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Pesquisa : D08.811.913.050.350 [Categoria DeCS]
Referências encontradas : 352 [refinar]
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[PMID]:28438511
[Au] Autor:Tonazzi A; Giangregorio N; Console L; De Palma A; Indiveri C
[Ad] Endereço:CNR Institute of Biomembranes, Bioenergetics and Molecular Biotechnology, via Amendola 165/A, 70126 Bari, Italy.
[Ti] Título:Nitric oxide inhibits the mitochondrial carnitine/acylcarnitine carrier through reversible S-nitrosylation of cysteine 136.
[So] Source:Biochim Biophys Acta;1858(7):475-482, 2017 07.
[Is] ISSN:0006-3002
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:S-nitrosylation of the mitochondrial carnitine/acylcarnitine transporter (CACT) has been investigated on the native and the recombinant proteins reconstituted in proteoliposomes, and on intact mitochondria. The widely-used NO-releasing compound, GSNO, strongly inhibited the antiport measured in proteoliposomes reconstituted with the native CACT from rat liver mitochondria or the recombinant rat CACT over-expressed in E. coli. Inhibition was reversed by the reducing agent dithioerythritol, indicating a reaction mechanism based on nitrosylation of Cys residues of the CACT. The half inhibition constant (IC50) was very similar for the native and recombinant proteins, i.e., 74 and 71µM, respectively. The inhibition resulted to be competitive with respect the substrate, carnitine. NO competed also with NEM, correlating well with previous data showing interference of NEM with the substrate transport path. Using a site-directed mutagenesis approach on Cys residues of the recombinant CACT, the target of NO was identified. C136 plays a major role in the reaction mechanism. The occurrence of S-nitrosylation was demonstrated in intact mitochondria after treatment with GSNO, immunoprecipitation and immunostaining of CACT with a specific anti NO-Cys antibody. In parallel samples, transport activity of CACT measured in intact mitochondria, was strongly inhibited after GSNO treatment. The possible physiological and pathological implications of the post-translational modification of CACT are discussed.
[Mh] Termos MeSH primário: Carnitina Aciltransferases/antagonistas & inibidores
Cisteína/química
Mitocôndrias/metabolismo
Óxido Nítrico/farmacologia
Processamento de Proteína Pós-Traducional
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Animais
Transporte Biológico
Carnitina/análogos & derivados
Carnitina/metabolismo
Carnitina Aciltransferases/química
Carnitina Aciltransferases/genética
Carnitina Aciltransferases/metabolismo
Sequência Conservada
Ditioeritritol/farmacologia
Lipossomos
Mitocôndrias/efeitos dos fármacos
Modelos Moleculares
Doadores de Óxido Nítrico/farmacologia
Nitrogênio
Oxirredução
Conformação Proteica
Processamento de Proteína Pós-Traducional/efeitos dos fármacos
Ratos
S-Nitrosoglutationa/farmacologia
Alinhamento de Sequência
Homologia de Sequência de Aminoácidos
[Pt] Tipo de publicação:COMPARATIVE STUDY; JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Liposomes); 0 (Nitric Oxide Donors); 0 (acylcarnitine); 31C4KY9ESH (Nitric Oxide); 57564-91-7 (S-Nitrosoglutathione); 6892-68-8 (Dithioerythritol); EC 2.3.1.- (Carnitine Acyltransferases); EC 2.3.1.- (Slc25a20 protein, rat); K848JZ4886 (Cysteine); N762921K75 (Nitrogen); S7UI8SM58A (Carnitine)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171027
[Lr] Data última revisão:
171027
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170426
[St] Status:MEDLINE


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[PMID]:27864727
[Au] Autor:Giangregorio N; Tonazzi A; Console L; Indiveri C
[Ad] Endereço:CNR Institute of Biomembranes and Bioenergetics, Via Amendola 165/A, 70126, Bari, Italy. n.giangregorio@ibbe.cnr.it.
[Ti] Título:Post-translational modification by acetylation regulates the mitochondrial carnitine/acylcarnitine transport protein.
[So] Source:Mol Cell Biochem;426(1-2):65-73, 2017 Feb.
