Base de dados : MEDLINE
Pesquisa : D08.811.682.047.820.150.207 [Categoria DeCS]
Referências encontradas : 12 [refinar]
Mostrando: 1 .. 10   no formato [Detalhado]

página 1 de 2 ir para página        

  1 / 12 MEDLINE  
              next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28291236
[Au] Autor:Liu J; Ghaziani TT; Wolf JL
[Ad] Endereço:Department of Internal Medicine, Beth Israel Deaconess Medical Center, Boston, Massachusetts, USA.
[Ti] Título:Acute Fatty Liver Disease of Pregnancy: Updates in Pathogenesis, Diagnosis, and Management.
[So] Source:Am J Gastroenterol;112(6):838-846, 2017 Jun.
[Is] ISSN:1572-0241
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Acute fatty liver of pregnancy (AFLP) is an obstetric emergency characterized by maternal liver failure and may have complications for the mother and fetus, including death. This review examines recent literature on the epidemiology, pathogenesis, diagnosis, and treatment of acute fatty liver of pregnancy. Pathogenesis of this disease has been linked to defects in fatty acid metabolism during pregnancy, especially in the setting of fetal genetic defects in fatty acid oxidation. The value of screening all patients for these genetic defects remains to be determined. Distinguishing AFLP from other high-risk liver diseases of pregnancy that have overlap features, such as HELLP and preeclampsia, can be challenging. Although sensitive diagnostic tools such as the Swansea criteria have been developed, further work is needed to diagnose AFLP more quickly. Although survival rates have improved in the past 30 years, delay in diagnosis and treatment of AFLP has life-threatening consequences; an algorithmic approach to AFLP may be a valuable resource for clinicians. Future epidemiological and long-term studies will improve our prediction of women at risk for developing AFLP and determine the long-term consequences of this condition.
[Mh] Termos MeSH primário: 3-Hidroxiacil-CoA Desidrogenase/deficiência
Fígado Gorduroso/diagnóstico
Fígado Gorduroso/genética
Doenças Fetais/fisiopatologia
Complicações na Gravidez/diagnóstico
Complicações na Gravidez/genética
[Mh] Termos MeSH secundário: 3-Hidroxiacil-CoA Desidrogenase/genética
Doença Aguda
Diagnóstico Diferencial
Fígado Gorduroso/epidemiologia
Fígado Gorduroso/terapia
Feminino
Doenças Fetais/diagnóstico
Doenças Fetais/enzimologia
Seres Humanos
Falência Hepática Aguda/etiologia
Gravidez
Complicações na Gravidez/epidemiologia
Complicações na Gravidez/terapia
Fatores de Risco
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
EC 1.1.1.35 (3-Hydroxyacyl-CoA Dehydrogenase)
[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:170315
[St] Status:MEDLINE
[do] DOI:10.1038/ajg.2017.54


  2 / 12 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:26953163
[Au] Autor:Molven A; Hollister-Lock J; Hu J; Martinez R; Njølstad PR; Liew CW; Weir G; Kulkarni RN
[Ad] Endereço:Islet Cell and Regenerative Biology, Joslin Diabetes Center, Harvard Stem Cell Institute, Harvard Medical School, Boston, MA Gade Laboratory for Pathology, Department of Clinical Medicine, University of Bergen, Bergen, Norway KG Jebsen Center for Diabetes Research, Department of Clinical Science, Un
[Ti] Título:The Hypoglycemic Phenotype Is Islet Cell-Autonomous in Short-Chain Hydroxyacyl-CoA Dehydrogenase-Deficient Mice.
[So] Source:Diabetes;65(6):1672-8, 2016 Jun.
[Is] ISSN:1939-327X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Congenital hyperinsulinism of infancy (CHI) can be caused by inactivating mutations in the gene encoding short-chain 3-hydroxyacyl-CoA dehydrogenase (SCHAD), a ubiquitously expressed enzyme involved in fatty acid oxidation. The hypersecretion of insulin may be explained by a loss of interaction between SCHAD and glutamate dehydrogenase in the pancreatic ß-cells. However, there is also a general accumulation of metabolites specific for the enzymatic defect in affected individuals. It remains to be explored whether hypoglycemia in SCHAD CHI can be uncoupled from the systemic effect on fatty acid oxidation. We therefore transplanted islets from global SCHAD knockout (SCHADKO) mice into mice with streptozotocin-induced diabetes. After transplantation, SCHADKO islet recipients exhibited significantly lower random and fasting blood glucose compared with mice transplanted with normal islets or nondiabetic, nontransplanted controls. Furthermore, intraperitoneal glucose tolerance was improved in animals receiving SCHADKO islets compared with those receiving normal islets. Graft ß-cell proliferation and apoptosis rates were similar in the two transplantation groups. We conclude that hypoglycemia in SCHAD-CHI is islet cell-autonomous.
[Mh] Termos MeSH primário: 3-Hidroxiacil-CoA Desidrogenase/deficiência
Hiperinsulinismo Congênito/enzimologia
Hipoglicemia/enzimologia
Células Secretoras de Insulina/metabolismo
Fenótipo
[Mh] Termos MeSH secundário: Animais
Hiperinsulinismo Congênito/genética
Glutamato Desidrogenase/metabolismo
Hipoglicemia/genética
Insulina/secreção
Masculino
Camundongos
Camundongos Knockout
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Insulin); EC 1.1.1.35 (3-Hydroxyacyl-CoA Dehydrogenase); EC 1.4.1.2 (Glutamate Dehydrogenase)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:170601
[Lr] Data última revisão:
170601
[Sb] Subgrupo de revista:AIM; IM
[Da] Data de entrada para processamento:160309
[St] Status:MEDLINE
[do] DOI:10.2337/db15-1475


