 (Bach1) is a heme-responsive transcription factor that represses HO-1. Here, we examined the changes with time in the gene expression of Bach1, HO-1, and δ-aminolevulinate synthase (ALAS1, a heme biosynthetic enzyme) in the rat kidney using an RM-AKI model induced by the injection of 50% glycerol (10 mL/kg body weight) into bilateral limbs. We also examined the protein expression of Bach1 in the nucleus and cytosol, and HO-1 in the rat kidney. Glycerol treatment induced significant elevation of serum creatinine kinase and aspartate aminotransferase levels followed by the marked elevation of serum blood urea nitrogen and creatinine levels, which caused serious damage to renal tubules. Following glycerol treatment, HO-1 mRNA and protein levels were significantly up-regulated, while ALAS1 mRNA expression was down-regulated, suggesting an increase in the free renal heme concentration. The Bach1 mRNA level was drastically increased 3 h after glycerol treatment, and the increased level was maintained for 12 h. Nuclear Bach1 protein levels were significantly decreased 3 h after treatment. Conversely, cytosolic Bach1 protein levels abruptly increased after 6 h. In conclusion, we demonstrate the dynamic changes in Bach1 expression in a rat model of RM-AKI. Our findings suggest that the increase in Bach1 mRNA and cytosolic Bach1 protein expression may reflect de novo Bach1 protein synthesis to compensate for the depletion of nuclear Bach1 protein caused by the induction of HO-1 by free heme.
[Mh] Termos MeSH primário: Lesão Renal Aguda/metabolismo
Fatores de Transcrição de Zíper de Leucina Básica/genética
Fatores de Transcrição de Zíper de Leucina Básica/metabolismo
Proteínas Repressoras/genética
Proteínas Repressoras/metabolismo
Rabdomiólise/complicações
[Mh] Termos MeSH secundário: 5-Aminolevulinato Sintetase/genética
5-Aminolevulinato Sintetase/metabolismo
Lesão Renal Aguda/genética
Animais
Citosol/metabolismo
Modelos Animais de Doenças
Regulação da Expressão Gênica
Glicerol/efeitos adversos
Heme/metabolismo
Heme Oxigenase (Desciclizante)/genética
Heme Oxigenase (Desciclizante)/metabolismo
Seres Humanos
Masculino
Ratos
Rabdomiólise/induzido quimicamente
Rabdomiólise/genética
Rabdomiólise/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Bach 1 protein, rat); 0 (Basic-Leucine Zipper Transcription Factors); 0 (Repressor Proteins); 42VZT0U6YR (Heme); EC 1.14.14.18 (Heme Oxygenase (Decyclizing)); EC 1.14.14.18 (Hmox1 protein, rat); EC 2.3.1.37 (5-Aminolevulinate Synthetase); PDC6A3C0OX (Glycerol)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170922
[Lr] Data última revisão:
170922
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170714
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0180934


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[PMID]:28655775
[Au] Autor:Yanatori I; Richardson DR; Toyokuni S; Kishi F
[Ad] Endereço:From the Department of Molecular Genetics, Kawasaki Medical School, 577 Matsushima, Kurashiki, Okayama 701-0192, Japan.
[Ti] Título:The iron chaperone poly(rC)-binding protein 2 forms a metabolon with the heme oxygenase 1/cytochrome P450 reductase complex for heme catabolism and iron transfer.
[So] Source:J Biol Chem;292(32):13205-13229, 2017 Aug 11.