[Is] ISSN:1573-4919
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:The carnitine/acylcarnitine transporter (CACT; SLC25A20) mediates an antiport reaction allowing entry of acyl moieties in the form of acylcarnitines into the mitochondrial matrix and exit of free carnitine. The transport function of CACT is crucial for the ß-oxidation pathway. In this work, it has been found that CACT is partially acetylated in rat liver mitochondria as demonstrated by anti-acetyl-lys antibody immunostaining. Acetylation was reversed by the deacetylase Sirtuin 3 in the presence of NAD . After treatment of the mitochondrial extract with the deacetylase, the CACT activity, assayed in proteoliposomes, increased. The half-saturation constant of the CACT was not influenced, while the V was increased by deacetylation. Sirtuin 3 was not able to deacetylate the CACT when incubation was performed in intact mitoplasts, indicating that the acetylation sites are located in the mitochondrial matrix. Prediction on the localization of acetylated residues by bioinformatics correlates well with the experimental data. Recombinant CACT treated with acetyl-CoA was partially acetylated by non-enzymatic mechanism with a corresponding decrease of transport activity. The experimental data indicate that acetylation of CACT inhibits its transport activity, and thus may contribute to the regulation of the mitochondrial ß-oxidation pathway.
[Mh] Termos MeSH primário: Carnitina Aciltransferases/metabolismo
Proteínas Mitocondriais/metabolismo
Processamento de Proteína Pós-Traducional/fisiologia
[Mh] Termos MeSH secundário: Acetilação
Animais
Transporte Biológico Ativo/fisiologia
Carnitina Aciltransferases/química
Carnitina Aciltransferases/genética
Proteínas Mitocondriais/química
Proteínas Mitocondriais/genética
NAD/química
NAD/genética
NAD/metabolismo
Ratos
Proteínas Recombinantes/química
Proteínas Recombinantes/genética
Proteínas Recombinantes/metabolismo
Sirtuína 3/química
Sirtuína 3/genética
Sirtuína 3/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Mitochondrial Proteins); 0 (Recombinant Proteins); 0U46U6E8UK (NAD); EC 2.3.1.- (Carnitine Acyltransferases); EC 2.3.1.- (Slc25a20 protein, rat); EC 3.5.1.- (Sirtuin 3)
[Em] Mês de entrada:1702
[Cu] Atualização por classe:171030
[Lr] Data última revisão:
171030
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161120
[St] Status:MEDLINE
[do] DOI:10.1007/s11010-016-2881-0


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[PMID]:27502741
[Au] Autor:Convertini P; Menga A; Andria G; Scala I; Santarsiero A; Castiglione Morelli MA; Iacobazzi V; Infantino V
[Ad] Endereço:Department of Science, University of Basilicata, Potenza, Italy.
[Ti] Título:The contribution of the citrate pathway to oxidative stress in Down syndrome.
[So] Source:Immunology;149(4):423-431, 2016 Dec.
[Is] ISSN:1365-2567
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Inflammatory conditions and oxidative stress have a crucial role in Down syndrome (DS). Emerging studies have also reported an altered lipid profile in the early stages of DS. Our previous works demonstrate that citrate pathway activation is required for oxygen radical production during inflammation. Here, we find up-regulation of the citrate pathway and down-regulation of carnitine/acylcarnitine carrier and carnitine palmitoyl-transferase 1 genes in cells from children with DS. Interestingly, when the citrate pathway is inhibited, we observe a reduction in oxygen radicals as well as in lipid peroxidation levels. Our preliminary findings provide evidence for a citrate pathway dysregulation, which could be related to some phenotypic traits of people with DS.
