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[PMID]:29217198
[Au] Autor:Maalej M; Tej A; Bouguila J; Tilouche S; Majdoub S; Khabou B; Tabbebi M; Felhi R; Ammar M; Mkaouar-Rebai E; Keskes L; Boughamoura L; Fakhfakh F
[Ad] Endereço:Laboratory of Molecular and Functional Genetics, Faculty of Science of Sfax, University of Sfax, Tunisia; Laboratory of Human Molecular Genetics, Faculty of Medicine of Sfax, University of Sfax, Tunisia. Electronic address: marwamaalej7@gmail.com.
[Ti] Título:Clinical, Molecular, and Computational Analysis in two cases with mitochondrial encephalomyopathy associated with SUCLG1 mutation in a consanguineous family.
[So] Source:Biochem Biophys Res Commun;495(2):1730-1737, 2018 01 08.
[Is] ISSN:1090-2104
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Deficiency of the mitochondrial enzyme succinyl COA ligase (SUCL) is associated with encephalomyopathic mtDNA depletion syndrome and methylmalonic aciduria. This disorder is caused by mutations in both SUCL subunits genes: SUCLG1 (α subnit) and SUCLA2 (ß subnit). We report here, two Tunisian patients belonging to a consanguineous family with mitochondrial encephalomyopathy, hearing loss, lactic acidosis, hypotonia, psychomotor retardation and methylmalonic aciduria. Mutational analysis of SUCLG1 gene showed, for the first time, the presence of c.41T > C in the exon 1 at homozygous state. In-silico analysis revealed that this mutation substitutes a conserved methionine residue to a threonine at position 14 (p.M14T) located at the SUCLG1 protein mitochondrial targeting sequence. Moreover, these analysis predicted that this mutation alter stability structure and mitochondrial translocation of the protein. In Addition, a decrease in mtDNA copy number was revealed by real time PCR in the peripheral blood leukocytes in the two patients compared with controls.
[Mh] Termos MeSH primário: Encefalomiopatias Mitocondriais/enzimologia
Encefalomiopatias Mitocondriais/genética
Mutação de Sentido Incorreto
Succinato-CoA Ligases/deficiência
Succinato-CoA Ligases/genética
[Mh] Termos MeSH secundário: Acidose Láctica/genética
Erros Inatos do Metabolismo dos Aminoácidos/genética
Substituição de Aminoácidos
Pré-Escolar
Consanguinidade
DNA Mitocondrial/genética
Estabilidade Enzimática/genética
Feminino
Dosagem de Genes
Perda Auditiva/genética
Homozigoto
Seres Humanos
Lactente
Masculino
Hipotonia Muscular/genética
Succinato-CoA Ligases/química
[Pt] Tipo de publicação:CASE REPORTS; JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (DNA, Mitochondrial); EC 6.2.1.- (SUCLG1 protein, human); EC 6.2.1.- (Succinate-CoA Ligases)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180212
[Lr] Data última revisão:
180212
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171209
[St] Status:MEDLINE


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[PMID]:28749033
[Au] Autor:Couser NL; Marchuk DS; Smith LD; Arreola A; Kaiser-Rogers KA; Muenzer J; Pandya A; Gucsavas-Calikoglu M; Powell CM
[Ad] Endereço:Department of Pediatrics, Division of Genetics and Metabolism, School of Medicine, University of North Carolina at Chapel Hill, Chapel Hill, North Carolina.
[Ti] Título:Co-occurring Down syndrome and SUCLA2-related mitochondrial depletion syndrome.
[So] Source:Am J Med Genet A;173(10):2720-2724, 2017 Oct.
[Is] ISSN:1552-4833
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Mitochondrial DNA depletion syndrome 5 (MIM 612073) is a rare autosomal recessive disorder caused by homozygous or compound heterozygous pathogenic variants in the beta subunit of the succinate-CoA ligase gene located within the 13q14 band. We describe two siblings of Hispanic descent with SUCLA2-related mitochondrial depletion syndrome (encephalomyopathic form with methylmalonic aciduria); the older sibling is additionally affected with trisomy 21. SUCLA2 sequencing identified homozygous p.Arg284Cys pathogenic variants in both patients. This mutation has previously been identified in four individuals of Italian and Caucasian descent. The older sibling with concomitant disease has a more severe phenotype than what is typically described in patients with either SUCLA2-related mitochondrial depletion syndrome or Down syndrome alone. The younger sibling, who has a normal female chromosome complement, is significantly less affected compared to her brother. While the clinical and molecular findings have been reported in about 50 patients affected with a deficiency of succinate-CoA ligase caused by pathogenic variants in SUCLA2, this report describes the first known individual affected with both a mitochondrial depletion syndrome and trisomy 21.