[Is] ISSN:1083-351X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Mammals incorporate a major proportion of absorbed iron as heme, which is catabolized by the heme oxygenase 1 (HO1)-NADPH-cytochrome P450 reductase (CPR) complex into biliverdin, carbon monoxide, and ferrous iron. Moreover, intestinal iron is incorporated as ferrous iron, which is transported via the iron importer, divalent metal transporter 1 (DMT1). Recently, we demonstrated that the iron chaperone poly(rC)-binding protein 2 (PCBP2) can directly receive ferrous iron from DMT1 or transfer iron to the iron exporter, ferroportin 1. To promote intracellular iron flux, an iron chaperone may be essential for receiving iron generated by heme catabolism, but this hypothesis is untested so far. Herein, we demonstrate that HO1 binds to PCBP2, but not to other PCBP family members, namely PCBP1, PCBP3, or PCBP4. Interestingly, HO1 formed a complex with either CPR or PCBP2, and it was demonstrated that PCBP2 competes with CPR for HO1 binding. Using PCBP2-deletion mutants, we demonstrated that the PCBP2 K homology 3 domain is important for the HO1/PCBP2 interaction. In heme-loaded cells, heme prompted HO1-CPR complex formation and decreased the HO1/PCBP2 interaction. Furthermore, reconstitution experiments with purified recombinant proteins indicated that HO1 could bind to PCBP2 in the presence of heme, whereas loading of PCBP2 with ferrous iron caused PCBP2 to lose its affinity for HO1. These results indicate that ferrous iron released from heme can be bound by PCBP2 and suggest a model for an integrated heme catabolism and iron transport metabolon.
[Mh] Termos MeSH primário: Heme Oxigenase-1/metabolismo
Heme/metabolismo
Ferro/metabolismo
NADPH-Ferri-Hemoproteína Redutase/metabolismo
Proteínas de Ligação a RNA/metabolismo
[Mh] Termos MeSH secundário: Substituição de Aminoácidos
Sítios de Ligação
Ligação Competitiva
Transporte Biológico
Linhagem Celular
Deleção de Genes
Heme Oxigenase (Desciclizante)/química
Heme Oxigenase (Desciclizante)/genética
Heme Oxigenase (Desciclizante)/metabolismo
Heme Oxigenase-1/antagonistas & inibidores
Heme Oxigenase-1/química
Heme Oxigenase-1/genética
Seres Humanos
Metaloporfirinas/metabolismo
Mutação
NADPH-Ferri-Hemoproteína Redutase/antagonistas & inibidores
NADPH-Ferri-Hemoproteína Redutase/química
NADPH-Ferri-Hemoproteína Redutase/genética
Domínios e Motivos de Interação entre Proteínas
Multimerização Proteica
Transporte Proteico
Interferência de RNA
Proteínas de Ligação a RNA/química
Proteínas de Ligação a RNA/genética
Proteínas Recombinantes de Fusão/química
Proteínas Recombinantes de Fusão/metabolismo
Homologia Estrutural de Proteína
Fatores de Transcrição/química
Fatores de Transcrição/genética
Fatores de Transcrição/metabolismo
[Pt] Tipo de publicação:COMPARATIVE STUDY; JOURNAL ARTICLE
[Nm] Nome de substância:
0 (DMRT1 protein); 0 (Metalloporphyrins); 0 (PCBP2 protein, human); 0 (RNA-Binding Proteins); 0 (Recombinant Fusion Proteins); 0 (Transcription Factors); 0KAE1U0G7Q (tin mesoporphyrin); 42VZT0U6YR (Heme); E1UOL152H7 (Iron); EC 1.14.14.18 (HMOX1 protein, human); EC 1.14.14.18 (Heme Oxygenase (Decyclizing)); EC 1.14.14.18 (Heme Oxygenase-1); EC 1.14.14.18 (heme oxygenase-2); EC 1.6.2.4 (NADPH-Ferrihemoprotein Reductase)
[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:170629
[St] Status:MEDLINE
[do] DOI:10.1074/jbc.M117.776021


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[PMID]:28654333
[Au] Autor:Hongo Y; Yasuda N; NagaI S
[Ti] Título:Identification of Genes for Synthesis of the Blue Pigment, Biliverdin IXα, in the Blue Coral Heliopora coerulea.
[So] Source:Biol Bull;232(2):71-81, 2017 Apr.