[Mh] Termos MeSH primário: Proteínas de Transporte de Ânions/metabolismo
Carnitina Aciltransferases/metabolismo
Carnitina O-Palmitoiltransferase/metabolismo
Carnitina/metabolismo
Ácido Cítrico/metabolismo
Síndrome de Down/metabolismo
Leucócitos/fisiologia
Proteínas Mitocondriais/metabolismo
[Mh] Termos MeSH secundário: Proteínas de Transporte de Ânions/genética
Carnitina Aciltransferases/genética
Carnitina O-Palmitoiltransferase/genética
Linhagem Celular Transformada
Pré-Escolar
Síndrome de Down/genética
Síndrome de Down/imunologia
Regulação da Expressão Gênica
Seres Humanos
Peroxidação de Lipídeos
Proteínas Mitocondriais/genética
Estresse Oxidativo
Fenótipo
Característica Quantitativa Herdável
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Anion Transport Proteins); 0 (Mitochondrial Proteins); 0 (Slc25a1 protein, human); 2968PHW8QP (Citric Acid); EC 2.3.1.- (Carnitine Acyltransferases); EC 2.3.1.21 (Carnitine O-Palmitoyltransferase); S7UI8SM58A (Carnitine)
[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:160810
[St] Status:MEDLINE
[do] DOI:10.1111/imm.12659


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[PMID]:27354540
[Au] Autor:Britton L; Jaskowski L; Bridle K; Santrampurwala N; Reiling J; Musgrave N; Subramaniam VN; Crawford D
[Ad] Endereço:Gallipoli Medical Research Institute, Greenslopes Private Hospital, Greenslopes, Queensland, Australia The School of Medicine, University of Queensland, Herston, Queensland, Australia The Department of Gastroenterology, Princess Alexandra Hospital, Woolloongabba, Queensland, Australia QIMR Berghofer
[Ti] Título:Heterozygous Hfe gene deletion leads to impaired glucose homeostasis, but not liver injury in mice fed a high-calorie diet.
[So] Source:Physiol Rep;4(12), 2016 Jun.
[Is] ISSN:2051-817X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Heterozygous mutations of the Hfe gene have been proposed as cofactors in the development and progression of nonalcoholic fatty liver disease (NAFLD). Homozygous Hfe deletion previously has been shown to lead to dysregulated hepatic lipid metabolism and accentuated liver injury in a dietary mouse model of NAFLD We sought to establish whether heterozygous deletion of Hfe is sufficient to promote liver injury when mice are exposed to a high-calorie diet (HCD). Eight-week-old wild-type and Hfe(+/-) mice received 8 weeks of a control diet or HCD Liver histology and pathways of lipid and iron metabolism were analyzed. Liver histology demonstrated that mice fed a HCD had increased NAFLD activity score (NAS), steatosis, and hepatocyte ballooning. However, liver injury was unaffected by Hfe genotype. Hepatic iron concentration (HIC) was increased in Hfe(+/-) mice of both dietary groups. HCD resulted in a hepcidin-independent reduction in HIC Hfe(+/-) mice demonstrated raised fasting serum glucose concentrations and HOMA-IR score, despite unaltered serum adiponectin concentrations. Downstream regulators of hepatic de novo lipogenesis (pAKT, SREBP-1, Fas, Scd1) and fatty acid oxidation (AdipoR2, Pparα, Cpt1) were largely unaffected by genotype. In summary, heterozygous Hfe gene deletion is associated with impaired iron and glucose metabolism. However, unlike homozygous Hfe deletion, heterozygous gene deletion did not affect lipid metabolism pathways or liver injury in this model.
[Mh] Termos MeSH primário: Dieta Hiperlipídica/efeitos adversos
Deleção de Genes
Glucose/metabolismo
Antígenos de Histocompatibilidade Classe I/metabolismo
Homeostase
Proteínas de Membrana/metabolismo
Hepatopatia Gordurosa não Alcoólica/metabolismo
[Mh] Termos MeSH secundário: Animais
Carnitina Aciltransferases/metabolismo
Proteína da Hemocromatose
Hepatócitos/metabolismo
Heterozigoto
Antígenos de Histocompatibilidade Classe I/genética
Ferro/metabolismo
Lipogênese
Fígado/metabolismo
Masculino
Proteínas de Membrana/genética
Camundongos
Camundongos Endogâmicos C57BL
Hepatopatia Gordurosa não Alcoólica/genética
PPAR alfa/metabolismo
Receptores de Adiponectina/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Hemochromatosis Protein); 0 (Hfe protein, mouse); 0 (Histocompatibility Antigens Class I); 0 (Membrane Proteins); 0 (PPAR alpha); 0 (Receptors, Adiponectin); E1UOL152H7 (Iron); EC 2.3.1.- (Carnitine Acyltransferases); IY9XDZ35W2 (Glucose)
[Em] Mês de entrada:1610
[Cu] Atualização por classe:170220
[Lr] Data última revisão:
170220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160630
[St] Status:MEDLINE


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[PMID]:27231907
[Au] Autor:Giudetti AM; Stanca E; Siculella L; Gnoni GV; Damiano F
[Ad] Endereço:Laboratory of Biochemistry and Molecular Biology, Department of Biological and Environmental Sciences and Technologies, University of Salento, Lecce 73100, Italy. anna.giudetti@unisalento.it.
