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  1 / 1826 MEDLINE  
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[PMID]:28668825
[Au] Autor:Nguyen KH; Nguyen AH; Dabir DV
[Ad] Endereço:Department of Biology, Loyola Marymount University, Los Angeles, CA, U.S.A.
[Ti] Título:Clinical Implications of Augmenter of Liver Regeneration in Cancer: A Systematic Review.
[So] Source:Anticancer Res;37(7):3379-3383, 2017 07.
[Is] ISSN:1791-7530
[Cp] País de publicação:Greece
[La] Idioma:eng
[Ab] Resumo:BACKGROUND/AIM: Hepatocellular carcinoma is a substantial healthcare burden with high prevalence and poor prognosis. As such, efforts are continually made to uncover molecules relevant in cancer biology, that are exploitable as targets for therapy. The mitochondrion is the powerhouse of the cell and exhibits altered functionality in the malignant state, including aberrant regulation of apoptosis and cellular respiration. Augmenter of liver regeneration (ALR) is a multifunctional mitochondrial protein that demonstrates anti-oxidative and anti-apoptotic properties and plays a key role in liver regeneration. MATERIALS AND METHODS: The present study systematically reviews the available literature on the role of ALR in cancer. RESULTS: Systematic search of PubMed resulted in 12 studies discussing ALR in multiple types of cancer. More specifically, ALR appears to be up-regulated in malignant cells and tissues. Furthermore, treatment of cells with exogenous ALR shows an anti-apoptotic effect while silencing or inhibiting ALR decreases cell and tumor survival. CONCLUSION: ALR clearly plays a role in cancer biology and demonstrates potential as a therapeutic target.
[Mh] Termos MeSH primário: Redutases do Citocromo/metabolismo
Regeneração Hepática/fisiologia
Proteínas Mitocondriais/metabolismo
Neoplasias/metabolismo
Neoplasias/patologia
[Mh] Termos MeSH secundário: Apoptose/fisiologia
Seres Humanos
Mitocôndrias/metabolismo
Mitocôndrias/patologia
Regulação para Cima/fisiologia
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Mitochondrial Proteins); EC 1.6.2.- (Cytochrome Reductases); EC 1.6.2.- (GFER protein, human)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170906
[Lr] Data última revisão:
170906
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170703
[St] Status:MEDLINE


  2 / 1826 MEDLINE  
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[PMID]:28506765
[Au] Autor:Dayoub R; Buerger L; Ibrahim S; Melter M; Weiss TS
[Ad] Endereço:University Children's Hospital Regensburg (KUNO), University Hospital Regensburg, Germany; Department of Biochemistry and Microbiology, Faculty of Pharmacy, Damascus University, Damascus, Syria. Electronic address: rania.dayoub@ukr.de.
[Ti] Título:Augmenter of liver regeneration (ALR) exhibits a dual signaling impact on hepatic acute-phase response.
[So] Source:Exp Mol Pathol;102(3):428-433, 2017 Jun.
[Is] ISSN:1096-0945
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:The acute-phase response (APR) is an inflammatory process triggered mainly by IL-6 in response to neoplasm, tissue injury, infection or inflammation. Signaling of IL-6 is transduced by activating STAT3 which rapidly results in production of acute-phase proteins (APPs) such as fibrinogen ß (FGB) and haptoglobin (HP). Augmenter of liver regeneration (ALR), a hepatotrophic factor supporting liver regeneration, was reported to be upregulated after liver damage. In this study we analyzed the role of ALR for IL-6 signaling and APR. Thus, we investigated the expression and release of APPs in human liver cells under conditions of increased exogenous or endogenous ALR. HepG2 cells and ALR-reexpressing HepG2 cells were treated with IL-6 in the presence or absence of exogenous ALR for different time points. The mRNA expression and release of both FGB and HP were measured by RT-PCR and ELISA. We found that exogenously applied ALR attenuated the IL-6-induced mRNA expression and protein secretion of both FGB and HP. In contrast, IL-6 stimulation in HepG2 cells which re-express ALR, revealed elevated APR shown by increased mRNA expression and secretion of FGB and HP. Furthermore, we found that ALR-mediated regulation of IL-6-induced APP production is accompanied by altered STAT3 activity. While exogenous ALR reduced the IL-6-induced phosphorylation of STAT3, endogenous ALR enhanced STAT3 activity in liver cells. In conclusion, ALR, dependent on its localization, changes APR at least in part, by modifying STAT3 activation. This study shows a dual signaling of ALR and suggests that ALR is pivotal for the regulation of APR, a crucial event in liver injury and regeneration.