  3 / 12 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:26626913
[Au] Autor:Vigelsø A; Gram M; Wiuff C; Hansen CN; Prats C; Dela F; Helge JW
[Ad] Endereço:Xlab, Center for Healthy Aging, Department of Biomedical Sciences, Faculty of Health Sciences, University of Copenhagen, 2200, Copenhagen, Denmark. avhansen@sund.ku.dk.
[Ti] Título:Effects of immobilization and aerobic training on proteins related to intramuscular substrate storage and metabolism in young and older men.
[So] Source:Eur J Appl Physiol;116(3):481-94, 2016 Mar.
[Is] ISSN:1439-6327
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:PURPOSE: Aging and inactivity lead to skeletal muscle metabolic inflexibility, but the underlying molecular mechanisms are not entirely elucidated. Therefore, we investigated how muscle lipid and glycogen stores and major regulatory proteins were affected by short-term immobilization followed by aerobic training in young and older men. METHODS: 17 young (23 ± 1 years, 24 ± 1 kg m(-2), and 20 ± 2% body fat) and 15 older men (68 ± 1 years; 27 ± 1 kg m(-2), and 29 ± 2% body fat) underwent 2 weeks' one leg immobilization followed by 6 weeks' cycle training. Biopsies were obtained from m. vastus lateralis just before immobilization (at inclusion), after immobilization, and the after 6 weeks' training. The biopsies were analyzed for muscle substrates; muscle perilipin protein (PLIN), glycogen synthase (GS), synaptosomal-associated protein of 23 kDa (SNAP23) protein content, and muscle 3-hydroxyacyl-CoA dehydrogenase (HAD) activity RESULTS: The older men had higher intramuscular triglyceride (IMTG) (73 %) and Glycogen (16%) levels compared to the young men, and IMTG tended to increase with immobilization. PLIN2 and 3 protein content increased with immobilization in the older men only. The young men had higher GS (74%) protein compared to the older men. Immobilization decreased and training restored HAD activity, GS and SNAP23 protein content in young and older men. CONCLUSION: Evidence of age-related metabolic inflexibility is presented, seen as body fat and IMTG accumulation. The question arises as to whether IMTG accumulation in the older men is caused by or leading to the increase in PLIN2 and 3 protein content. Training decreased body fat and IMTG levels in both young and older men; hence, training should be prioritized to reduce the detrimental effect of aging on metabolism.
[Mh] Termos MeSH primário: Exercício
Glicogênio/metabolismo
Imobilização/efeitos adversos
Metabolismo dos Lipídeos
Proteínas Musculares/metabolismo
Músculo Esquelético/metabolismo
[Mh] Termos MeSH secundário: 3-Hidroxiacil-CoA Desidrogenase/metabolismo
Idoso
Proteínas de Transporte/metabolismo
Glicogênio Sintase/metabolismo
Seres Humanos
Masculino
Músculo Esquelético/crescimento & desenvolvimento
Perilipina-1
Fosfoproteínas/metabolismo
Proteínas Qb-SNARE/metabolismo
Proteínas Qc-SNARE/metabolismo
Adulto Jovem
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Carrier Proteins); 0 (Muscle Proteins); 0 (Perilipin-1); 0 (Phosphoproteins); 0 (Qb-SNARE Proteins); 0 (Qc-SNARE Proteins); 0 (SNAP23 protein, human); 9005-79-2 (Glycogen); EC 1.1.1.35 (3-Hydroxyacyl-CoA Dehydrogenase); EC 2.4.1.11 (Glycogen Synthase)
[Em] Mês de entrada:1611
[Cu] Atualização por classe:171005
[Lr] Data última revisão:
171005
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:151203
[St] Status:MEDLINE
[do] DOI:10.1007/s00421-015-3302-x


