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Pesquisa : D02.092.570.050 [Categoria DeCS]
Referências encontradas : 823 [refinar]
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[PMID]:28259988
[Au] Autor:Sato M; Kawana K; Adachi K; Fujimoto A; Yoshida M; Nakamura H; Nishida H; Inoue T; Taguchi A; Ogishima J; Eguchi S; Yamashita A; Tomio K; Wada-Hiraike O; Oda K; Nagamatsu T; Osuga Y; Fujii T
[Ad] Endereço:Department of Obstetrics and Gynecology, Graduate School of Medicine, The University of Tokyo, Bunkyo-ku, Tokyo 113-8655, Japan.
[Ti] Título:Targeting glutamine metabolism and the focal adhesion kinase additively inhibits the mammalian target of the rapamycin pathway in spheroid cancer stem-like properties of ovarian clear cell carcinoma in vitro.
[So] Source:Int J Oncol;50(4):1431-1438, 2017 Apr.
[Is] ISSN:1791-2423
[Cp] País de publicação:Greece
[La] Idioma:eng
[Ab] Resumo:Ovarian cancer is one of the leading causes of death in the world, which is linked to its resistance to chemotherapy. Strategies to overcome chemoresistance have been keenly investigated. Culturing cancer cells in suspension, which results in formation of spheroids, is a more accurate reflection of clinical cancer behavior in vitro than conventional adherent cultures. By performing RNA-seq analysis, we found that the focal adhesion pathway was essential in spheroids. The phosphorylation of focal adhesion kinase (FAK) was increased in spheroids compared to adherent cells, and inhibition of FAK in spheroids resulted in inhibition of the downstream mammalian target of the rapamycin (mTOR) pathway in ovarian clear cell carcinomas. This result also suggested that only using a FAK inhibitor might have limitations because the phosphorylation level of FAK could not be reduced to the level in adherent cells, and it appeared that some combination therapies might be necessary. We previously reported that glutamine and glutamate concentrations were higher in spheroids than adherent cells, and we investigated a synergistic effect targeting glutamine metabolism with FAK inhibition on the mTOR pathway. The combination of AOA, a pan-transaminase inhibitor, and PF 573228, a FAK inhibitor, additively inhibited the mTOR pathway in spheroids from ovarian clear cell carcinomas. Our in vitro study proposed a rationale for the positive and negative effects of using FAK inhibitors in ovarian clear cell carcinomas and suggested that targeting glutamine metabolism could overcome the limitation of FAK inhibitors by additively inhibiting the mTOR pathway.
[Mh] Termos MeSH primário: Adenocarcinoma de Células Claras/tratamento farmacológico
Inibidores Enzimáticos/uso terapêutico
Quinase 1 de Adesão Focal/metabolismo
Glutamina/metabolismo
Neoplasias Ovarianas/tratamento farmacológico
Transdução de Sinais/efeitos dos fármacos
Serina-Treonina Quinases TOR/metabolismo
[Mh] Termos MeSH secundário: Ácido Amino-Oxiacético/uso terapêutico
Técnicas de Cultura de Células/métodos
Linhagem Celular Tumoral
Resistência a Medicamentos Antineoplásicos/efeitos dos fármacos
Quimioterapia Combinada
Feminino
Quinase 1 de Adesão Focal/antagonistas & inibidores
Seres Humanos
Fosforilação
Quinolonas/uso terapêutico
RNA Mensageiro/genética
Análise de Sequência de RNA
Esferoides Celulares
Sulfonas/uso terapêutico
Transaminases/antagonistas & inibidores
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (6-(4-(3-(methylsulfonyl)benzylamino)-5-(trifluoromethyl)pyrimidin-2-ylamino)-3,4-dihydroquinolin-2(1H)-one); 0 (Enzyme Inhibitors); 0 (Quinolones); 0 (RNA, Messenger); 0 (Sulfones); 0RH81L854J (Glutamine); 14I68GI3OQ (Aminooxyacetic Acid); EC 2.6.1.- (Transaminases); EC 2.7.1.1 (MTOR protein, human); EC 2.7.1.1 (TOR Serine-Threonine Kinases); EC 2.7.10.2 (Focal Adhesion Kinase 1); EC 2.7.10.2 (PTK2 protein, human)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:170717
[Lr] Data última revisão:
170717
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170306
[St] Status:MEDLINE
[do] DOI:10.3892/ijo.2017.3891


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[PMID]:28097769
[Au] Autor:Nadvi NA; Salam NK; Park J; Akladios FN; Kapoor V; Collyer CA; Gorrell MD; Church WB
[Ad] Endereço:Group in Biomolecular Structure and Informatics, Faculty of Pharmacy, University of Sydney, Sydney, New South Wales, Australia.