[Mh] Termos MeSH primário: Síndrome de Down/genética
Homozigoto
Doenças Mitocondriais/genética
Mutação
Succinato-CoA Ligases/genética
[Mh] Termos MeSH secundário: Adulto
Criança
Pré-Escolar
Síndrome de Down/complicações
Síndrome de Down/diagnóstico
Feminino
Seres Humanos
Masculino
Doenças Mitocondriais/complicações
Doenças Mitocondriais/diagnóstico
Fenótipo
Prognóstico
Síndrome
Adulto Jovem
[Pt] Tipo de publicação:CASE REPORTS; JOURNAL ARTICLE
[Nm] Nome de substância:
EC 6.2.1.- (Succinate-CoA Ligases); EC 6.2.1.5 (SUCLA2 protein, human)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180207
[Lr] Data última revisão:
180207
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170728
[St] Status:MEDLINE
[do] DOI:10.1002/ajmg.a.38351


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[PMID]:28559280
[Au] Autor:Chen Y; Li TL; Lin X; Li X; Li XD; Guo Z
[Ad] Endereço:From the Department of Chemistry, Hong Kong University of Science and Technology, Clear Water Bay, Kowloon, Hong Kong and.
[Ti] Título:Crystal structure of the thioesterification conformation of -succinylbenzoyl-CoA synthetase reveals a distinct substrate-binding mode.
[So] Source:J Biol Chem;292(29):12296-12310, 2017 Jul 21.
[Is] ISSN:1083-351X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:-Succinylbenzoyl-CoA (OSB-CoA) synthetase (MenE) is an essential enzyme in bacterial vitamin K biosynthesis and an important target in the development of new antibiotics. It is a member of the adenylating enzymes (ANL) family, which reconfigure their active site in two different active conformations, one for the adenylation half-reaction and the other for a thioesterification half-reaction, in a domain-alternation catalytic mechanism. Although several aspects of the adenylating mechanism in MenE have recently been uncovered, its thioesterification conformation remains elusive. Here, using a catalytically competent mutant protein complexed with an OSB-CoA analogue, we determined MenE high-resolution structures to 1.76 and 1.90 Å resolution in a thioester-forming conformation. By comparison with the adenylation conformation, we found that MenE's C-domain rotates around the Ser-384 hinge by 139.5° during domain-alternation catalysis. The structures also revealed a thioesterification active site specifically conserved among MenE orthologues and a substrate-binding mode distinct from those of many other acyl/aryl-CoA synthetases. Of note, using site-directed mutagenesis, we identified several residues that specifically contribute to the thioesterification half-reaction without affecting the adenylation half-reaction. Moreover, we observed a substantial movement of the activated succinyl group in the thioesterification half-reaction. These findings provide new insights into the domain-alternation catalysis of a bacterial enzyme essential for vitamin K biosynthesis and of its adenylating homologues in the ANL enzyme family.