  4 / 12 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
[PMID]:26675572
[Au] Autor:Han Y; Yang Z; Ding X; Yu H; Yi Y
[Ad] Endereço:Department of Obstetrics and Gynecology, Peking University Third Hospital, Beijing 100191, China.
[Ti] Título:[Variation of long-chain 3-hydroxyacyl-CoA dehydrogenase DNA methylation in placenta of different preeclampsia-like mouse models].
[So] Source:Zhonghua Fu Chan Ke Za Zhi;50(10):740-6, 2015 Oct.
[Is] ISSN:0529-567X
[Cp] País de publicação:China
[La] Idioma:chi
[Ab] Resumo:OBJECTIVE: By detecting the variation of long-chain 3-hydroxyacyl-CoA dehydrogenase (LCHAD) DNA methylation in preeclampsia-like mouse models generated by different ways, to explore the roles of multifactor and multiple pathways in preeclampsia pathogenesis on molecular basis. METHODS: Established preeclampsia-like mouse models in different ways and divided into groups as follows: (1) Nw-nitro-L-arginine-methyl ester (L-NAME) group: wild-type pregnant mouse received subcutaneous injection of L-NAME; (2) lipopolysaccharide (LPS) group: wild-type pregnant mouse received intraperitoneal injection of LPS; (3) apolipoprotein C-III (ApoC3) group: ApoC3 transgenic pregnant mouse with dysregulated lipid metabolism received subcutaneous injection of L-NAME; (4) ß2 glycoprotein I (ß-2GPI) group: wild-type pregnant mouse received subcutaneous injection of ß-2GPI. According to the first injection time (on day 3, 11, 16 respectively), the L-NAME, LPS and ApoC3 groups were further subdivided into: pre-implantation (PI) experimental stage, early gestation (EG) experimental stage, and late gestation (LG) experimental stage. ß-2GPI group was only injected before implantation. LCHAD gene methylation levels in placental were detected in different experimental stage. Normal saline control groups were set within wild-type and ApoC3 transgenic pregnant mice simultaneously. RESULTS: (1) CG sites in LCHAD DNA: 45 CG sites were detected in the range of 728 bp before LCHAD gene transcription start site, the 5, 12, 13, 14, 15, 16, 19, 24, 25, 27, 28, 29, 30, 31, 32, 34, 35, 43 CG sites were complex sites which contained two or more CG sequences, others were single site which contained one CG sequence. The 3, 5, 6, 11, 13, 14, 18, 28 sites in L-NAME, LPS, ApoC3 and ß-2GPI groups showed different high levels of methylation; the 16, 25, 31, 42, 44 sites showed different low levels of methylation; other 32 sites were unmethylated. (2) Comparison of LCHAD gene methylation between different groups: the methylation levels of LCAHD gene at 3, 11, 13, 14, 18 sites in L-NAME, LPS, ApoC3 and ß-2GPI groups were significantly higher than those in the normal saline control group (P < 0.05); and the methylation levels of 42, 44 sites in these groups were significantly lower than those in the normal saline control group (P < 0.05). (3) Methylation of LCHAD gene at the same site between different experimental stages: ① The 3, 11, 18 sites of EG experimental stage was significantly lower than PI and LG experimental stage in L-NAME group (P < 0.05); the 3, 11, 18 sites of PI experimental stage was significantly lower than EG and LG experimental stage in LPS group (P < 0.05); these sites of PI experimental stage was significantly higher than EG and LG experimental stages in ApoC3 group (P < 0.05). ② The methylation of site 5 in L-NAME and LPS groups were significantly higher than that of the normal saline control group (P < 0.05), and the LG experimental stages were significantly higher than other stages, but in ApoC3 group, only PI and EG stages were significantly higher than the normal saline control group (P < 0.05). ③ At site 6 in L-NAME group which showed high methylation level was significantly higher than the same site in other groups which showed low methylation level (P < 0.05). ④ At 13, 14 sites, earlier preeclampsia onset caused a lower methylation level in L-NAME group, but PI experimental stage was significantly higher than EG and LG experimental stages in LPS group (P < 0.05), EG experimental stage was significantly higher than PI and LG experimental stages in ApoC3 group (P < 0.05). ⑤ At site 28, earlier preeclampsia onset caused a higher methylation level in L-NAME group, but PI experimental stage was significantly lower than EG and LG experimental stages in LPS group (P < 0.05), EG experimental stage was significantly higher than PI and LG experimental stages in ApoC3 group (P < 0.05). ⑥ The 16, 25, 31 sites in ApoC3 group were significantly higher than other groups (P < 0.05). ⑦ At site 42 in ß-2GPI group was unmethylated, but it in other groups showed low methylation level, the methylation level of site 42 in ß-2GPI group was significantly lower than that in other groups (P < 0.05). CONCLUSIONS: The methylation of 6 and 42 CG sites may be related to LCHAD gene expression in placenta of L-NAME and ß-2GPI induced preeclampsia-like models respectively; LCHAD gene expression and DNA methylation may not have obvious correlation in LPS and ApoC3 induced preeclampsia-like models. Differences exist in LCHAD DNA methylation in preeclampsia-like models generated by different ways, revealed a molecular basis to expand our understanding of the multi-factorial pathogenesis of preeclampsia.
[Mh] Termos MeSH primário: 3-Hidroxiacil-CoA Desidrogenases/deficiência
Arginina/análogos & derivados
Cardiomiopatias/genética
Metilação de DNA/genética
Erros Inatos do Metabolismo Lipídico/genética
3-Hidroxiacil-CoA Desidrogenase de Cadeia Longa/metabolismo
Miopatias Mitocondriais/genética
Doenças do Sistema Nervoso/genética
Pré-Eclâmpsia/metabolismo
Rabdomiólise/genética
[Mh] Termos MeSH secundário: 3-Hidroxiacil-CoA Desidrogenases/genética
3-Hidroxiacil-CoA Desidrogenase
Animais
Arginina/genética
Modelos Animais de Doenças
Ácidos Graxos
Feminino
Seres Humanos
Metabolismo dos Lipídeos
Camundongos
Proteína Mitocondrial Trifuncional/deficiência
Oxirredução
Estresse Oxidativo
Placenta
Pré-Eclâmpsia/genética
Gravidez
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Fatty Acids); 2577-94-8 (arginine methyl ester); 94ZLA3W45F (Arginine); EC 1.1.1.- (3-Hydroxyacyl CoA Dehydrogenases); EC 1.1.1.211 (Long-Chain-3-Hydroxyacyl-CoA Dehydrogenase); EC 1.1.1.35 (3-Hydroxyacyl-CoA Dehydrogenase); EC 2.3.1.16 (Mitochondrial Trifunctional Protein)
[Em] Mês de entrada:1603
[Cu] Atualização por classe:161126
[Lr] Data última revisão:
161126
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:151218
[St] Status:MEDLINE