[Ti] Título:Nutritional and Hormonal Regulation of Citrate and Carnitine/Acylcarnitine Transporters: Two Mitochondrial Carriers Involved in Fatty Acid Metabolism.
[So] Source:Int J Mol Sci;17(6), 2016 May 25.
[Is] ISSN:1422-0067
[Cp] País de publicação:Switzerland
[La] Idioma:eng
[Ab] Resumo:The transport of solutes across the inner mitochondrial membrane is catalyzed by a family of nuclear-encoded membrane-embedded proteins called mitochondrial carriers (MCs). The citrate carrier (CiC) and the carnitine/acylcarnitine transporter (CACT) are two members of the MCs family involved in fatty acid metabolism. By conveying acetyl-coenzyme A, in the form of citrate, from the mitochondria to the cytosol, CiC contributes to fatty acid and cholesterol synthesis; CACT allows fatty acid oxidation, transporting cytosolic fatty acids, in the form of acylcarnitines, into the mitochondrial matrix. Fatty acid synthesis and oxidation are inversely regulated so that when fatty acid synthesis is activated, the catabolism of fatty acids is turned-off. Malonyl-CoA, produced by acetyl-coenzyme A carboxylase, a key enzyme of cytosolic fatty acid synthesis, represents a regulator of both metabolic pathways. CiC and CACT activity and expression are regulated by different nutritional and hormonal conditions. Defects in the corresponding genes have been directly linked to various human diseases. This review will assess the current understanding of CiC and CACT regulation; underlining their roles in physio-pathological conditions. Emphasis will be placed on the molecular basis of the regulation of CiC and CACT associated with fatty acid metabolism.
[Mh] Termos MeSH primário: Carnitina Aciltransferases/metabolismo
Proteínas de Transporte/metabolismo
Colesterol/biossíntese
Ácidos Graxos/biossíntese
Hormônios Tireóideos/fisiologia
[Mh] Termos MeSH secundário: Acetilcoenzima A/metabolismo
Animais
Carnitina Aciltransferases/genética
Proteínas de Transporte/genética
Citosol/metabolismo
Regulação Enzimológica da Expressão Gênica
Seres Humanos
Lipogênese
Mitocôndrias/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Carrier Proteins); 0 (Fatty Acids); 0 (Thyroid Hormones); 0 (citrate-binding transport protein); 72-89-9 (Acetyl Coenzyme A); 97C5T2UQ7J (Cholesterol); EC 2.3.1.- (Carnitine Acyltransferases)
[Em] Mês de entrada:1703
[Cu] Atualização por classe:170315
[Lr] Data última revisão:
170315
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160528
[St] Status:MEDLINE


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[PMID]:27199118
[Au] Autor:Chen J; Young ME; Chatham JC; Crossman DK; Dell'Italia LJ; Shalev A
[Ad] Endereço:Endocrinology, Diabetes and Metabolism, Department of Medicine, University of Alabama at Birmingham, Birmingham, Alabama;
[Ti] Título:TXNIP regulates myocardial fatty acid oxidation via miR-33a signaling.
[So] Source:Am J Physiol Heart Circ Physiol;311(1):H64-75, 2016 Jul 01.