[Mh] Termos MeSH primário: Acil Coenzima A/metabolismo
Monofosfato de Adenosina/metabolismo
Bacillus subtilis/enzimologia
Proteínas de Bactérias/metabolismo
Modelos Moleculares
Processamento de Proteína Pós-Traducional
Succinato-CoA Ligases/metabolismo
[Mh] Termos MeSH secundário: Acil Coenzima A/química
Monofosfato de Adenosina/química
Sequência de Aminoácidos
Substituição de Aminoácidos
Proteínas de Bactérias/química
Domínio Catalítico
Sequência Conservada
Cristalografia por Raios X
Dimerização
Esterificação
Ligantes
Mutagênese Sítio-Dirigida
Mutação Puntual
Conformação Proteica
Dobramento de Proteína
Proteínas Recombinantes/química
Proteínas Recombinantes/metabolismo
Alinhamento de Sequência
Homologia Estrutural de Proteína
Succinato-CoA Ligases/química
Succinato-CoA Ligases/genética
[Pt] Tipo de publicação:COMPARATIVE STUDY; JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Acyl Coenzyme A); 0 (Bacterial Proteins); 0 (Ligands); 0 (Recombinant Proteins); 415SHH325A (Adenosine Monophosphate); 72471-59-1 (2-succinylbenzoyl-coenzyme A); EC 6.2.1.- (Succinate-CoA Ligases); EC 6.2.1.26 (O-succinylbenzoate - CoA ligase)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170808
[Lr] Data última revisão:
170808
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170601
[St] Status:MEDLINE
[do] DOI:10.1074/jbc.M117.790410


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[PMID]:28400269
[Au] Autor:Zhou F; Xu X; Wu J; Wang D; Wang J
[Ad] Endereço:State Key Laboratory of Bioelectronics, Southeast University, Nanjing 210096, China.
[Ti] Título:NF-κB controls four genes encoding core enzymes of tricarboxylic acid cycle.
[So] Source:Gene;621:12-20, 2017 Jul 20.
[Is] ISSN:1879-0038
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:NF-κB may promote tumor progression by altering cell metabolism. Hence, finding its target genes that are involved in cell metabolism is helpful for understanding its role in tumor growth. Here we discovered four metabolism-related target genes of this transcription factor. By analyzing a chromatin immunoprecipitation followed by deep sequencing (ChIP-Seq) data that characterizing the global binding sites (BSs) of NF-κB RelA in the TNFα-stimulated HeLa cells, we found that four genes that encode core enzymes of the tricarboxylic acid (TCA) cycle, including IDH1, IDH3A, ACO2, and SUCLA2, were multiply bound by this transcription factor. The subsequent bioinformatic analysis revealed that the NF-κB BSs contained many canonical κB sequences and the NF-κB-like DNA-binding motifs. Detection of ChIPed DNA with polymerase chain reaction (ChIP-PCR) also indicated that the NF-κB BSs were bound by NF-κB in both TNFα-treated HeLa and HepG2 cells. The reporter construct showed that the NF-κB BSs could activate the luciferase expression in cells in a NF-κB-specific manner. The quantitative PCR and Western blot detections demonstrated that NF-κB could regulate the expressions of IDH1, IDH3A, and ACO2 genes at both mRNA and protein levels and that of SUCLA2 gene at mRNA level in the TNFα-treated HeLa and HepG2 cells. Based on these investigations we identified the four genes as new target genes of NF-κB. The finding provides new insights into the role of NF-κB in cellular energetic metabolism, which may be beneficial for understanding the metabolic physiology of tumor growth.
[Mh] Termos MeSH primário: Ciclo do Ácido Cítrico/genética
Regulação Neoplásica da Expressão Gênica
NF-kappa B/metabolismo
[Mh] Termos MeSH secundário: Aconitato Hidratase/genética
Aconitato Hidratase/metabolismo
Células HeLa
Células Hep G2
Seres Humanos
Isocitrato Desidrogenase/genética
Isocitrato Desidrogenase/metabolismo
Succinato-CoA Ligases/genética
Succinato-CoA Ligases/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (NF-kappa B); EC 1.1.1.41 (Isocitrate Dehydrogenase); EC 1.1.1.42. (IDH1 protein, human); EC 4.2.1.3 (ACO2 protein, human); EC 4.2.1.3 (Aconitate Hydratase); EC 6.2.1.- (Succinate-CoA Ligases); EC 6.2.1.5 (SUCLA2 protein, human)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:170615
[Lr] Data última revisão:
170615
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170413
[St] Status:MEDLINE


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[PMID]:27913098
[Au] Autor:Huang X; Bedoyan JK; Demirbas D; Harris DJ; Miron A; Edelheit S; Grahame G; DeBrosse SD; Wong LJ; Hoppel CL; Kerr DS; Anselm I; Berry GT
[Ad] Endereço:Division of Genetics and Genomics, The Manton Center for Orphan Disease Research, Boston Children's Hospital, Boston, MA, USA.