[Mh] Termos MeSH primário: Reação de Fase Aguda/genética
Redutases do Citocromo/metabolismo
Hepatócitos/metabolismo
Fator de Transcrição STAT3/metabolismo
[Mh] Termos MeSH secundário: Reação de Fase Aguda/patologia
Redutases do Citocromo/genética
Fibrinogênio/genética
Fibrinogênio/metabolismo
Haptoglobinas/genética
Haptoglobinas/metabolismo
Células Hep G2
Seres Humanos
Interleucina-6/farmacologia
Fígado/metabolismo
Regeneração Hepática
Chaperonas Moleculares/genética
Chaperonas Moleculares/metabolismo
Fosforilação
Proteínas Inibidoras de STAT Ativados/genética
Proteínas Inibidoras de STAT Ativados/metabolismo
RNA Mensageiro/genética
RNA Mensageiro/metabolismo
Fator de Transcrição STAT3/genética
Transdução de Sinais
Proteína 3 Supressora da Sinalização de Citocinas/genética
Proteína 3 Supressora da Sinalização de Citocinas/metabolismo
Regulação para Cima
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Haptoglobins); 0 (Interleukin-6); 0 (Molecular Chaperones); 0 (PIAS3 protein, human); 0 (Protein Inhibitors of Activated STAT); 0 (RNA, Messenger); 0 (SOCS3 protein, human); 0 (STAT3 Transcription Factor); 0 (STAT3 protein, human); 0 (Suppressor of Cytokine Signaling 3 Protein); 9001-32-5 (Fibrinogen); EC 1.6.2.- (Cytochrome Reductases); EC 1.6.2.- (GFER protein, human)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170814
[Lr] Data última revisão:
170814
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170517
[St] Status:MEDLINE


  3 / 1826 MEDLINE  
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[PMID]:28431972
[Au] Autor:Villa RF; Ferrari F; Bagini L; Gorini A; Brunello N; Tascedda F
[Ad] Endereço:Laboratory of Pharmacology and Molecular Medicine of Central Nervous System, Department of Biology and Biotechnology, University of Pavia, Via Ferrata 9, 27100 Pavia, Italy. Electronic address: robertofederico.villa@unipv.it.
[Ti] Título:Mitochondrial energy metabolism of rat hippocampus after treatment with the antidepressants desipramine and fluoxetine.
[So] Source:Neuropharmacology;121:30-38, 2017 Jul 15.
[Is] ISSN:1873-7064
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Alterations in mitochondrial functions have been hypothesized to participate in the pathogenesis of depression, because brain bioenergetic abnormalities have been detected in depressed patients by neuroimaging in vivo studies. However, this hypothesis is not clearly demonstrated in experimental studies: some suggest that antidepressants are inhibitors of mitochondrial metabolism, while others observe the opposite. In this study, the effects of 21-day treatment with desipramine (15 mg/kg) and fluoxetine (10 mg/kg) were examined on the energy metabolism of rat hippocampus, evaluating the catalytic activity of regulatory enzymes of mitochondrial energy-yielding metabolic pathways. Because of the micro-heterogeneity of brain mitochondria, we have distinguished between (a) non-synaptic mitochondria (FM) of neuronal perikaryon (post-synaptic compartment) and (b) intra-synaptic light (LM) and heavy (HM) mitochondria (pre-synaptic compartment). Desipramine and fluoxetine changed the catalytic activity of specific enzymes in the different types of mitochondria: (a) in FM, both drugs enhanced cytochrome oxidase and glutamate dehydrogenase, (b) in LM, the overall bioenergetics was unaffected and (c) in HM only desipramine increased malate dehydrogenase and decreased the activities of Electron Transport Chain Complexes. These results integrate the pharmacodynamic features of desipramine and fluoxetine at subcellular level, overcoming the previous conflicting data about the effects of antidepressants on brain energy metabolism, mainly referred to whole brain homogenates or to bulk of cerebral mitochondria. With the differentiation in non-synaptic and intra-synaptic mitochondria, this study demonstrates that desipramine and fluoxetine lead to adjustments in the mitochondrial bioenergetics respect to the energy requirements of pre- and post-synaptic compartments.