[Is] ISSN:1939-8697
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Heliopora coerulea is the only species in the subclass Octocorallia that has a crystalline aragonite skeleton. The skeleton has been reported to contain the blue pigment, biliverdin IXα, which is formed by heme oxygenase (HO) during heme decomposition. There is little information regarding gene expression in H. coerulea; therefore, the biosynthesis pathway for biliverdin IXα is poorly understood. To identify the genes related to heme synthesis and degradation, metatranscripts of H. coerulea and its symbiont Symbiodinium spp. were sequenced and separated from the host- and symbiont-derived sequences. From the metatranscriptome analyses, all genes for heme synthesis and three HOs were isolated from the host and symbiont. From our phylogenetic and amino acid analysis, we noted that one of the HO isoforms in the host coral was predicted to possess HO activity. However, biliverdin reductase, which reduces biliverdin to bilirubin, was not identified in the present study. Similarly, biliverdin reductase was not identified in the transcripts of the red coral Corallium rubrum, a species that also belongs to Octocorallia. However, genes related to heme synthesis and HO were found in C. rubrum. We speculate that Heliopora coerulea can produce biliverdin and accumulate it in the skeleton, while red corals and other Octocorallia species cannot. Further information from molecular studies of H. coerulea will provide insights into the synthesis of biliverdin IXα, the blue pigment in the hard crystalline aragonite skeleton, and will be fundamental to future ecological and physiological studies.
[Mh] Termos MeSH primário: Antozoários/genética
Biliverdina/genética
[Mh] Termos MeSH secundário: Animais
Antozoários/classificação
Heme/metabolismo
Heme Oxigenase (Desciclizante)/metabolismo
Filogenia
Transcriptoma
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
42VZT0U6YR (Heme); EC 1.14.14.18 (Heme Oxygenase (Decyclizing)); O9MIA842K9 (Biliverdine)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171025
[Lr] Data última revisão:
171025
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170628
[St] Status:MEDLINE
[do] DOI:10.1086/692661


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[PMID]:28635609
[Au] Autor:Allam MM; El-Gohary OA
[Ad] Endereço:Department of Physiology, Faculty of Medicine, Benha University, Benha, Egypt. monamaher8011@yahoo.com.
[Ti] Título:Gastroprotective effect of ghrelin against indomethacin-induced gastric injury in rats: possible role of heme oxygenase-1 pathway.
[So] Source:Gen Physiol Biophys;36(3):321-330, 2017 Jul.
[Is] ISSN:0231-5882
[Cp] País de publicação:Slovakia
[La] Idioma:eng
[Ab] Resumo:Ghrelin has been shown to ameliorate gastric injury by several mechanisms in experimental animal models. The present study aimed to investigate the effect of pretreatment with ghrelin on indomethacin-induced gastric injury in rats and the role of heme oxygenase-1(HO-1) pathway as a novel mechanism underlying the gastroprotective effect of ghrelin. In all groups studied, ulcer score (U.S), ulcer index (U.I) and preventive index (P.I) were evaluated and the gastric inflammatory biomarkers including levels of tumor necrosis factor-α (TNF-α), interleukin-1ß (IL-1ß) and myeloperoxidase (MPO) activity as well as prostaglandin E2 (PGE2), malondialdehyde (MDA), glutathione (GSH), superoxide dismutase (SOD), HO-1 and bilirubin as an indicator of heme oxygenase activity were measured. Indomethacin induced significant elevation in U.S and U.I as well as the inflammatory and the oxidative markers and reduced the PGE2 in addition to HO-1 level and activity. Pretreatment with ghrelin reversed these results. In order to elucidate the possible role of HO-1 in mediating the protective effects of ghrelin, tin protoporphyrin (SnPP) HO-1 blocker was administrated; it significantly attenuated the gastroprotective effect of ghrelin. In conclusion HO-1 activity significantly contributes toward ghrelin-mediated gastroprotection.