[Ti] Título:Succinyl-CoA synthetase (SUCLA2) deficiency in two siblings with impaired activity of other mitochondrial oxidative enzymes in skeletal muscle without mitochondrial DNA depletion.
[So] Source:Mol Genet Metab;120(3):213-222, 2017 Mar.
[Is] ISSN:1096-7206
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Mutations in SUCLA2 result in succinyl-CoA ligase (ATP-forming) or succinyl-CoA synthetase (ADP-forming) (A-SCS) deficiency, a mitochondrial tricarboxylic acid cycle disorder. The phenotype associated with this gene defect is largely encephalomyopathy. We describe two siblings compound heterozygous for SUCLA2 mutations, c.985A>G (p.M329V) and c.920C>T (p.A307V), with parents confirmed as carriers of each mutation. We developed a new LC-MS/MS based enzyme assay to demonstrate the decreased SCS activity in the siblings with this unique genotype. Both siblings shared bilateral progressive hearing loss, encephalopathy, global developmental delay, generalized myopathy, and dystonia with choreoathetosis. Prior to diagnosis and because of lactic acidosis and low activity of muscle pyruvate dehydrogenase complex (PDC), sibling 1 (S1) was placed on dichloroacetate, while sibling 2 (S2) was on a ketogenic diet. S1 developed severe cyclic vomiting refractory to therapy, while S2 developed Leigh syndrome, severe GI dysmotility, intermittent anemia, hypogammaglobulinemia and eventually succumbed to his disorder. The mitochondrial DNA contents in skeletal muscle (SM) were normal in both siblings. Pyruvate dehydrogenase complex, ketoglutarate dehydrogenase complex, and several mitochondrial electron transport chain (ETC) activities were low or at the low end of the reference range in frozen SM from S1 and/or S2. In contrast, activities of PDC, other mitochondrial enzymes of pyruvate metabolism, ETC and, integrated oxidative phosphorylation, in skin fibroblasts were not significantly impaired. Although we show that propionyl-CoA inhibits PDC, it does not appear to account for decreased PDC activity in SM. A better understanding of the mechanisms of phenotypic variability and the etiology for tissue-specific secondary deficiencies of mitochondrial enzymes of oxidative metabolism, and independently mitochondrial DNA depletion (common in other cases of A-SCS deficiency), is needed given the implications for control of lactic acidosis and possible clinical management.
[Mh] Termos MeSH primário: Doenças Mitocondriais/genética
Músculo Esquelético/enzimologia
Polimorfismo de Nucleotídeo Único
Succinato-CoA Ligases/deficiência
[Mh] Termos MeSH secundário: Adolescente
Criança
DNA Mitocondrial/genética
Evolução Fatal
Seres Humanos
Masculino
Doenças Mitocondriais/enzimologia
Músculo Esquelético/metabolismo
Deleção de Sequência
Irmãos
Succinato-CoA Ligases/genética
[Pt] Tipo de publicação:CASE REPORTS; JOURNAL ARTICLE
[Nm] Nome de substância:
0 (DNA, Mitochondrial); EC 6.2.1.- (Succinate-CoA Ligases); EC 6.2.1.5 (SUCLA2 protein, human)
[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:161204
[St] Status:MEDLINE


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[PMID]:27478903
[Au] Autor:Vashisht K; Verma S; Gupta S; Lynn AM; Dixit R; Mishra N; Valecha N; Hamblin KA; Maytum R; Pandey KC; van der Giezen M
[Ad] Endereço:Host-parasite Interaction Biology Group, National Institute of Malaria Research, ICMR , New Delhi 110077, India.
[Ti] Título:Engineering Nucleotide Specificity of Succinyl-CoA Synthetase in Blastocystis: The Emerging Role of Gatekeeper Residues.
[So] Source:Biochemistry;56(3):534-542, 2017 Jan 24.