[Mh] Termos MeSH primário: Antidepressivos/farmacologia
Desipramina/farmacologia
Metabolismo Energético/efeitos dos fármacos
Fluoxetina/farmacologia
Hipocampo
Mitocôndrias/efeitos dos fármacos
[Mh] Termos MeSH secundário: Análise de Variância
Animais
Redutases do Citocromo/metabolismo
Complexo IV da Cadeia de Transporte de Elétrons/metabolismo
Glutamato Desidrogenase/metabolismo
Hipocampo/efeitos dos fármacos
Hipocampo/enzimologia
Hipocampo/ultraestrutura
Masculino
Ratos
Ratos Sprague-Dawley
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antidepressive Agents); 01K63SUP8D (Fluoxetine); EC 1.4.1.2 (Glutamate Dehydrogenase); EC 1.6.2.- (Cytochrome Reductases); EC 1.6.2.- (NADH-cytochrome o reductase); EC 1.9.3.1 (Electron Transport Complex IV); TG537D343B (Desipramine)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170906
[Lr] Data última revisão:
170906
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170423
[St] Status:MEDLINE


  4 / 1826 MEDLINE  
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[PMID]:27994073
[Au] Autor:Freire MO; Dalli J; Serhan CN; Van Dyke TE
[Ad] Endereço:Department of Applied Oral Sciences, Center for Periodontology, The Forsyth Institute, Cambridge, MA 02142.
[Ti] Título:Neutrophil Resolvin E1 Receptor Expression and Function in Type 2 Diabetes.
[So] Source:J Immunol;198(2):718-728, 2017 Jan 15.
[Is] ISSN:1550-6606
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Unresolved inflammation is key in linking metabolic dysregulation and the immune system in type 2 diabetes. Successful regulation of acute inflammation requires biosynthesis of specialized proresolving lipid mediators, such as E-series resolvin (RvE) 1, and activation of cognate G protein-coupled receptors. RvE1 binds to leukotriene B4 (BLT-1) on neutrophils and to ERV-1/ChemR23 on monocyte/macrophages. We show novel actions of RvE1 and expression patterns of neutrophil receptors in type 2 diabetes. Neutrophils from healthy subjects express functional BLT-1, low levels of minimally functional ERV-1, and inversed coexpression when compared to neutrophils from type 2 diabetes subjects. Stimulation with TNF-α or LPS increased the expression of ERV-1 by healthy and diabetic neutrophils. RvE1 counteracted LPS and TNF-α induction of ERV-1 overexpression and endogenous diabetic overexpression, activating phagocytosis and resolution signals. Functional ERV-1 was determined by phosphorylation of the signaling protein ribosomal S6. Receptor-antagonism experiments revealed that the increase in phosphorylation of ribosomal S6 was mediated by BLT-1 in healthy subject neutrophils and by ERV-1 in diabetes. Metabololipidomics reveal a proinflammatory profile in diabetic serum. Cell phagocytosis is impaired in type 2 diabetes and requires RvE1 for activation. The dose of RvE1 required to activate resolution signals in type 2 diabetic neutrophils was significantly higher than in healthy controls. RvE1 rescues the dysregulation seen on neutrophil receptor profile and, following a therapeutic dosage, activates phagocytosis and resolution signals in type 2 diabetes. These findings reveal the importance of resolution receptors in health, disease, and dysregulation of inflammation in type 2 diabetes.