[Mh] Termos MeSH primário: Fármacos Gastrointestinais/administração & dosagem
Grelina/administração & dosagem
Heme Oxigenase (Desciclizante)/metabolismo
Pré-Medicação/métodos
Úlcera Gástrica/induzido quimicamente
Úlcera Gástrica/prevenção & controle
[Mh] Termos MeSH secundário: Animais
Anti-Inflamatórios não Esteroides/efeitos adversos
Relação Dose-Resposta a Droga
Masculino
Ratos
Ratos Wistar
Transdução de Sinais/efeitos dos fármacos
Úlcera Gástrica/metabolismo
Resultado do Tratamento
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Anti-Inflammatory Agents, Non-Steroidal); 0 (Gastrointestinal Agents); 0 (Ghrelin); EC 1.14.14.18 (Heme Oxygenase (Decyclizing))
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170912
[Lr] Data última revisão:
170912
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170622
[St] Status:MEDLINE
[do] DOI:10.4149/gpb_2016056


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[PMID]:28378932
[Au] Autor:Gomperts E; Belcher JD; Otterbein LE; Coates TD; Wood J; Skolnick BE; Levy H; Vercellotti GM
[Ad] Endereço:Hillhurst Biopharmaceuticals, Inc, 2029 Verdugo Blvd., #125, Montrose, CA, 91020, USA.
[Ti] Título:The role of carbon monoxide and heme oxygenase in the prevention of sickle cell disease vaso-occlusive crises.
[So] Source:Am J Hematol;92(6):569-582, 2017 Jun.
[Is] ISSN:1096-8652
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Sickle Cell Disease (SCD) is a painful, lifelong hemoglobinopathy inherited as a missense point mutation in the hemoglobin (Hb) beta-globin gene. This disease has significant impact on quality of life and mortality, thus a substantial medical need exists to reduce the vaso-occlusive crises which underlie the pathophysiology of the disease. The concept that a gaseous molecule may exert biological function has been well known for over one hundred years. Carbon monoxide (CO), although studied in SCD for over 50 years, has recently emerged as a powerful cytoprotective biological response modifier capable of regulating a host of physiologic and therapeutic processes that, at low concentrations, exerts key physiological functions in various models of tissue inflammation and injury. CO is physiologically generated by the metabolism of heme by the heme oxygenase enzymes and is measurable in blood. A substantial amount of preclinical and clinical data with CO have been generated, which provide compelling support for CO as a potential therapeutic in a number of pathological conditions. Data underlying the therapeutic mechanisms of CO, including in SCD, have been generated by a plethora of in vitro and preclinical studies including multiple SCD mouse models. These data show CO to have key signaling impacts on a host of metallo-enzymes as well as key modulating genes that in sum, result in significant anti-inflammatory, anti-oxidant and anti-apoptotic effects as well as vasodilation and anti-adhesion of cells to the endothelium resulting in preservation of vascular flow. CO may also have a role as an anti-polymerization HbS agent. In addition, considerable scientific data in the non-SCD literature provide evidence for a beneficial impact of CO on cerebrovascular complications, suggesting that in SCD, CO could potentially limit these highly problematic neurologic outcomes. Research is needed and hopefully forthcoming, to carefully elucidate the safety and benefits of this potential therapy across the age spectrum of patients impacted by the host of pathophysiological complications of this devastating disease.