[Is] ISSN:1520-4995
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Charged, solvent-exposed residues at the entrance to the substrate binding site (gatekeeper residues) produce electrostatic dipole interactions with approaching substrates, and control their access by a novel mechanism called "electrostatic gatekeeper effect". This proof-of-concept study demonstrates that the nucleotide specificity can be engineered by altering the electrostatic properties of the gatekeeper residues outside the binding site. Using Blastocystis succinyl-CoA synthetase (SCS, EC 6.2.1.5), we demonstrated that the gatekeeper mutant (ED) resulted in ATP-specific SCS to show high GTP specificity. Moreover, nucleotide binding site mutant (LF) had no effect on GTP specificity and remained ATP-specific. However, via combination of the gatekeeper mutant with the nucleotide binding site mutant (ED+LF), a complete reversal of nucleotide specificity was obtained with GTP, but no detectable activity was obtained with ATP. This striking result of the combined mutant (ED+LF) was due to two changes; negatively charged gatekeeper residues (ED) favored GTP access, and nucleotide binding site residues (LF) altered ATP binding, which was consistent with the hypothesis of the "electrostatic gatekeeper effect". These results were further supported by molecular modeling and simulation studies. Hence, it is imperative to extend the strategy of the gatekeeper effect in a different range of crucial enzymes (synthetases, kinases, and transferases) to engineer substrate specificity for various industrial applications and substrate-based drug design.
[Mh] Termos MeSH primário: Trifosfato de Adenosina/química
Blastocystis/genética
Guanosina Trifosfato/química
Engenharia de Proteínas
Proteínas de Protozoários/química
Succinato-CoA Ligases/química
[Mh] Termos MeSH secundário: Trifosfato de Adenosina/metabolismo
Sequência de Aminoácidos
Animais
Sítios de Ligação
Blastocystis/enzimologia
Clonagem Molecular
Escherichia coli/genética
Escherichia coli/metabolismo
Expressão Gênica
Guanosina Trifosfato/metabolismo
Cinética
Simulação de Dinâmica Molecular
Mutação
Ligação Proteica
Estrutura Secundária de Proteína
Proteínas de Protozoários/genética
Proteínas de Protozoários/metabolismo
Proteínas Recombinantes/química
Proteínas Recombinantes/genética
Proteínas Recombinantes/metabolismo
Alinhamento de Sequência
Eletricidade Estática
Especificidade por Substrato
Succinato-CoA Ligases/genética
Succinato-CoA Ligases/metabolismo
Suínos
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Protozoan Proteins); 0 (Recombinant Proteins); 86-01-1 (Guanosine Triphosphate); 8L70Q75FXE (Adenosine Triphosphate); EC 6.2.1.- (Succinate-CoA Ligases)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:170515
[Lr] Data última revisão:
170515
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160802
[St] Status:MEDLINE
[do] DOI:10.1021/acs.biochem.6b00098


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[PMID]:27933791
[Au] Autor:Chen Y; Jiang Y; Guo Z
[Ad] Endereço:Department of Chemistry, The Hong Kong University of Science and Technology , Clear Water Bay, Kowloon, Hong Kong SAR, China.
[Ti] Título:Mechanistic Insights from the Crystal Structure of Bacillus subtilis o-Succinylbenzoyl-CoA Synthetase Complexed with the Adenylate Intermediate.
[So] Source:Biochemistry;55(48):6685-6695, 2016 Dec 06.
[Is] ISSN:1520-4995
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:o-Succinylbenzoyl-CoA (OSB-CoA) synthetase, or MenE, catalyzes an essential step in vitamin K biosynthesis and is a valuable drug target. Like many other adenylating enzymes, it changes its structure to accommodate substrate binding, catalysis, and product release along the path of a domain alternation catalytic mechanism. We have determined the crystal structure of its complex with the adenylation product, o-succinylbenzoyl-adenosine monophosphate (OSB-AMP), and captured a new postadenylation state. This structure presents unique features such as a strained conformation for the bound adenylate intermediate to indicate that it represents the enzyme state after completion of the adenylation reaction but before release of the C domain in its transition to the thioesterification conformation. By comparison to the ATP-bound preadenylation conformation, structural changes are identified in both the reactants and the active site to allow inference about how these changes accommodate and facilitate the adenylation reaction and to directly support an in-line backside attack nucleophilic substitution mechanism for the first half-reaction. Mutational analysis suggests that the conserved His196 plays an important role in desolvation of the active site rather than stabilizing the transition state of the adenylation reaction. In addition, comparison of the new structure with a previously determined OSB-AMP-bound structure of the same enzyme allows us to propose a release mechanism of the C domain in its alteration to form the thioesterification conformation. These findings allow us to better understand the domain alternation catalytic mechanism of MenE as well as many other adenylating enzymes.