[Is] ISSN:1522-1539
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Myocardial fatty acid ß-oxidation is critical for the maintenance of energy homeostasis and contractile function in the heart, but its regulation is still not fully understood. While thioredoxin-interacting protein (TXNIP) has recently been implicated in cardiac metabolism and mitochondrial function, its effects on ß-oxidation have remained unexplored. Using a new cardiomyocyte-specific TXNIP knockout mouse and working heart perfusion studies, as well as loss- and gain-of-function experiments in rat H9C2 and human AC16 cardiomyocytes, we discovered that TXNIP deficiency promotes myocardial ß-oxidation via signaling through a specific microRNA, miR-33a. TXNIP deficiency leads to increased binding of nuclear factor Y (NFYA) to the sterol regulatory element binding protein 2 (SREBP2) promoter, resulting in transcriptional inhibition of SREBP2 and its intronic miR-33a. This allows for increased translation of the miR-33a target genes and ß-oxidation-promoting enzymes, carnitine octanoyl transferase (CROT), carnitine palmitoyl transferase 1 (CPT1), hydroxyacyl-CoA dehydrogenase/3-ketoacyl-CoA thiolase/enoyl-CoA hydratase-ß (HADHB), and AMPKα and is associated with an increase in phospho-AMPKα and phosphorylation/inactivation of acetyl-CoA-carboxylase. Thus, we have identified a novel TXNIP-NFYA-SREBP2/miR-33a-AMPKα/CROT/CPT1/HADHB pathway that is conserved in mouse, rat, and human cardiomyocytes and regulates myocardial ß-oxidation.
[Mh] Termos MeSH primário: Proteínas de Transporte/metabolismo
Metabolismo Energético
Ácidos Graxos/metabolismo
MicroRNAs/metabolismo
Miócitos Cardíacos/metabolismo
Tiorredoxinas/metabolismo
[Mh] Termos MeSH secundário: Proteínas Quinases Ativadas por AMP/genética
Proteínas Quinases Ativadas por AMP/metabolismo
Animais
Fator de Ligação a CCAAT/genética
Fator de Ligação a CCAAT/metabolismo
Carnitina Aciltransferases/genética
Carnitina Aciltransferases/metabolismo
Carnitina O-Palmitoiltransferase/genética
Carnitina O-Palmitoiltransferase/metabolismo
Proteínas de Transporte/genética
Linhagem Celular
Regulação Enzimológica da Expressão Gênica
Genótipo
Seres Humanos
Preparação de Coração Isolado
Masculino
Camundongos Endogâmicos C57BL
Camundongos Knockout
MicroRNAs/genética
Subunidade beta da Proteína Mitocondrial Trifuncional/genética
Subunidade beta da Proteína Mitocondrial Trifuncional/metabolismo
Miócitos Cardíacos/enzimologia
Oxirredução
Fenótipo
Interferência de RNA
Ratos
Transdução de Sinais
Proteína de Ligação a Elemento Regulador de Esterol 2/genética
Proteína de Ligação a Elemento Regulador de Esterol 2/metabolismo
Tiorredoxinas/genética
Transfecção
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (CCAAT-Binding Factor); 0 (Carrier Proteins); 0 (Fatty Acids); 0 (MIRN33 microRNA, human); 0 (MIRN33 microRNA, rat); 0 (MicroRNAs); 0 (Mirn33 microRNA, mouse); 0 (Nfya protein, mouse); 0 (Srebf2 protein, mouse); 0 (Sterol Regulatory Element Binding Protein 2); 0 (TXNIP protein, human); 0 (TXNIP protein, rat); 0 (Txnip protein, mouse); 52500-60-4 (Thioredoxins); EC 2.3.1.- (Carnitine Acyltransferases); EC 2.3.1.- (carnitine octanoyltransferase); EC 2.3.1.16 (Hadhb protein, mouse); EC 2.3.1.16 (Mitochondrial Trifunctional Protein, beta Subunit); EC 2.3.1.21 (Carnitine O-Palmitoyltransferase); EC 2.7.11.31 (AMP-Activated Protein Kinases)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160521
[St] Status:MEDLINE
[do] DOI:10.1152/ajpheart.00151.2016


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[PMID]:26459002
[Au] Autor:Giangregorio N; Tonazzi A; Console L; Lorusso I; De Palma A; Indiveri C
[Ad] Endereço:CNR Institute of Biomembranes and Bioenergetics, Via Amendola 165/A, 70126 Bari, Italy.
[Ti] Título:The mitochondrial carnitine/acylcarnitine carrier is regulated by hydrogen sulfide via interaction with C136 and C155.