  5 / 12 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:26007288
[Au] Autor:Crescenti A; del Bas JM; Arola-Arnal A; Oms-Oliu G; Arola L; Caimari A
[Ad] Endereço:Grup de Recerca en Nutrició i Salut (GRNS), Centre Tecnològic de Nutrició i Salut (CTNS), TECNIO, CEICS, Reus, Spain.
[Ti] Título:Grape seed procyanidins administered at physiological doses to rats during pregnancy and lactation promote lipid oxidation and up-regulate AMPK in the muscle of male offspring in adulthood.
[So] Source:J Nutr Biochem;26(9):912-20, 2015 Sep.
[Is] ISSN:1873-4847
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The aim of the present study was to test whether the administration of a grape seed procyanidin extract (GSPE) during pregnancy and lactation, at doses extrapolated to human consumption, programs male offspring toward improved metabolism in adulthood. For this purpose, female rats were fed a normal-fat diet (NFD) and treated with either GSPE (25 mg kg(-1) of body weight/day) or vehicle during gestation and lactation. The metabolic programming effects of GSPE were evaluated in the male offspring fed NFD from 30 to 170 days of life. No changes were observed in body weight, adiposity, circulating lipid profile and insulin sensitivity between the offspring of dams treated with GSPE (STD-GSPE group) and their counterparts (STD-veh). However, the STD-GSPE offspring had lower circulating levels of C-reactive protein and lower respiratory quotient values, shifting whole-body energy catabolism from carbohydrate to fat oxidation. Furthermore, the STD-GSPE animals also exhibited increased levels of total and phosphorylated AMP-activated protein kinase (AMPK) and an over-expression of the mRNA levels of key genes related to fatty acid uptake (Fatp1 and CD36) and ß-oxidation (pparα and had) in skeletal muscle. Our results indicate that GSPE programs healthy male offspring towards a better circulating inflammatory profile and greater lipid utilisation in adulthood. The metabolic programming effects of GSPE that are related to the enhancement of fatty acid oxidation in skeletal muscle seem to be mediated, at least in part, by AMPK. These findings could be of relevance in the prevention of pathologies associated to lifestyle and aging, such as obesity and insulin resistance.
[Mh] Termos MeSH primário: Proteínas Quinases Ativadas por AMP/metabolismo
Suplementos Nutricionais
Extrato de Sementes de Uva/administração & dosagem
Lactação/metabolismo
Metabolismo dos Lipídeos
Fenômenos Fisiológicos da Nutrição Materna
Músculo Esquelético/enzimologia
Proantocianidinas/administração & dosagem
[Mh] Termos MeSH secundário: 3-Hidroxiacil-CoA Desidrogenase/química
3-Hidroxiacil-CoA Desidrogenase/genética
3-Hidroxiacil-CoA Desidrogenase/metabolismo
Proteínas Quinases Ativadas por AMP/química
Proteínas Quinases Ativadas por AMP/genética
Animais
Antígenos CD36/química
Antígenos CD36/genética
Antígenos CD36/metabolismo
Indução Enzimática
Proteínas de Ligação a Ácido Graxo/agonistas
Proteínas de Ligação a Ácido Graxo/genética
Proteínas de Ligação a Ácido Graxo/metabolismo
Feminino
Desenvolvimento Fetal
Masculino
Músculo Esquelético/crescimento & desenvolvimento
Músculo Esquelético/metabolismo
PPAR alfa/agonistas
PPAR alfa/genética
PPAR alfa/metabolismo
Fosforilação
Gravidez
Processamento de Proteína Pós-Traducional
Ratos
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (CD36 Antigens); 0 (Cd36 protein, rat); 0 (Fatty Acid-Binding Proteins); 0 (Grape Seed Extract); 0 (Grape Seed Proanthocyanidins); 0 (PPAR alpha); 0 (Proanthocyanidins); 0 (Slc27a1 protein, rat); EC 1.1.1.35 (3-Hydroxyacyl-CoA Dehydrogenase); EC 2.7.11.31 (AMP-Activated Protein Kinases)
[Em] Mês de entrada:1605
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150527
[St] Status:MEDLINE