[Mh] Termos MeSH primário: Monofosfato de Adenosina/metabolismo
Bacillus subtilis/enzimologia
Proteínas de Bactérias/metabolismo
Succinato-CoA Ligases/metabolismo
[Mh] Termos MeSH secundário: Monofosfato de Adenosina/química
Trifosfato de Adenosina/química
Trifosfato de Adenosina/metabolismo
Proteínas de Bactérias/química
Proteínas de Bactérias/genética
Biocatálise
Domínio Catalítico
Cristalografia por Raios X
Histidina/química
Histidina/genética
Histidina/metabolismo
Cinética
Modelos Químicos
Modelos Moleculares
Estrutura Molecular
Mutação
Ligação Proteica
Conformação Proteica
Domínios Proteicos
Especificidade por Substrato
Succinato-CoA Ligases/química
Succinato-CoA Ligases/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Bacterial Proteins); 415SHH325A (Adenosine Monophosphate); 4QD397987E (Histidine); 8L70Q75FXE (Adenosine Triphosphate); EC 6.2.1.- (Succinate-CoA Ligases); EC 6.2.1.26 (O-succinylbenzoate - CoA ligase)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:170529
[Lr] Data última revisão:
170529
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161210
[St] Status:MEDLINE


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[PMID]:27766610
[Au] Autor:Huang S; Wang J; Wang L
[Ad] Endereço:Department of Human Anatomy and Neuroscience, Medical School, Southeast University, Nanjing, China. huangsp-8888@163.com.
[Ti] Título:Knockdown of Sucla2 decreases the viability of mouse spermatocytes by inducing apoptosis through injury of the mitochondrial function of cells.
[So] Source:Folia Histochem Cytobiol;54(3):134-142, 2016.
[Is] ISSN:1897-5631
[Cp] País de publicação:Poland
[La] Idioma:eng
[Ab] Resumo:INTRODUCTION: Sucla2, a ß subunit of succinyl coenzyme A synthase, is located in the mitochondrial matrix. Sucla2 catalyzes the reversible synthesis of succinate and adenosine triphosphate (ATP) in the tricarboxylic acid cycle. Sucla2 expression was found to be correlated with the capacitation of boar spermatozoa. We have previously reported that Sucla2 was decreased in the testes of rats with spermatogenesis failure after exposure to endocrine disruptor BDE47. Yet, the expression model of Sucla2 in spermatogenesis and the function of Sucla2 in spermatogenic cells are still unclear. Our objective was to explore the localization of Sucla2 during mouse spermatogenesis and its function in the mouse spermatocyte line (GC2). MATERIAL AND METHODS: The localization of Sucla2 in the mouse testis was explored through immunohistochemistry (IHC). Sucla2 was knocked down in GC2 cells and its expression was detected by Western blot (WB) to verify the efficiency of the siRNA transfection. Mitochondrial membrane potential (MMP), apoptosis and ROS of GC2 were detected by flow cytometry. ATP production was measured by the luminometric method and the presence of Bcl2 of GC2 was detected by WB. RESULTS: Sucla2 is highly expressed in all germ cells but not in interstitial cells. Coarse Sucla2 signals are found in spermatocytes in stages VII­XII of mouse spermatogenesis. In GC2 cells, knockdown of Sucla2 decreased cell viability and MMP, induced apoptosis of GC2 cells, decreased ATP production, and Bcl2 expression, and increased ROS levels. CONCLUSIONS: Sucla2 is related to the developmental stages of mouse spermatogenesis. Knockdown of Sucla2 decreases the viability of mouse spermatocytes by inducing apoptosis via decreased mitochondrial function of the cells