[So] Source:Biochim Biophys Acta;1860(1 Pt A):20-7, 2016 Jan.
[Is] ISSN:0006-3002
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: The carnitine/acylcarnitine carrier (CAC or CACT) mediates transport of acylcarnitines into mitochondria for the ß-oxidation. CAC possesses Cys residues which respond to redox changes undergoing to SH/disulfide interconversion. METHODS: The effect of H2S has been investigated on the [(3)H]carnitine/carnitine antiport catalyzed by recombinant or native CAC reconstituted in proteoliposomes. Site-directed mutagenesis was employed for identifying Cys reacting with H2S. RESULTS: H2S led to transport inhibition, which was dependent on concentration, pH and time of incubation. Best inhibition with IC50 of 0.70 µM was observed at physiological pH after 30-60 min incubation. At longer times of incubation, inhibition was reversed. After oxidation of the carrier by O2, transport activity was rescued by H2S indicating that the inhibition/activation depends on the initial redox state of the protein. The observed effects were more efficient on the native rat liver transporter than on the recombinant protein. Only the protein containing both C136 and C155 responded to the reagent as the WT. While reduced responses were observed in the mutants containing C136 or C155. Multi-alignment of known mitochondrial carriers, highlighted that only the CAC possesses both Cys residues. This correlates well with the absence of effects of H2S on carriers which does not contain the Cys couple. CONCLUSIONS: Altogether, these data demonstrate that H2S regulates the CAC by inhibiting or activating transport on the basis of the redox state of the protein. GENERAL SIGNIFICANCE: CAC represents a specific target of H2S among mitochondrial carriers in agreement with the presence of a reactive Cys couple.
[Mh] Termos MeSH primário: Carnitina Aciltransferases/antagonistas & inibidores
Cisteína/química
Sulfeto de Hidrogênio/farmacologia
Mitocôndrias/metabolismo
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Carnitina Aciltransferases/química
Dados de Sequência Molecular
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
EC 2.3.1.- (Carnitine Acyltransferases); K848JZ4886 (Cysteine); YY9FVM7NSN (Hydrogen Sulfide)
[Em] Mês de entrada:1605
[Cu] Atualização por classe:161126
[Lr] Data última revisão:
161126
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:151014
[St] Status:MEDLINE


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[PMID]:26057744
[Au] Autor:Zheng Y; Jiang S; Zhang Y; Zhang R; Gong D
[Ad] Endereço:College of Animal Science and Technology, Yangzhou University, Yangzhou 225009, China. zhengyun@yzu.edu.cn.
[Ti] Título:Detection of miR-33 Expression and the Verification of Its Target Genes in the Fatty Liver of Geese.
[So] Source:Int J Mol Sci;16(6):12737-52, 2015 Jun 05.
[Is] ISSN:1422-0067
[Cp] País de publicação:Switzerland
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: miRNAs are single-stranded, small RNA molecules with a length of 18-25 nucleotides. They bind to the 3' untranslated regions of mRNA transcripts to reduce the translation of these transcripts or to cause their degradation. The roles of these molecules differ in biological processes, such as cell differentiation, proliferation, apoptosis and tumor genesis. miRNA-33 is encoded by the gene introns of proteins that bind sterol-regulatory elements. This molecule cooperates with these proteins to control cholesterol homeostasis, fatty acid levels and the genes that are related to the expression of fat metabolism. The examination of miR-33 expression and its target genes can promote the in-depth study of the miRNA regulation mechanism in the formation process of goose fatty liver and can lay a foundation for research into human fatty liver. METHODOLOGY/PRINCIPAL FINDINGS: (1) Through real-time fluorescent quantitative polymerase chain reaction (TaqMan MicroRNA Assay), we detected the expression of miR-33 during the feeding of Landes geese. The expression level of miR-33 increases significantly in the liver after 19 days in comparison with the control group; (2) By using the bioinformatics software programs TargetScan, miRDB and miRCosm to predict the target genes of miR-33 according to laboratory prophase transcriptome results and references, we screen nine target genes: adenosine triphosphate binding cassette transporters A1, adenosine triphosphate binding cassette transporters G1, Neimann Pick C, carnitine O-octanoyltransferase (CROT), cyl-CoA dehydrogenase/3-ketoacyl-CoA thiolase/enoyl-CoA hydratase, beta subunit (HADHB), AMP-activated protein kinase, alpha subunit 1 (AMPKα1), insulin receptor substrate 2, glutamic pyruvate transaminase and adipose differentiation-related protein. The dual luciferase reporter gene system in the CHO cell line verifies that CROT, HADHB and NPC1 are the target genes of miR-33 in geese. The inhibition rate of CROT is highest and reaches 70%; (3) The seed sequence (5' 2-8 bases) is the acting site of miR-33. The two predicted target sites of CROT are the target sites of miR-33. Moreover, the predicted target site of HADHB and NPC1 is the target site of miR-33. CONCLUSIONS/SIGNIFICANCE: (1) After 19 days of overfeeding, the expression level of miR-33 increases significantly in the livers of geese; (2) CROT, HADHB and NPC1 are the target genes of miR-33 in geese. These genes determine the combined target site.