[Mh] Termos MeSH primário: Redutases do Citocromo/metabolismo
Diabetes Mellitus Tipo 2/metabolismo
Ácido Eicosapentaenoico/análogos & derivados
Neutrófilos/metabolismo
Receptores do Leucotrieno B4/metabolismo
[Mh] Termos MeSH secundário: Adulto
Células Cultivadas
Cromatografia Líquida
Redutases do Citocromo/imunologia
Diabetes Mellitus Tipo 2/imunologia
Ácido Eicosapentaenoico/imunologia
Ácido Eicosapentaenoico/metabolismo
Feminino
Seres Humanos
Inflamação/imunologia
Inflamação/metabolismo
Masculino
Meia-Idade
Neutrófilos/imunologia
Fagocitose/imunologia
Reação em Cadeia da Polimerase
Receptores do Leucotrieno B4/imunologia
Espectrometria de Massas em Tandem
Transcriptoma
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (5S,12R,18R-trihydroxy-6Z,8E,10E,14Z,16E-eicosapentaenoic acid); 0 (LTB4R protein, human); 0 (Receptors, Leukotriene B4); AAN7QOV9EA (Eicosapentaenoic Acid); EC 1.6.2.- (Cytochrome Reductases); EC 1.6.2.- (GFER protein, human)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170808
[Lr] Data última revisão:
170808
[Sb] Subgrupo de revista:AIM; IM
[Da] Data de entrada para processamento:161221
[St] Status:MEDLINE
[do] DOI:10.4049/jimmunol.1601543


  5 / 1826 MEDLINE  
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[PMID]:27390784
[Au] Autor:Wójcik K; Piekarska A; Szymanska B; Jablonowska E
[Ad] Endereço:Department of Infectious Diseases and Hepatology, Medical University of Lodz, Lódz, Poland.
[Ti] Título:Hepatic expression of miR-122 and antioxidant genes in patients with chronic hepatitis B.
[So] Source:Acta Biochim Pol;63(3):527-31, 2016.
[Is] ISSN:1734-154X
[Cp] País de publicação:Poland
[La] Idioma:eng
[Ab] Resumo:INTRODUCTION: The pathogenesis of chronic hepatitis B depends on both, the immune response and oxidative stress. AIM OF THE STUDY: To assess the hepatic expression of miR-122 and the antioxidant genes: HMOX-1, NQO1 and GFER1, in liver biopsy specimens obtained from patients with chronic hepatitis B, with regard to selected clinical and histological parameters, using RT-PCR. RESULTS: The study group comprised 34 HBV-infected patients. Statistically significant associations were found between lower hepatic expression of HMOX-1 and greater severity of liver inflammation (p=0.04). However, significantly higher expression of NQO1 was observed in patients with advanced liver fibrosis (p=0.035). Hepatic expression of miR-122 in HBV patients was not associated with viral load or liver injury. CONCLUSION: The hepatic expression of HMOX-1and NQO1 may be associated with liver injuries in chronic hepatitis B. However, hepatic expression of miR-122 does not seem to correspond to progression of the liver disease.
[Mh] Termos MeSH primário: Hepatite B Crônica/metabolismo
Fígado/metabolismo
MicroRNAs/metabolismo
[Mh] Termos MeSH secundário: Adulto
Redutases do Citocromo/metabolismo
Feminino
Expressão Gênica
Heme Oxigenase-1/metabolismo
Hepatite B Crônica/genética
Hepatite B Crônica/virologia
Seres Humanos
Fígado/patologia
Masculino
MicroRNAs/genética
Meia-Idade
NAD(P)H Desidrogenase (Quinona)/metabolismo
Carga Viral
Adulto Jovem
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (MIRN122 microRNA, human); 0 (MicroRNAs); EC 1.14.14.18 (HMOX1 protein, human); EC 1.14.14.18 (Heme Oxygenase-1); EC 1.6.2.- (Cytochrome Reductases); EC 1.6.2.- (GFER protein, human); EC 1.6.5.2 (NAD(P)H Dehydrogenase (Quinone)); EC 1.6.5.2 (NQO1 protein, human)
[Em] Mês de entrada:1701
[Cu] Atualização por classe:170124
[Lr] Data última revisão:
170124
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160709
[St] Status:MEDLINE
[do] DOI:10.18388/abp.2016_1216


  6 / 1826 MEDLINE  
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[PMID]:27289096
[Au] Autor:Saber MM; Adeyemi Babarinde I; Hettiarachchi N; Saitou N
[Ad] Endereço:Department of Biological Sciences, Graduate School of Science, University of Tokyo Division of Population Genetics, National Institute of Genetics, Mishima, Japan.