[Mh] Termos MeSH primário: Mitocôndrias/fisiologia
Espermatócitos/fisiologia
Succinato-CoA Ligases/fisiologia
[Mh] Termos MeSH secundário: Trifosfato de Adenosina/metabolismo
Animais
Apoptose/fisiologia
Linhagem Celular
Sobrevivência Celular/efeitos dos fármacos
Técnicas de Silenciamento de Genes
Imuno-Histoquímica
Masculino
Potencial da Membrana Mitocondrial/efeitos dos fármacos
Camundongos
Camundongos Endogâmicos ICR
Mitocôndrias/enzimologia
Espécies Reativas de Oxigênio/metabolismo
Espermatócitos/citologia
Espermatogênese/efeitos dos fármacos
Espermatogênese/fisiologia
Succinato-CoA Ligases/deficiência
Succinato-CoA Ligases/genética
Ácido Succínico/metabolismo
Testículo/metabolismo
Testículo/fisiologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Reactive Oxygen Species); 8L70Q75FXE (Adenosine Triphosphate); AB6MNQ6J6L (Succinic Acid); EC 6.2.1.- (Succinate-CoA Ligases); EC 6.2.1.5 (Sucla2 protein, mouse)
[Em] Mês de entrada:1704
[Cu] Atualização por classe:170403
[Lr] Data última revisão:
170403
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161022
[St] Status:MEDLINE
[do] DOI:10.5603/FHC.a2016.0020


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[PMID]:27627803
[Au] Autor:Gomes C; Palma N; Pons MJ; Magallón-Tejada A; Sandoval I; Tinco-Valdez C; Gutarra C; Del Valle-Mendoza J; Ruiz J; Matsuoka M
[Ad] Endereço:ISGlobal, Barcelona Centre for International Health Research (CRESIB), Hospital Clínic, Universitat de Barcelona, Barcelona, Spain.
[Ti] Título:Succinyl-CoA Synthetase: New Antigen Candidate of Bartonella bacilliformis.
[So] Source:PLoS Negl Trop Dis;10(9):e0004989, 2016 Sep.
[Is] ISSN:1935-2735
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: Bartonella bacilliformis is the causative agent of Carrion's disease, a neglected illness with mortality rates of 40-85% in the absence of treatment. The lack of a diagnostic technique to overcome misdiagnosis and treat asymptomatic carriers is of note. This study aimed to identify new B. bacilliformis antigenic candidates that could lead to a new diagnostic tool able to be implemented in endemic rural areas. METHODOLOGY/PRINCIPAL FINDINGS: Blood (n = 198) and serum (n = 177) samples were collected in northern Peru. Clinical data were recorded. Specific 16S rRNA amplification by RT-PCR, IFA and ELISA for IgM/IgG with whole cells as antigens was done. Western blot analysis and N-terminal amino acid sequencing detected seroreactive proteins. ELISAs for IgM/IgG for the antigenic candidates were performed. Of the population 33.3% reported at least one symptom compatible with Carrion's disease; 25.4% (IFA), 27.1% (ELISA-IgG), 33.9% (ELISA-IgM) and 38.9% (RT-PCR) of samples were positive. Four proteins were considered potential antigenic candidates, including two new antigenic candidates, succinyl-CoA synthetase subunit α (SCS-α) and succinyl-CoA synthetase subunit ß (SCS-ß). On Western blot both Pap31 and SCS-α interacted with IgM, while GroEL and SCS-ß interacted with IgG. The presence of specific antibodies against the antigenic candidates varied from 34.5% (IgG against SCS-α) to 97.2% (IgM against Pap31). CONCLUSIONS/SIGNIFICANCE: RT-PCR and the high levels of positivity for specific ELISAs demonstrate high levels of B. bacilliformis exposure and asymptomatic carriers among inhabitants. The new antigens identified might be used as a new rapid diagnostic tool to diagnose acute Carrion's disease and identify asymptomatic carriers.