  6 / 12 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:25446130
[Au] Autor:Mugo AN; Kobayashi J; Mikami B; Yoshikane Y; Yagi T; Ohnishi K
[Ad] Endereço:Research Institute of Molecular Genetics, Kochi University, Nankoku, Kochi 783-8502, Japan.
[Ti] Título:Crystal structure of 5-formyl-3-hydroxy-2-methylpyridine 4-carboxylic acid 5-dehydrogenase, an NAD⁺-dependent dismutase from Mesorhizobium loti.
[So] Source:Biochem Biophys Res Commun;456(1):35-40, 2015 Jan 02.
[Is] ISSN:1090-2104
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:5-Formyl-3-hydroxy-2-methylpyridine 4-carboxylic acid 5-dehydrogenase (FHMPCDH) from Mesorhizobium loti is the fifth enzyme in degradation pathway I for pyridoxine. The enzyme catalyzes a dismutation reaction: the oxidation of 5-formyl-3-hydroxy-2-methylpyridine 4-carboxylic acid (FHMPC) to 3-hydroxy-2-methylpyridine 4,5-dicarboxylic acid with NAD(+) and reduction of FHMPC to 4-pyridoxic acid with NADH. FHMPCDH belongs to the l-3-hydroxyacyl-CoA dehydrogenase (HAD) family. The crystal structure was determined by molecular replacement and refined to a resolution of 1.55Å (R-factor of 16.4%, Rfree=19.4%). There were two monomers in the asymmetric unit. The overall structure of the monomer consisted of N- and C-terminal domains connected by a short linker loop. The monomer was similar to members of the HAD family (RMSD=1.9Å). The active site was located between the domains and highly conserved to that of human heart l-3-hydroxyacyl-CoA dehydrogenase (HhHAD). His-Glu catalytic dyad, a serine and two asparagine residues of HhHAD were conserved. Ser116, His137 and Glu149 in FHMPCDH are connected by a hydrogen bonding network forming a catalytic triad. The functions of the active site residues in the reaction mechanism are discussed.
[Mh] Termos MeSH primário: Oxirredutases do Álcool/química
Proteínas de Bactérias/química
Mesorhizobium/enzimologia
[Mh] Termos MeSH secundário: 3-Hidroxiacil-CoA Desidrogenase/química
Catálise
Domínio Catalítico
Sequência Conservada
Cristalografia por Raios X
Regulação Enzimológica da Expressão Gênica
Seres Humanos
Ligações de Hidrogênio
Modelos Moleculares
Miocárdio/enzimologia
NAD/química
Ligação Proteica
Estrutura Terciária de Proteína
Vitamina B 6/química
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Bacterial Proteins); 0U46U6E8UK (NAD); 8059-24-3 (Vitamin B 6); EC 1.1.- (Alcohol Oxidoreductases); EC 1.1.1.- (5-formyl-3-hydroxy-2-methylpyridine-4-carboxylic acid dehydrogenase); EC 1.1.1.35 (3-Hydroxyacyl-CoA Dehydrogenase)
[Em] Mês de entrada:1503
[Cu] Atualização por classe:141224
[Lr] Data última revisão:
141224
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:141203
[St] Status:MEDLINE