[Ti] Título:High resolution crystal structures of human kynurenine aminotransferase-I bound to PLP cofactor, and in complex with aminooxyacetate.
[So] Source:Protein Sci;26(4):727-736, 2017 Apr.
[Is] ISSN:1469-896X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:In this study, we report two high-resolution structures of the pyridoxal 5' phosphate (PLP)-dependent enzyme kynurenine aminotransferase-I (KAT-I). One is the native structure with the cofactor in the PLP form bound to Lys247 with the highest resolution yet available for KAT-I at 1.28 Å resolution, and the other with the general PLP-dependent aminotransferase inhibitor, aminooxyacetate (AOAA) covalently bound to the cofactor at 1.54 Å. Only small conformational differences are observed in the vicinity of the aldimine (oxime) linkage with which the PLP forms the Schiff base with Lys247 in the 1.28 Å resolution native structure, in comparison to other native PLP-bound structures. We also report the inhibition of KAT-1 by AOAA and aminooxy-phenylpropionic acid (AOPP), with IC50s of 13.1 and 5.7 µM, respectively. The crystal structure of the enzyme in complex with the inhibitor AOAA revealed that the cofactor is the PLP form with the external aldimine linkage. The location of this oxime with the PLP, which forms in place of the native internal aldimine linkage of PLP of the native KAT-I, is away from the position of the native internal aldimine, with the free Lys247 substantially retaining the orientation of the native structure. Tyr101, at the active site, was observed in two conformations in both structures.
[Mh] Termos MeSH primário: Ácido Amino-Oxiacético/química
Fosfato de Piridoxal/química
Transaminases/antagonistas & inibidores
Transaminases/química
[Mh] Termos MeSH secundário: Cristalografia por Raios X
Seres Humanos
Domínios Proteicos
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
14I68GI3OQ (Aminooxyacetic Acid); 5V5IOJ8338 (Pyridoxal Phosphate); EC 2.6.1.- (Transaminases); EC 2.6.1.7 (kynurenine-oxoglutarate transaminase)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:170717
[Lr] Data última revisão:
170717
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170119
[St] Status:MEDLINE
[do] DOI:10.1002/pro.3119


  3 / 823 MEDLINE  
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Coimbra, Terezila M
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[PMID]:27901369
[Au] Autor:Sabino JP; Soriano RN; Donatti AF; Fernandez RR; Kwiatkoski M; Francescato HD; Coimbra TM; Branco LG
[Ad] Endereço:a Dental School of Ribeirão Preto, 14040-904, University of São Paulo, Ribeirão Preto, SP, Brazil.
[Ti] Título:Involvement of endogenous central hydrogen sulfide (H S) in hypoxia-induced hypothermia in spontaneously hypertensive rats.
[So] Source:Can J Physiol Pharmacol;95(2):157-162, 2017 Feb.
[Is] ISSN:1205-7541
[Cp] País de publicação:Canada
[La] Idioma:eng
[Ab] Resumo:Spontaneously hypertensive rats (SHR) display autonomic imbalance and abnormal body temperature (Tb) adjustments. Hydrogen sulfide (H S) modulates hypoxia-induced hypothermia, but its role in SHR thermoregulation is unknown. We tested the hypothesis that SHR display peculiar thermoregulatory response to hypoxia and that endogenous H S overproduced in the caudal nucleus of the solitary tract (NTS) of SHR modulates this response. SHR and Wistar rats were microinjected into the fourth ventricle with aminooxyacetate (AOA, H S-synthezing enzyme inhibitor) or sodium sulfide (Na S, H S donor) and exposed to normoxia (21% inspired O ) or hypoxia (10% inspired O , 30 min). Tb was continuously measured, and H S production rate was assessed in caudal NTS homogenates. In both groups, AOA, Na S, or saline (i.e., control; 1 µL) did not affect euthermia. Hypoxia caused similar decreases in Tb in both groups. AOA presented a longer latency to potentiate hypoxic hypothermia in SHR. Caudal NTS H S production rate was higher in SHR. We suggest that increased bioavailability of H S in the caudal NTS of SHR enables the adequate modulation of excitability of peripheral chemoreceptor-activated NTS neurons that ultimately induce suppression of brown adipose tissue thermogenesis, thus accounting for the normal hypoxic hypothermia.