[Ti] Título:Emergence and Evolution of Hominidae-Specific Coding and Noncoding Genomic Sequences.
[So] Source:Genome Biol Evol;8(7):2076-92, 2016 Jul 12.
[Is] ISSN:1759-6653
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Family Hominidae, which includes humans and great apes, is recognized for unique complex social behavior and intellectual abilities. Despite the increasing genome data, however, the genomic origin of its phenotypic uniqueness has remained elusive. Clade-specific genes and highly conserved noncoding sequences (HCNSs) are among the high-potential evolutionary candidates involved in driving clade-specific characters and phenotypes. On this premise, we analyzed whole genome sequences along with gene orthology data retrieved from major DNA databases to find Hominidae-specific (HS) genes and HCNSs. We discovered that Down syndrome critical region 4 (DSCR4) is the only experimentally verified gene uniquely present in Hominidae. DSCR4 has no structural homology to any known protein and was inferred to have emerged in several steps through LTR/ERV1, LTR/ERVL retrotransposition, and transversion. Using the genomic distance as neutral evolution threshold, we identified 1,658 HS HCNSs. Polymorphism coverage and derived allele frequency analysis of HS HCNSs showed that these HCNSs are under purifying selection, indicating that they may harbor important functions. They are overrepresented in promoters/untranslated regions, in close proximity of genes involved in sensory perception of sound and developmental process, and also showed a significantly lower nucleosome occupancy probability. Interestingly, many ancestral sequences of the HS HCNSs showed very high evolutionary rates. This suggests that new functions emerged through some kind of positive selection, and then purifying selection started to operate to keep these functions.
[Mh] Termos MeSH primário: Evolução Molecular
Hominidae/genética
Fases de Leitura Aberta
Sequências Reguladoras de Ácido Nucleico
[Mh] Termos MeSH secundário: Animais
Sequência Conservada
Redutases do Citocromo/genética
Genoma Humano
Seres Humanos
Polimorfismo Genético
Proteínas da Gravidez/genética
Seleção Genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (DSCR4 protein, human); 0 (Pregnancy Proteins); EC 1.6.2.- (Cytochrome Reductases); EC 1.6.2.- (GFER protein, human)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170926
[Lr] Data última revisão:
170926
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160612
[St] Status:MEDLINE
[do] DOI:10.1093/gbe/evw132


  7 / 1826 MEDLINE  
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[PMID]:26018198
[Au] Autor:Calderwood L; Holm IA; Teot LA; Anselm I
[Ad] Endereço:Department of Obstetrics and Gynecology, Boston University School of Medicine, Boston, MA, USA.
[Ti] Título:Adrenal Insufficiency in Mitochondrial Disease: A Rare Case of GFER-Related Mitochondrial Encephalomyopathy and Review of the Literature.
[So] Source:J Child Neurol;31(2):190-4, 2016 Feb.
[Is] ISSN:1708-8283
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:GFER-related mitochondrial encephalomyopathy has been previously described only in 3 siblings of a consanguineous Moroccan family. Their phenotype included congenital cataracts, hypotonia, developmental delay, and sensorineural hearing loss. Multiple mitochondrial respiratory chain complex deficiencies were identified on muscle biopsy. We describe a now-19-year-old woman with adrenal insufficiency, lactic acidosis, congenital cataracts, and respiratory insufficiency secondary to mitochondrial disorder, who was reported by North et al (1996) as a toddler. Compound heterozygous GFER mutations c.373C>T (Q125X) and c.581G>A (R194 H) were recently discovered in this patient. The purpose of this report is (1) to expand the phenotype this ultra-rare disorder and (2) to provide a review of the literature describing the unique finding of adrenal insufficiency in patients with molecularly confirmed disorders of mitochondrial metabolism.