  7 / 12 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
PubMed Central Texto completo
Texto completo
[PMID]:25068317
[Au] Autor:Sun Z; Kang Y; Norris MH; Troyer RM; Son MS; Schweizer HP; Dow SW; Hoang TT
[Ad] Endereço:Department of Microbiology, University of Hawaii at Manoa, Honolulu, Hawaii, United States of America.
[Ti] Título:Blocking phosphatidylcholine utilization in Pseudomonas aeruginosa, via mutagenesis of fatty acid, glycerol and choline degradation pathways, confirms the importance of this nutrient source in vivo.
[So] Source:PLoS One;9(7):e103778, 2014.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Pseudomonas aeruginosa can grow to very high-cell-density (HCD) during infection of the cystic fibrosis (CF) lung. Phosphatidylcholine (PC), the major component of lung surfactant, has been hypothesized to support HCD growth of P. aeruginosa in vivo. The phosphorylcholine headgroup, a glycerol molecule, and two long-chain fatty acids (FAs) are released by enzymatic cleavage of PC by bacterial phospholipase C and lipases. Three different bacterial pathways, the choline, glycerol, and fatty acid degradation pathways, are then involved in the degradation of these PC components. Here, we identified five potential FA degradation (Fad) related fadBA-operons (fadBA1-5, each encoding 3-hydroxyacyl-CoA dehydrogenase and acyl-CoA thiolase). Through mutagenesis and growth analyses, we showed that three (fadBA145) of the five fadBA-operons are dominant in medium-chain and long-chain Fad. The triple fadBA145 mutant also showed reduced ability to degrade PC in vitro. We have previously shown that by partially blocking Fad, via mutagenesis of fadBA5 and fadDs, we could significantly reduce the ability of P. aeruginosa to replicate on FA and PC in vitro, as well as in the mouse lung. However, no studies have assessed the ability of mutants, defective in choline and/or glycerol degradation in conjunction with Fad, to grow on PC or in vivo. Hence, we constructed additional mutants (ΔfadBA145ΔglpD, ΔfadBA145ΔbetAB, and ΔfadBA145ΔbetABΔglpD) significantly defective in the ability to degrade FA, choline, and glycerol and, therefore, PC. The analysis of these mutants in the BALB/c mouse lung infection model showed significant inability to utilize PC in vitro, resulted in decreased replication fitness and competitiveness in vivo compared to the complement strain, although there was little to no variation in typical virulence factor production (e.g., hemolysin, lipase, and protease levels). This further supports the hypothesis that lung surfactant PC serves as an important nutrient for P. aeruginosa during CF lung infection.
[Mh] Termos MeSH primário: Colina/metabolismo
Ácidos Graxos/metabolismo
Glicerol/metabolismo
Fosfatidilcolinas/metabolismo
Pseudomonas aeruginosa/metabolismo
[Mh] Termos MeSH secundário: 3-Hidroxiacil-CoA Desidrogenase/genética
3-Hidroxiacil-CoA Desidrogenase/metabolismo
Sequência de Aminoácidos
Animais
Proteínas de Bactérias/genética
Proteínas de Bactérias/metabolismo
Fibrose Cística/metabolismo
Fibrose Cística/microbiologia
Interações Hospedeiro-Patógeno
Pulmão/metabolismo
Pulmão/microbiologia
Pulmão/patologia
Camundongos Endogâmicos BALB C
Dados de Sequência Molecular
Mutagênese
Mutação
Óperon
Infecções por Pseudomonas/metabolismo
Infecções por Pseudomonas/microbiologia
Pseudomonas aeruginosa/genética
Pseudomonas aeruginosa/fisiologia
Homologia de Sequência de Aminoácidos
Transdução de Sinais/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL
[Nm] Nome de substância:
0 (Bacterial Proteins); 0 (Fatty Acids); 0 (Phosphatidylcholines); EC 1.1.1.35 (3-Hydroxyacyl-CoA Dehydrogenase); N91BDP6H0X (Choline); PDC6A3C0OX (Glycerol)
[Em] Mês de entrada:1512
[Cu] Atualização por classe:170220
[Lr] Data última revisão:
170220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:140729
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0103778