[Mh] Termos MeSH primário: Anemia Falciforme/complicações
Anemia Falciforme/metabolismo
Monóxido de Carbono/metabolismo
Heme Oxigenase (Desciclizante)/metabolismo
Doenças Vasculares/etiologia
Doenças Vasculares/prevenção & controle
[Mh] Termos MeSH secundário: Anemia Falciforme/genética
Anemia Falciforme/terapia
Animais
Monóxido de Carbono/administração & dosagem
Monóxido de Carbono/efeitos adversos
Monóxido de Carbono/sangue
Ensaios Clínicos como Assunto
Modelos Animais de Doenças
Heme Oxigenase (Desciclizante)/sangue
Hemoglobinas/química
Hemoglobinas/genética
Hemoglobinas/metabolismo
Seres Humanos
Transdução de Sinais
Resultado do Tratamento
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Hemoglobins); 7U1EE4V452 (Carbon Monoxide); EC 1.14.14.18 (Heme Oxygenase (Decyclizing))
[Em] Mês de entrada:1707
[Cu] Atualização por classe:170724
[Lr] Data última revisão:
170724
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170406
[St] Status:MEDLINE
[do] DOI:10.1002/ajh.24750


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[PMID]:28323775
[Au] Autor:Hoeksma D; Rebolledo RA; Hottenrott M; Bodar YS; Wiersema-Buist JJ; Van Goor H; Leuvenink HG
[Ad] Endereço:1 Department of Surgery, University Medical Center Groningen, Groningen, The Netherlands. 2 Department of Digestive Surgery, Faculty of Medicine, Pontificia Universidad Católica de Chile, Santiago, Chile. 3 Department of Cardiothoracic Surgery, University Medical Center Groningen, Groningen, The Netherlands. 4 Department of Pathology, University Medical Center Groningen, Groningen, The Netherlands.
[Ti] Título:Inadequate Antioxidative Responses in Kidneys of Brain-Dead Rats.
[So] Source:Transplantation;101(4):746-753, 2017 Apr.
[Is] ISSN:1534-6080
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: Brain death (BD)-related lipid peroxidation, measured as serum malondialdehyde (MDA) levels, correlates with delayed graft function in renal transplant recipients. How BD affects lipid peroxidation is not known. The extent of BD-induced organ damage is influenced by the speed at which intracranial pressure increases. To determine possible underlying causes of lipid peroxidation, we investigated the renal redox balance by assessing oxidative and antioxidative processes in kidneys of brain-dead rats after fast and slow BD induction. METHODS: Brain death was induced in 64 ventilated male Fisher rats by inflating a 4.0F Fogarty catheter in the epidural space. Fast and slow inductions were achieved by an inflation speed of 0.45 and 0.015 mL/min, respectively, until BD confirmation. Healthy non-brain-dead rats served as reference values. Brain-dead rats were monitored for 0.5, 1, 2, or 4 hours, after which organs and blood were collected. RESULTS: Increased MDA levels became evident at 2 hours of slow BD induction at which increased superoxide levels, decreased glutathione peroxidase (GPx) activity, decreased glutathione levels, increased inducible nitric oxide synthase and heme-oxygenase 1 expression, and increased plasma creatinine levels were evident. At 4 hours after slow BD induction, superoxide, MDA, and plasma creatinine levels increased further, whereas GPx activity remained decreased. Increased MDA and plasma creatinine levels also became evident after 4 hours fast BD induction. CONCLUSION: Brain death leads to increased superoxide production, decreased GPx activity, decreased glutathione levels, increased inducible nitric oxide synthase and heme-oxygenase 1 expression, and increased MDA and plasma creatinine levels. These effects were more pronounced after slow BD induction. Modulation of these processes could lead to decreased incidence of delayed graft function.