[Mh] Termos MeSH primário: Acidose Láctica/genética
Insuficiência Adrenal/genética
Catarata/genética
Redutases do Citocromo/genética
Doenças Mitocondriais/genética
[Mh] Termos MeSH secundário: Acidose Láctica/patologia
Acidose Láctica/fisiopatologia
Insuficiência Adrenal/patologia
Insuficiência Adrenal/fisiopatologia
Catarata/patologia
Catarata/fisiopatologia
Consanguinidade
Família
Feminino
Seres Humanos
Mitocôndrias/patologia
Doenças Mitocondriais/patologia
Doenças Mitocondriais/fisiopatologia
Marrocos
Fenótipo
Adulto Jovem
[Pt] Tipo de publicação:CASE REPORTS; JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
EC 1.6.2.- (Cytochrome Reductases); EC 1.6.2.- (GFER protein, human)
[Em] Mês de entrada:1610
[Cu] Atualização por classe:161230
[Lr] Data última revisão:
161230
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150529
[St] Status:MEDLINE
[do] DOI:10.1177/0883073815587327


  8 / 1826 MEDLINE  
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[PMID]:26271971
[Au] Autor:Xia N; Yan R; Liu Q; Sun H; Guo H; Zhang L
[Ad] Endereço:Department of Nephrology, Second Affiliated Hospital, Chongqing Medical University, Chongqing 400010, China.
[Ti] Título:[Over-expression of augmenter of liver regeneration promotes proliferation and suppresses hydrogen peroxide-induced apoptosis in LO2 cells].
[So] Source:Xi Bao Yu Fen Zi Mian Yi Xue Za Zhi;31(8):1017-21, 2015 Aug.
[Is] ISSN:1007-8738
[Cp] País de publicação:China
[La] Idioma:chi
[Ab] Resumo:OBJECTIVE: To investigate the effects of over-expression of 23 kDa augmenter of liver regeneration (ALR) on cell proliferation and apoptosis in the normal human hepatic cell line LO2. METHODS: The recombinant plasmid expressing 23 kDa ALR (pcDNA6/23 kDa ALR) was constructed and transfected into LO2 cells with MegaTran 1.0 transfection reagent. The expressions of ALR mRNA and protein in LO2 cells were detected by real-time quantitative PCR and Western blotting, respectively; MTS assay was used to detect the cell proliferation of LO2 cells; cell cycle and apoptosis of LO2 cells were measured by flow cytometry. RESULTS: The recombinant expression plasmid pcDNA6/23 kDa ALR was constructed successfully, and the expression of the target protein 23 kDa ALR increased significantly in the transfected cells. Compared with pcDNA6-myc/HisA group, the transient transfection of pcDNA6/23 kDa ALR into LO2 cells promoted cell proliferation and inhibited cell apoptosis induced by H2O2, however, no significant differences were detected in G0 phase and S phase. CONCLUSION: The over-expression of 23 kDa ALR in LO2 cells promoted the cell proliferation and enhanced cell resistance to H2O2.
[Mh] Termos MeSH primário: Apoptose/efeitos dos fármacos
Proliferação Celular
Redutases do Citocromo/metabolismo
Peróxido de Hidrogênio/farmacologia
[Mh] Termos MeSH secundário: Apoptose/genética
Western Blotting
Ciclo Celular/efeitos dos fármacos
Ciclo Celular/genética
Linhagem Celular
Redutases do Citocromo/genética
Citometria de Fluxo
Expressão Gênica
Células Hep G2
Seres Humanos
Fígado/citologia
Fígado/efeitos dos fármacos
Fígado/metabolismo
Oxidantes/farmacologia
Reação em Cadeia da Polimerase Via Transcriptase Reversa
[Pt] Tipo de publicação:ENGLISH ABSTRACT; JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Oxidants); BBX060AN9V (Hydrogen Peroxide); EC 1.6.2.- (Cytochrome Reductases); EC 1.6.2.- (GFER protein, human)
[Em] Mês de entrada:1512
[Cu] Atualização por classe:150814
[Lr] Data última revisão:
150814
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150815
[St] Status:MEDLINE


  9 / 1826 MEDLINE  
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[PMID]:26014136
[Au] Autor:Hudson DA; Thorpe C
[Ad] Endereço:Department of Chemistry and Biochemistry, University of Delaware, Newark, DE 19716, United States.