[Mh] Termos MeSH primário: Regulação da Temperatura Corporal
Sulfeto de Hidrogênio/metabolismo
Hipotermia Induzida
Hipóxia/fisiopatologia
[Mh] Termos MeSH secundário: Ácido Amino-Oxiacético/administração & dosagem
Ácido Amino-Oxiacético/farmacologia
Animais
Temperatura Corporal/efeitos dos fármacos
Hipóxia/complicações
Masculino
Microinjeções
Ratos
Ratos Endogâmicos SHR
Núcleo Solitário/metabolismo
Núcleo Solitário/fisiopatologia
Sulfetos/administração & dosagem
Sulfetos/farmacologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Sulfides); 14I68GI3OQ (Aminooxyacetic Acid); YGR27ZW0Y7 (sodium sulfide); YY9FVM7NSN (Hydrogen Sulfide)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161201
[St] Status:MEDLINE
[do] DOI:10.1139/cjpp-2016-0033


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[PMID]:27538376
[Au] Autor:Moreno-Sánchez R; Marín-Hernández Á; Del Mazo-Monsalvo I; Saavedra E; Rodríguez-Enríquez S
[Ad] Endereço:Instituto Nacional de Cardiología, Departamento de Bioquímica, Tlalpan D.F. 14080, Mexico. Electronic address: rafael.moreno@cardiologia.org.mx.
[Ti] Título:Assessment of the low inhibitory specificity of oxamate, aminooxyacetate and dichloroacetate on cancer energy metabolism.
[So] Source:Biochim Biophys Acta;1861(1 Pt A):3221-3236, 2017 01.
[Is] ISSN:0006-3002
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: Exceedingly high therapeutic/experimental doses of metabolic drugs such as oxamate, aminooxyacetate (AOA) and dichloroacetate (DCA) are required to diminish growth, glycolysis and oxidative phosphorylation (OxPhos) of different cancer cells. To identify the mechanisms of action of these drugs on cancer energy metabolism, a systematic analysis of their specificities was undertaken. METHODS: Hepatocarcinoma AS-30D cells were treated with the inhibitors and glycolysis and OxPhos enzyme activities, metabolites and fluxes were analyzed. Kinetic modeling of glycolysis was used to identify the regulatory mechanisms. RESULTS: Oxamate (i) not only inhibited LDH, but also PYK and ENO activities inducing an increase in the cytosolic NAD(P)H, Fru1,6BP and DHAP levels in AS-30D cells; (ii) it slightly inhibited HPI, ALD and Glc6PDH; and (iii) it inhibited pyruvate-driven OxPhos in isolated heart mitochondria. AOA (i) strongly inhibited both AAT and AlaT, and 2-OGDH and glutamate-driven OxPhos; and (ii) moderately affected GAPDH and TPI. DCA slightly affected pyruvate-driven OxPhos and Glc6PDH. Kinetic modeling of cancer glycolysis revealed that oxamate inhibition of LDH, PYK and ENO was insufficient to achieve glycolysis flux inhibition. To do so, HK, HPI, TPI and GAPDH have to be also inhibited by the accumulated Fru1,6BP and DHAP induced by oxamate. CONCLUSION: Oxamate, AOA, and DCA are not specific drugs since they inhibit several enzymes/transporters of the glycolytic and OxPhos pathways through direct interaction or indirect mechanisms. GENERAL SIGNIFICANCE: These data explain why oxamate or AOA, through their multisite inhibitory actions on glycolysis or OxPhos, may be able to decrease the proliferation of cancer cells.
[Mh] Termos MeSH primário: Ácido Amino-Oxiacético/farmacologia
Ácido Dicloroacético/farmacologia
Metabolismo Energético/efeitos dos fármacos
Neoplasias/metabolismo
Ácido Oxâmico/farmacologia
[Mh] Termos MeSH secundário: Animais
Antineoplásicos/farmacologia
Linhagem Celular Tumoral
Simulação por Computador
Fosfato de Di-Hidroxiacetona/farmacologia
Inibidores Enzimáticos/farmacologia
Feminino
Glicólise/efeitos dos fármacos
Seres Humanos
Cinética
Camundongos
Mitocôndrias Cardíacas/efeitos dos fármacos
Mitocôndrias Cardíacas/metabolismo
Modelos Moleculares
NADP/metabolismo
Fosforilação Oxidativa/efeitos dos fármacos
Ratos Wistar
Sus scrofa
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Antineoplastic Agents); 0 (Enzyme Inhibitors); 14I68GI3OQ (Aminooxyacetic Acid); 53-59-8 (NADP); 57-04-5 (Dihydroxyacetone Phosphate); 9LSH52S3LQ (Dichloroacetic Acid); QU60N5OPLG (Oxamic Acid)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171103
[Lr] Data última revisão:
171103
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160820
[St] Status:MEDLINE


  5 / 823 MEDLINE  
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Coimbra, Terezila M
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[PMID]:27592137
[Au] Autor:Fernández RA; Soriano RN; Francescato HD; Sabino JP; Coimbra TM; Branco LG
[Ad] Endereço:Medical School of Ribeirão Preto, University of São Paulo, 14049-900 Ribeirão Preto, São Paulo, Brazil.