  8 / 12 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:24925763
[Au] Autor:Kato G; Sakai T; Suzuki K; Sano N; Takano T; Matsuyama T; Nakayasu C
[Ad] Endereço:Tamaki Laboratory, National Research Institute of Aquaculture, Fisheries Research Agency, 224-1 Hiruta, Tamaki, Watarai, Mie 519-0423, Japan; The Japan Society for the Promotion of Science, 5-3-1 Kojimachi, Chiyoda-ku, Tokyo 102-0083, Japan.
[Ti] Título:Protective efficacies and immune responses induced by recombinant HCD, atpD and gdhA against bacterial cold-water disease in ayu (Plecoglossus altivelis).
[So] Source:Fish Shellfish Immunol;39(2):396-400, 2014 Aug.
[Is] ISSN:1095-9947
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Protective efficacies of three antigenic proteins (3-hydroxyacyl-CoA dehydrogenase (HCD), ATP synthase beta subunit (atpD), and glutamate dehydrogenase (gdhA)) against Flavobacterium psychrophilum were investigated in ayu (Plecoglossus altivelis). Recombinant proteins of HCD, atpD, and gdhA were expressed in Escherichia coli BL21 cells. Ayu were then vaccinated with inactivated cells via the intraperitoneal route. Compared with the empty BL21- and PBS-injected groups, the vaccinated group had a significantly longer survival time after challenge with F. psychrophilum. The antibody titers against each recombinant protein were significantly higher in serum from vaccinated fish, compared with serum from control fish. Results of indirect immunofluorescence assays using serum indicated that the HCD, atpD, and gdhA proteins are located on the surface of F. psychrophilum. These results suggest that these three surface proteins are protective antigens and are good candidates for development of vaccines against bacterial cold-water disease in ayu.
[Mh] Termos MeSH primário: Vacinas Bacterianas/farmacologia
Doenças dos Peixes/imunologia
Doenças dos Peixes/microbiologia
Doenças dos Peixes/prevenção & controle
Infecções por Flavobacteriaceae/veterinária
Flavobacterium/imunologia
Osmeriformes
[Mh] Termos MeSH secundário: 3-Hidroxiacil-CoA Desidrogenase
Animais
Vacinas Bacterianas/administração & dosagem
Western Blotting/veterinária
Clonagem Molecular
Primers do DNA/genética
Eletroforese em Gel de Poliacrilamida/veterinária
Ensaio de Imunoadsorção Enzimática/veterinária
Infecções por Flavobacteriaceae/imunologia
Infecções por Flavobacteriaceae/prevenção & controle
Flavobacterium/genética
Técnica Indireta de Fluorescência para Anticorpo/veterinária
Glutamato Desidrogenase/metabolismo
ATPases Mitocondriais Próton-Translocadoras/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Bacterial Vaccines); 0 (DNA Primers); EC 1.1.1.35 (3-Hydroxyacyl-CoA Dehydrogenase); EC 1.4.1.2 (Glutamate Dehydrogenase); EC 3.6.3.- (Mitochondrial Proton-Translocating ATPases)
[Em] Mês de entrada:1503
[Cu] Atualização por classe:140714
[Lr] Data última revisão:
140714
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:140614
[St] Status:MEDLINE


  9 / 12 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
PubMed Central Texto completo
Texto completo
[PMID]:24884439
[Au] Autor:Segawa T; Nomura KH; Villanueva SY; Saito M; Nomura K; Gloriani NG; Yoshida S
[Ad] Endereço:Department of Bacteriology, Graduate School of Medical Sciences, Kyushu University, Fukuoka 812-8582, Japan. tsegawa@bact.med.kyushu-u.ac.jp.
[Ti] Título:Identification of leptospiral 3-hydroxyacyl-CoA dehydrogenase released in the urine of infected hamsters.
[So] Source:BMC Microbiol;14:132, 2014 May 21.
[Is] ISSN:1471-2180
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: Leptospirosis is a global zoonosis caused by pathogenic Leptospira. The non-specific clinical signs and symptoms of leptospirosis lead to its misdiagnosis. To date, there is still no reliable rapid test kit that can accurately diagnose leptospirosis at bedside or in field. In this research, with the ultimate goal of formulating a rapid and accurate diagnostic tool for leptospirosis, we aimed to identify leptospiral proteins excreted in urine of infected hamsters, which are thought to mimic Weil's disease. RESULTS: Hamsters were subcutaneously infected with leptospires, and the general attributes of urine as well as the proteins excreted in it were examined. Some leptospiral proteins were found to be excreted in the urine from the early phase of infection. The most important finding of this study was the detection of the lipid-metabolizing enzyme, 3-hydroxyacyl-CoA dehydrogenase (HADH), before the onset of illness, when leptospires were not yet detected in the urine of infected hamsters. CONCLUSIONS: This is the first report on the detection of leptospiral HADH in the host urine, which may be a possible candidate leptospiral antigen that can be used in the early diagnosis of human and animal leptospirosis.
[Mh] Termos MeSH primário: 3-Hidroxiacil-CoA Desidrogenase/urina
Leptospira/enzimologia
Leptospirose/patologia
Urina/química
[Mh] Termos MeSH secundário: Animais
Cricetinae
Modelos Animais de Doenças
Feminino
Masculino
Mesocricetus
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
EC 1.1.1.35 (3-Hydroxyacyl-CoA Dehydrogenase)
[Em] Mês de entrada:1508
[Cu] Atualização por classe:170220
[Lr] Data última revisão:
170220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:140603
[St] Status:MEDLINE
[do] DOI:10.1186/1471-2180-14-132