[Ti] Título:Mia40 is a facile oxidant of unfolded reduced proteins but shows minimal isomerase activity.
[So] Source:Arch Biochem Biophys;579:1-7, 2015 Aug 01.
[Is] ISSN:1096-0384
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Mia40 participates in oxidative protein folding within the mitochondrial intermembrane space (IMS) by mediating the transfer of reducing equivalents from client proteins to FAD-linked oxidoreductases of the Erv1 family (lfALR in mammals). Here we investigate the specificity of the human Mia40/lfALR system towards non-cognate unfolded protein substrates to assess whether the efficient introduction of disulfides requires a particular amino acid sequence context or the presence of an IMS targeting signal. Reduced pancreatic ribonuclease A (rRNase), avian lysozyme, and riboflavin binding protein are all competent substrates of the Mia40/lfALR system, although they lack those sequence features previously thought to direct disulfide bond formation in cognate IMS substrates. The oxidation of rRNase by Mia40 does not limit overall turnover of unfolded substrate by the Mia40/lfALR system. Mia40 is an ineffective protein disulfide isomerase when its ability to restore enzymatic activity from scrambled RNase is compared to that of protein disulfide isomerase. Mia40's ability to bind amphipathic peptides is evident by avid binding to the isolated B-chain during the insulin reductase assay. In aggregate these data suggest that the Mia40/lfALR system has a broad sequence specificity and that potential substrates may be protected from adventitious oxidation by kinetic sequestration within the mitochondrial IMS.
[Mh] Termos MeSH primário: Redutases do Citocromo/química
Redutases do Citocromo/ultraestrutura
Isomerases/química
Isomerases/ultraestrutura
Proteínas de Transporte da Membrana Mitocondrial/química
Proteínas de Transporte da Membrana Mitocondrial/ultraestrutura
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Sítios de Ligação
Simulação por Computador
Ativação Enzimática
Seres Humanos
Modelos Químicos
Modelos Moleculares
Dados de Sequência Molecular
Oxidantes/química
Oxirredução
Ligação Proteica
Conformação Proteica
Dobramento de Proteína
Relação Estrutura-Atividade
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL
[Nm] Nome de substância:
0 (MIA40 protein, human); 0 (Mitochondrial Membrane Transport Proteins); 0 (Oxidants); EC 1.6.2.- (Cytochrome Reductases); EC 1.6.2.- (GFER protein, human); EC 5.- (Isomerases)
[Em] Mês de entrada:1509
[Cu] Atualização por classe:170220
[Lr] Data última revisão:
170220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150528
[St] Status:MEDLINE


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[PMID]:25989539
[Au] Autor:Harrington M
[Ti] Título:Genetic predisposition to liver cirrhosis.
[So] Source:Lab Anim (NY);44(6):191, 2015 Jun.
[Is] ISSN:1548-4475
[Cp] País de publicação:United States
[La] Idioma:eng
[Mh] Termos MeSH primário: Redutases do Citocromo/genética
Cirrose Hepática Alcoólica/genética
Oxirredutases atuantes sobre Doadores de Grupo Enxofre/genética
[Mh] Termos MeSH secundário: Animais
Modelos Animais de Doenças
Predisposição Genética para Doença
Seres Humanos
Camundongos
Polimorfismo de Nucleotídeo Único
[Pt] Tipo de publicação:NEWS
[Nm] Nome de substância:
EC 1.6.2.- (Cytochrome Reductases); EC 1.6.2.- (GFER protein, human); EC 1.8.- (Oxidoreductases Acting on Sulfur Group Donors); EC 1.8.3.- (GFER protein, mouse)
[Em] Mês de entrada:1611
[Cu] Atualização por classe:161230
[Lr] Data última revisão:
161230
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150520
[St] Status:MEDLINE
[do] DOI:10.1038/laban.793



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