[Mh] Termos MeSH primário: Fígado Gorduroso/metabolismo
MicroRNAs/genética
Transcriptoma
[Mh] Termos MeSH secundário: Animais
Carnitina Aciltransferases/genética
Carnitina Aciltransferases/metabolismo
Gansos
Glicoproteínas de Membrana/genética
Glicoproteínas de Membrana/metabolismo
Subunidade beta da Proteína Mitocondrial Trifuncional/genética
Subunidade beta da Proteína Mitocondrial Trifuncional/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Membrane Glycoproteins); 0 (MicroRNAs); EC 2.3.1.- (Carnitine Acyltransferases); EC 2.3.1.- (carnitine octanoyltransferase); EC 2.3.1.16 (Mitochondrial Trifunctional Protein, beta Subunit)
[Em] Mês de entrada:1603
[Cu] Atualização por classe:150708
[Lr] Data última revisão:
150708
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150610
[St] Status:MEDLINE
[do] DOI:10.3390/ijms160612737


  9 / 352 MEDLINE  
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[PMID]:26010953
[Au] Autor:Zhou S; Xiong L; Xie P; Ambalavanan A; Bourassa CV; Dionne-Laporte A; Spiegelman D; Turcotte Gauthier M; Henrion E; Diallo O; Dion PA; Rouleau GA
[Ad] Endereço:Montreal Neurological Institute and Hospital, McGill University, Montréal (Que), Canada; Département de médecine, Faculté de médecine, Université de Montréal, Montréal (Que), Canada.
[Ti] Título:Increased missense mutation burden of Fatty Acid metabolism related genes in nunavik inuit population.
[So] Source:PLoS One;10(5):e0128255, 2015.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: Nunavik Inuit (northern Quebec, Canada) reside along the arctic coastline where for generations their daily energy intake has mainly been derived from animal fat. Given this particular diet it has been hypothesized that natural selection would lead to population specific allele frequency differences and unique variants in genes related to fatty acid metabolism. A group of genes, namely CPT1A, CPT1B, CPT1C, CPT2, CRAT and CROT, encode for three carnitine acyltransferases that are important for the oxidation of fatty acids, a critical step in their metabolism. METHODS: Exome sequencing and SNP array genotyping were used to examine the genetic variations in the six genes encoding for the carnitine acyltransferases in 113 Nunavik Inuit individuals. RESULTS: Altogether ten missense variants were found in genes CPT1A, CPT1B, CPT1C, CPT2 and CRAT, including three novel variants and one Inuit specific variant CPT1A p.P479L (rs80356779). The latter has the highest frequency (0.955) compared to other Inuit populations. We found that by comparison to Asians or Europeans, the Nunavik Inuit have an increased mutation burden in CPT1A, CPT2 and CRAT; there is also a high level of population differentiation based on carnitine acyltransferase gene variations between Nunavik Inuit and Asians. CONCLUSION: The increased number and frequency of deleterious variants in these fatty acid metabolism genes in Nunavik Inuit may be the result of genetic adaptation to their diet and/or the extremely cold climate. In addition, the identification of these variants may help to understand some of the specific health risks of Nunavik Inuit.