  10 / 12 MEDLINE  
              first record previous record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:23512564
[Au] Autor:Bouwman FG; Wang P; van Baak M; Saris WH; Mariman EC
[Ad] Endereço:Department of Human Biology, NUTRIM School for Nutrition, Toxicology and Metabolism, Maastricht University Medical Centre, Maastricht, The Netherlands.
[Ti] Título:Increased ß-oxidation with improved glucose uptake capacity in adipose tissue from obese after weight loss and maintenance.
[So] Source:Obesity (Silver Spring);22(3):819-27, 2014 Mar.
[Is] ISSN:1930-739X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:OBJECTIVE: We investigated protein markers for pathways of the fatty acids (FAs) and glucose metabolism in human adipose tissue after a weight loss program by calorie restriction. METHODS: Overweight/obese subjects underwent an intervention of 5 weeks of a very low-calorie diet followed by a 3-week weight maintenance diet. Abdominal subcutaneous adipose tissue biopsies were sampled before and after the intervention. Seventeen target proteins as markers of metabolic pathways for the uptake and handling of FAs and glucose were quantified by Western blotting and 11 were retrieved from previous proteomics work. Correlation coefficients were calculated among changes of these proteins. RESULTS: Short-chain 3-hydroxyacyl-CoA dehydrogenase, catalase, fatty acid translocase, fatty acid transporter protein 3, adipose triglyceride lipase, fatty acid-binding protein 4, aldolase-C, tubulin-ß-5, and annexin A2 changed significantly, and lipoprotein lipase, perilipin 1, and hormone-sensitive lipase tended to change. On an average, increased glucose transporter type 4 translocation was observed, supported by a consistent increase of tyr-24 phosphorylated annexin A2. CONCLUSIONS: Our findings suggest that after weight loss by calorie restriction and a short period of maintenance, adipose tissue has an increased capacity for glucose uptake, and lipid mobilization and oxidation. Such metabolic profile may relate to the health benefit of weight loss.
[Mh] Termos MeSH primário: Tecido Adiposo/metabolismo
Restrição Calórica
Glucose/metabolismo
Obesidade/metabolismo
Sobrepeso/metabolismo
Perda de Peso
[Mh] Termos MeSH secundário: 3-Hidroxiacil-CoA Desidrogenase/metabolismo
Adulto
Anexina A2/metabolismo
Proteínas de Transporte/metabolismo
Catalase/metabolismo
Proteínas de Ligação a Ácido Graxo/metabolismo
Ácidos Graxos/metabolismo
Feminino
Frutose-Bifosfato Aldolase/metabolismo
Transportador de Glucose Tipo 4/metabolismo
Seres Humanos
Lipase/metabolismo
Metabolismo dos Lipídeos/fisiologia
Lipase Lipoproteica/metabolismo
Masculino
Meia-Idade
Obesidade/dietoterapia
Sobrepeso/dietoterapia
Oxirredução
Perilipina-1
Fosfoproteínas/metabolismo
Esterol Esterase/metabolismo
Tubulina (Proteína)/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (ANXA2 protein, human); 0 (Annexin A2); 0 (Carrier Proteins); 0 (FABP4 protein, human); 0 (Fatty Acid-Binding Proteins); 0 (Fatty Acids); 0 (Glucose Transporter Type 4); 0 (PLIN1 protein, human); 0 (Perilipin-1); 0 (Phosphoproteins); 0 (Tubulin); EC 1.1.1.35 (3-Hydroxyacyl-CoA Dehydrogenase); EC 1.11.1.6 (Catalase); EC 3.1.1.13 (Sterol Esterase); EC 3.1.1.3 (Lipase); EC 3.1.1.3 (PNPLA2 protein, human); EC 3.1.1.34 (Lipoprotein Lipase); EC 4.1.2.13 (Fructose-Bisphosphate Aldolase); IY9XDZ35W2 (Glucose)
[Em] Mês de entrada:1411
[Cu] Atualização por classe:161125
[Lr] Data última revisão:
161125
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:130321
[St] Status:MEDLINE
[do] DOI:10.1002/oby.20359



página 1 de 2 ir para página        
   


Refinar a pesquisa
  Base de dados : MEDLINE Formulário avançado   

    Pesquisar no campo  
1  
2
3
 
           



Search engine: iAH v2.6 powered by WWWISIS

BIREME/OPAS/OMS - Centro Latino-Americano e do Caribe de Informação em Ciências da Saúde