[Ti] Título:Cryogenic role of central endogenous hydrogen sulfide in the rat model of endotoxic shock.
[So] Source:Brain Res;1650:218-223, 2016 Nov 01.
[Is] ISSN:1872-6240
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Thermoregulatory responses to lipopolysaccharide (LPS) are affected by modulators that increase (propyretic) or decrease (cryogenic) body temperature (Tb). We tested the hypothesis that central hydrogen sulfide (H S) acts as a thermoregulatory modulator and that H S production in the anteroventral preoptic region of the hypothalamus (AVPO) is increased during hypothermia and decreased during fever induced by bacterial lipopolysaccharide (LPS, 2.5mg/kg i.p.) in rats kept at an ambient temperature of 25°C. Deep Tb was recorded before and after pharmacological inhibition of the enzyme cystathionine ß-synthase (CBS - responsible for H S endogenous production in the brain) combined or not with LPS administration. To further investigate the mechanisms responsible for these thermoregulatory adjustments, we also measured prostaglandin D (PGD ) production in the AVPO. LPS caused typical hypothermia followed by fever. Levels of AVPO H S were significantly increased during hypothermia when compared to both euthermic and febrile rats. Intracerebroventricular (icv) microinjection of aminooxyacetate (AOA, a CBS inhibitor; 100 pmol) neither affected Tb nor basal PGD production during euthermia. In LPS-treated rats, AOA caused increased Tb values during hypothermia, along with enhanced PGD production. We conclude that the gaseous messenger H S modulates hypothermia during endotoxic shock, acting as a cryogenic molecule.
[Mh] Termos MeSH primário: Temperatura Corporal/efeitos dos fármacos
Sulfeto de Hidrogênio/farmacologia
Choque Séptico/fisiopatologia
[Mh] Termos MeSH secundário: Ácido Amino-Oxiacético
Animais
Regulação da Temperatura Corporal/fisiologia
Cistationina beta-Sintase/metabolismo
Febre/induzido quimicamente
Hipotálamo/metabolismo
Hipotermia/fisiopatologia
Hipóxia
Lipopolissacarídeos
Masculino
Microinjeções
Área Pré-Óptica/metabolismo
Ratos
Ratos Wistar
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Lipopolysaccharides); 14I68GI3OQ (Aminooxyacetic Acid); EC 4.2.1.22 (Cystathionine beta-Synthase); YY9FVM7NSN (Hydrogen Sulfide)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170821
[Lr] Data última revisão:
170821
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160905
[St] Status:MEDLINE


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[PMID]:27157912
[Au] Autor:Wang C; Chen H; Zhang M; Zhang J; Wei X; Ying W
[Ad] Endereço:Med-X Research Institute and School of Biomedical Engineering, Shanghai Jiao Tong University, Shanghai 200030, China.
[Ti] Título:Malate-aspartate shuttle inhibitor aminooxyacetic acid leads to decreased intracellular ATP levels and altered cell cycle of C6 glioma cells by inhibiting glycolysis.
[So] Source:Cancer Lett;378(1):1-7, 2016 08 01.
[Is] ISSN:1872-7980
[Cp] País de publicação:Ireland
[La] Idioma:eng
[Ab] Resumo:NADH shuttles, including malate-aspartate shuttle (MAS) and glycerol-3-phosphate shuttle, can shuttle the reducing equivalents of cytosolic NADH into mitochondria. It is widely accepted that the major function of NADH shuttles is to increase mitochondrial energy production. Our study tested the hypothesis that the novel major function of NADH shuttles in cancer cells is to maintain glycolysis by decreasing cytosolic NADH/NAD(+) ratios. We found that AOAA, a widely used MAS inhibitor, led to decreased intracellular ATP levels, altered cell cycle and increased apoptosis and necrosis of C6 glioma cells, without affecting the survival of primary astrocyte cultures. AOAA also decreased the glycolytic rate and the levels of extracellular lactate and pyruvate, without affecting the mitochondrial membrane potential of C6 cells. Moreover, the toxic effects of AOAA were completely prevented by pyruvate treatment. Collectively, our study has suggested that AOAA may be used to selectively decrease glioma cell survival, and the major function of MAS in cancer cells may be profoundly different from its major function in normal cells: The major function of MAS in cancer cells is to maintain glycolysis, instead of increasing mitochondrial energy metabolism.