[Mh] Termos MeSH primário: Carnitina Aciltransferases/genética
Exoma
Ácidos Graxos/genética
Inuítes/genética
Mutação de Sentido Incorreto
Polimorfismo de Nucleotídeo Único
[Mh] Termos MeSH secundário: Carnitina Aciltransferases/metabolismo
Gorduras na Dieta/administração & dosagem
Gorduras na Dieta/efeitos adversos
Ácidos Graxos/metabolismo
Feminino
Seres Humanos
Masculino
Meia-Idade
Oxirredução
Quebeque
[Pt] Tipo de publicação:CLINICAL TRIAL; JOURNAL ARTICLE; MULTICENTER STUDY; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Dietary Fats); 0 (Fatty Acids); EC 2.3.1.- (Carnitine Acyltransferases)
[Em] Mês de entrada:1604
[Cu] Atualização por classe:150617
[Lr] Data última revisão:
150617
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150527
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0128255


  10 / 352 MEDLINE  
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[PMID]:25910653
[Au] Autor:Tonazzi A; Giangregorio N; Console L; Indiveri C
[Ad] Endereço:CNR Institute of Biomembranes and Bioenergetics, via Amendola 165/A, 70126 Bari, Italy. a.tonazzi@ibbe.cnr.it.
[Ti] Título:Mitochondrial carnitine/acylcarnitine translocase: insights in structure/ function relationships. Basis for drug therapy and side effects prediction.
[So] Source:Mini Rev Med Chem;15(5):396-405, 2015.
[Is] ISSN:1875-5607
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:The mitochondrial carnitine/acylcarnitine translocase has been identified, purified and reconstituted in liposomes in 1990. Since that time it has been object of studies aimed to characterize its function and to define the molecular determinants of the translocation pathway. Thanks to these tenacious studies the molecular map of the amino acids involved in the catalysis has been constructed and the roles of critical residues in the translocation pathway have been elucidated. This has been possible through the combination of transport assay in reconstituted liposomes, site-directed mutagenesis, chemical labeling and bioinformatics. Recently some molecules which modulate CACT activity have been identified, such as glutathione and hydrogen peroxide, constituting some of the few cases of control mechanisms of mitochondrial carriers. The vast knowledge on the carnitine/acylcarnitine translocase is essential both as a progress in basic science and as instrument to foresee therapeutic or toxic effects of xenobiotics and drugs. Such studies have been already started pointing out the inhibitory action of drugs such as K(+)/H(+)-ATPase inhibitors (omeprazole) or antibiotics (ß-lactams) on the carnitine/acylcarnitine translocase, which can explain some of their adverse effects.
[Mh] Termos MeSH primário: Carnitina Aciltransferases/química
Mitocôndrias/enzimologia
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Animais
Antibacterianos/efeitos adversos
Antibacterianos/uso terapêutico
Infecções Bacterianas/tratamento farmacológico
Encefalopatias/etiologia
Doenças Cardiovasculares/etiologia
Carnitina/metabolismo
Carnitina Aciltransferases/genética
Carnitina Aciltransferases/metabolismo
Biologia Computacional
Cisteína/química
Cisteína/metabolismo
Doenças do Sistema Digestório/etiologia
Gastroenteropatias/tratamento farmacológico
Seres Humanos
Peróxido de Hidrogênio/toxicidade
Mitocôndrias/metabolismo
Dados de Sequência Molecular
Mutagênese Sítio-Dirigida
Estresse Oxidativo/efeitos dos fármacos
Inibidores da Bomba de Prótons/efeitos adversos
Inibidores da Bomba de Prótons/uso terapêutico
Síndrome do Desconforto Respiratório do Adulto/etiologia
Alinhamento de Sequência
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Anti-Bacterial Agents); 0 (Proton Pump Inhibitors); BBX060AN9V (Hydrogen Peroxide); EC 2.3.1.- (Carnitine Acyltransferases); K848JZ4886 (Cysteine); S7UI8SM58A (Carnitine)
[Em] Mês de entrada:1601
[Cu] Atualização por classe:150427
[Lr] Data última revisão:
150427
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150426
[St] Status:MEDLINE



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