[Mh] Termos MeSH primário: Antígenos de Bactérias/imunologia
Infecções por Bartonella/microbiologia
Bartonella bacilliformis/imunologia
Succinato-CoA Ligases/imunologia
[Mh] Termos MeSH secundário: Adolescente
Adulto
Idoso
Idoso de 80 Anos ou mais
Animais
Anticorpos Antibacterianos/sangue
Antígenos de Bactérias/genética
Infecções por Bartonella/imunologia
Western Blotting
Cercopithecus aethiops
Criança
Pré-Escolar
Ensaio de Imunoadsorção Enzimática
Feminino
Seres Humanos
Imunoglobulina G/sangue
Imunoglobulina M/sangue
Lactente
Masculino
Meia-Idade
Peru
RNA Ribossômico 16S/genética
Reação em Cadeia da Polimerase em Tempo Real
Succinato-CoA Ligases/genética
Células Vero
Adulto Jovem
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antibodies, Bacterial); 0 (Antigens, Bacterial); 0 (Immunoglobulin G); 0 (Immunoglobulin M); 0 (RNA, Ribosomal, 16S); EC 6.2.1.- (Succinate-CoA Ligases)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:170616
[Lr] Data última revisão:
170616
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160915
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pntd.0004989


  10 / 284 MEDLINE  
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[PMID]:27496549
[Au] Autor:Kacso G; Ravasz D; Doczi J; Németh B; Madgar O; Saada A; Ilin P; Miller C; Ostergaard E; Iordanov I; Adams D; Vargedo Z; Araki M; Araki K; Nakahara M; Ito H; Gál A; Molnár MJ; Nagy Z; Patocs A; Adam-Vizi V; Chinopoulos C
[Ad] Endereço:Department of Medical Biochemistry, Semmelweis University, Tuzolto Street 37-47, Budapest 1094, Hungary MTA-SE Lendület Neurobiochemistry Research Group, Budapest 1094, Hungary.
[Ti] Título:Two transgenic mouse models for ß-subunit components of succinate-CoA ligase yielding pleiotropic metabolic alterations.
[So] Source:Biochem J;473(20):3463-3485, 2016 Oct 15.
[Is] ISSN:1470-8728
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Succinate-CoA ligase (SUCL) is a heterodimer enzyme composed of Suclg1 α-subunit and a substrate-specific Sucla2 or Suclg2 ß-subunit yielding ATP or GTP, respectively. In humans, the deficiency of this enzyme leads to encephalomyopathy with or without methylmalonyl aciduria, in addition to resulting in mitochondrial DNA depletion. We generated mice lacking either one Sucla2 or Suclg2 allele. Sucla2 heterozygote mice exhibited tissue- and age-dependent decreases in Sucla2 expression associated with decreases in ATP-forming activity, but rebound increases in cardiac Suclg2 expression and GTP-forming activity. Bioenergetic parameters including substrate-level phosphorylation (SLP) were not different between wild-type and Sucla2 heterozygote mice unless a submaximal pharmacological inhibition of SUCL was concomitantly present. mtDNA contents were moderately decreased, but blood carnitine esters were significantly elevated. Suclg2 heterozygote mice exhibited decreases in Suclg2 expression but no rebound increases in Sucla2 expression or changes in bioenergetic parameters. Surprisingly, deletion of one Suclg2 allele in Sucla2 heterozygote mice still led to a rebound but protracted increase in Suclg2 expression, yielding double heterozygote mice with no alterations in GTP-forming activity or SLP, but more pronounced changes in mtDNA content and blood carnitine esters, and an increase in succinate dehydrogenase activity. We conclude that a partial reduction in Sucla2 elicits rebound increases in Suclg2 expression, which is sufficiently dominant to overcome even a concomitant deletion of one Suclg2 allele, pleiotropically affecting metabolic pathways associated with SUCL. These results as well as the availability of the transgenic mouse colonies will be of value in understanding SUCL deficiency.
[Mh] Termos MeSH primário: Succinato-CoA Ligases/metabolismo
[Mh] Termos MeSH secundário: Alelos
Animais
Western Blotting
Carnitina/análogos & derivados
Carnitina/metabolismo
Células Cultivadas
DNA Mitocondrial/genética
Heterozigoto
Seres Humanos
Técnicas In Vitro
Potencial da Membrana Mitocondrial/genética
Potencial da Membrana Mitocondrial/fisiologia
Camundongos
Camundongos Knockout
Camundongos Mutantes
Mitocôndrias/genética
Fosforilação/genética
Fosforilação/fisiologia
RNA Mensageiro/genética
Succinato-CoA Ligases/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (DNA, Mitochondrial); 0 (RNA, Messenger); 0 (acylcarnitine); EC 6.2.1.- (Succinate-CoA Ligases); EC 6.2.1.5 (Sucla2 protein, mouse); S7UI8SM58A (Carnitine)
[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:160807
[St] Status:MEDLINE



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