[Mh] Termos MeSH primário: Antioxidantes/metabolismo
Morte Encefálica/metabolismo
Encéfalo/metabolismo
Peroxidação de Lipídeos
Estresse Oxidativo
[Mh] Termos MeSH secundário: Animais
Biomarcadores/sangue
Encéfalo/fisiopatologia
Morte Encefálica/sangue
Morte Encefálica/fisiopatologia
Catalase/metabolismo
Creatinina/sangue
Modelos Animais de Doenças
Glutationa/sangue
Glutationa Peroxidase/metabolismo
Glutationa Redutase/metabolismo
Heme Oxigenase (Desciclizante)/genética
Heme Oxigenase (Desciclizante)/metabolismo
Rim/enzimologia
Masculino
Malondialdeído/metabolismo
Óxido Nítrico Sintase Tipo II/genética
Óxido Nítrico Sintase Tipo II/metabolismo
Oxirredução
Ratos Endogâmicos F344
Superóxido Dismutase/metabolismo
Superóxidos/metabolismo
Fatores de Tempo
[Pt] Tipo de publicação:COMPARATIVE STUDY; JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antioxidants); 0 (Biomarkers); 11062-77-4 (Superoxides); 4Y8F71G49Q (Malondialdehyde); AYI8EX34EU (Creatinine); EC 1.11.1.6 (Catalase); EC 1.11.1.9 (Glutathione Peroxidase); EC 1.14.13.39 (Nitric Oxide Synthase Type II); EC 1.14.13.39 (Nos2 protein, rat); EC 1.14.14.18 (Heme Oxygenase (Decyclizing)); EC 1.14.14.18 (Hmox1 protein, rat); EC 1.15.1.1 (Superoxide Dismutase); EC 1.8.1.7 (Glutathione Reductase); GAN16C9B8O (Glutathione)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:170522
[Lr] Data última revisão:
170522
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170322
[St] Status:MEDLINE
[do] DOI:10.1097/TP.0000000000001417


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[PMID]:28290603
[Au] Autor:Park C; Ji HM; Kim SJ; Kil SH; Lee JN; Kwak S; Choe SK; Park R
[Ad] Endereço:Department of Microbiology and Center for Metabolic Function Regulation, Wonkwang University School of Medicine, Iksan, Jeonbuk 54538, Republic of Korea.
[Ti] Título:Fenofibrate exerts protective effects against gentamicin-induced toxicity in cochlear hair cells by activating antioxidant enzymes.
[So] Source:Int J Mol Med;39(4):960-968, 2017 Apr.
[Is] ISSN:1791-244X
[Cp] País de publicação:Greece
[La] Idioma:eng
[Ab] Resumo:Fenofibrate, an activator of peroxisome proliferator-activated receptors (PPARs), has been shown to protect the kidneys and brain cells from oxidative stress; however, its role in preventing hearing loss has not been reported to date, at least to the best of our knowledge. In this study, we demonstrated the protective effects of fenofibrate against gentamicin (GM)-induced ototoxicity. We found that the auditory brainstem response threshold which was increased by GM was significantly reduced by pre-treatment with fenofibrate in rats. In cochlear explants, the disruption of hair cell layers by GM was also markedly attenuated by pre-treatment with fenofibrate. In addition, fenofibrate almost completely abolished GM-induced reactive oxygen species generation, which seemed to be mediated at least in part by the restoration of the expression of PPAR­α­dependent antioxidant enzymes, including catalase and superoxide dismutase (SOD)-1. Of note, fenofibrate markedly increased the expression of heme oxygenase-1 (HO-1) which was also induced to a certain degree by GM alone. The induced expression of HO-1 by fenofibrate appeared to be essential for mediating the protective effects of fenofibrate, as the inhibition of HO-1 activity significantly diminished the protective effects of fenofibrate against the GM-mediated death of sensory hair cells in cochlea explant culture, as well as in zebrafish neuromasts. These results suggest that fenofibrate protects sensory hair cells from GM-induced toxicity by upregulating PPAR­α-dependent antioxidant enzymes, including HO-1. Our results provide insight into the preventive therapy for hearing loss caused by aminoglycoside antibiotics.
[Mh] Termos MeSH primário: Antioxidantes/metabolismo
Catalase/metabolismo
Fenofibrato/farmacologia
Gentamicinas/efeitos adversos
Células Ciliadas Auditivas/enzimologia
Heme Oxigenase (Desciclizante)/metabolismo
Superóxido Dismutase-1/metabolismo
Proteínas de Peixe-Zebra/metabolismo
Peixe-Zebra/metabolismo
[Mh] Termos MeSH secundário: Animais
Morte Celular
Ativação Enzimática/efeitos dos fármacos
Feminino
Gentamicinas/farmacologia
Células Ciliadas Auditivas/patologia
Masculino
PPAR alfa/metabolismo
Ratos
Ratos Sprague-Dawley
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antioxidants); 0 (Gentamicins); 0 (PPAR alpha); 0 (Zebrafish Proteins); EC 1.11.1.6 (Catalase); EC 1.14.14.18 (Heme Oxygenase (Decyclizing)); EC 1.14.14.18 (Hmox1 protein, rat); EC 1.15.1.1 (Sod1 protein, rat); EC 1.15.1.1 (Superoxide Dismutase-1); U202363UOS (Fenofibrate)
[Em] Mês de entrada:1704
[Cu] Atualização por classe:170428
[Lr] Data última revisão:
170428
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170315
[St] Status:MEDLINE
[do] DOI:10.3892/ijmm.2017.2916


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[PMID]:28254443
[Au] Autor:França EJ; Furlaneto-Maia L; Furlaneto MC
[Ad] Endereço:Department of Microbiology, State University of Londrina, Paraná, Brazil; State University of North of Paraná, Brazil.
[Ti] Título:Hemolytic capability and expression of a putative haem oxygenase-encoding gene by blood isolates of Candida tropicalis are influenced by iron deprivation and the presence of hemoglobin and erythrocytes.
[So] Source:Microb Pathog;105:235-239, 2017 Apr.
[Is] ISSN:1096-1208
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Although hemolytic activity is known to be a putative virulence factor contributing to candidal pathogenesis, its production by Candida tropicalis, a species closely related to Candida albicans, is poor understood. The present study was undertaken to evaluate the hemolytic activity and the expression level of a putative haem oxygenase encoding gene by blood isolates of C. tropicalis following growth in iron deprivation, and in the presence of hemoglobin and erythrocytes. The lowest values of hemolytic activity were observed in cell-free culture supernatants of isolates growing in iron-restricted medium (RPMI medium and RPMI medium supplemented with iron chelator bathophenanthrolindisulphonic acid). Hemolysis was increased in the presence of either hemoglobin or erythrocytes. Reverse transcriptase PCR analysis showed that the putative haem oxygenase encoding gene (CtHMX1), potentially related with iron uptake, was up-regulated (p < 0.001) following growth in iron deprivation and in the presence of hemoglobin; CtHMX1 was repressed in the presence of human erythrocytes (p < 0.001). Our data suggest that hemoglobin had positive effect in the production of hemolytic factor and gene expression related to iron uptake in C. tropicalis.
[Mh] Termos MeSH primário: Sangue/microbiologia
Candida tropicalis/enzimologia
Candida tropicalis/genética
Eritrócitos/metabolismo
Heme Oxigenase (Desciclizante)/genética
Heme Oxigenase (Desciclizante)/metabolismo
Hemoglobinas/metabolismo
Ferro/metabolismo
[Mh] Termos MeSH secundário: Candida tropicalis/crescimento & desenvolvimento
Candida tropicalis/ultraestrutura
Candidíase/sangue
Candidíase/microbiologia
Meios de Cultura
DNA Fúngico/isolamento & purificação
Proteínas Fúngicas/biossíntese
Proteínas Fúngicas/genética
Fungos/crescimento & desenvolvimento
Proteínas Hemolisinas
Hemólise
Seres Humanos
RNA Fúngico/isolamento & purificação
Regulação para Cima
Fatores de Virulência/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Culture Media); 0 (DNA, Fungal); 0 (Fungal Proteins); 0 (Hemoglobins); 0 (Hemolysin Proteins); 0 (RNA, Fungal); 0 (Virulence Factors); E1UOL152H7 (Iron); EC 1.14.14.18 (Heme Oxygenase (Decyclizing))
[Em] Mês de entrada:1705
[Cu] Atualização por classe:170505
[Lr] Data última revisão:
170505
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170304
[St] Status:MEDLINE



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