[Mh] Termos MeSH primário: Trifosfato de Adenosina/metabolismo
Ácido Amino-Oxiacético/farmacologia
Antineoplásicos/farmacologia
Ácido Aspártico/metabolismo
Pontos de Checagem da Fase G1 do Ciclo Celular/efeitos dos fármacos
Glioma/tratamento farmacológico
Glicólise/efeitos dos fármacos
Malatos/metabolismo
Moduladores de Transporte de Membrana/farmacologia
Proteínas de Membrana Transportadoras/efeitos dos fármacos
[Mh] Termos MeSH secundário: Animais
Apoptose/efeitos dos fármacos
Astrócitos/efeitos dos fármacos
Astrócitos/metabolismo
Transporte Biológico
Linhagem Celular Tumoral
Relação Dose-Resposta a Droga
Regulação para Baixo
Glioma/metabolismo
Glioma/patologia
Proteínas de Membrana Transportadoras/metabolismo
Necrose
Cultura Primária de Células
Ratos
Transdução de Sinais/efeitos dos fármacos
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Antineoplastic Agents); 0 (Malates); 0 (Membrane Transport Modulators); 0 (Membrane Transport Proteins); 14I68GI3OQ (Aminooxyacetic Acid); 30KYC7MIAI (Aspartic Acid); 817L1N4CKP (malic acid); 8L70Q75FXE (Adenosine Triphosphate)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:171028
[Lr] Data última revisão:
171028
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160510
[St] Status:MEDLINE


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[PMID]:27062388
[Au] Autor:Blancquaert L; Baba SP; Kwiatkowski S; Stautemas J; Stegen S; Barbaresi S; Chung W; Boakye AA; Hoetker JD; Bhatnagar A; Delanghe J; Vanheel B; Veiga-da-Cunha M; Derave W; Everaert I
[Ad] Endereço:Department of Movement and Sports Sciences, Ghent University, Ghent, Belgium.
[Ti] Título:Carnosine and anserine homeostasis in skeletal muscle and heart is controlled by ß-alanine transamination.
[So] Source:J Physiol;594(17):4849-63, 2016 Sep 01.
[Is] ISSN:1469-7793
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:KEY POINTS: Using recombinant DNA technology, the present study provides the first strong and direct evidence indicating that ß-alanine is an efficient substrate for the mammalian transaminating enzymes 4-aminobutyrate-2-oxoglutarate transaminase and alanine-glyoxylate transaminase. The concentration of carnosine and anserine in murine skeletal and heart muscle depends on circulating availability of ß-alanine, which is in turn controlled by degradation of ß-alanine in liver and kidney. Chronic oral ß-alanine supplementation is a popular ergogenic strategy in sports because it can increase the intracellular carnosine concentration and subsequently improve the performance of high-intensity exercises. The present study can partly explain why the ß-alanine supplementation protocol is so inefficient, by demonstrating that exogenous ß-alanine can be effectively routed toward oxidation. ABSTRACT: The metabolic fate of orally ingested ß-alanine is largely unknown. Chronic ß-alanine supplementation is becoming increasingly popular for improving high-intensity exercise performance because it is the rate-limiting precursor of the dipeptide carnosine (ß-alanyl-l-histidine) in muscle. However, only a small fraction (3-6%) of the ingested ß-alanine is used for carnosine synthesis. Thus, the present study aimed to investigate the putative contribution of two ß-alanine transamination enzymes, namely 4-aminobutyrate-2-oxoglutarate transaminase (GABA-T) and alanine-glyoxylate transaminase (AGXT2), to the homeostasis of carnosine and its methylated analogue anserine. We found that, when transfected into HEK293T cells, recombinant mouse and human GABA-T and AGXT2 are able to transaminate ß-alanine efficiently. The reaction catalysed by GABA-T is inhibited by vigabatrin, whereas both GABA-T and AGXT2 activity is inhibited by aminooxyacetic acid (AOA). Both GABA-T and AGXT2 are highly expressed in the mouse liver and kidney and the administration of the inhibitors effectively reduced their enzyme activity in liver (GABA-T for vigabatrin; GABA-T and AGXT2 for AOA). In vivo, injection of AOA in C57BL/6 mice placed on ß-alanine (0.1% w/v in drinking water) for 2 weeks lead to a 3-fold increase in circulating ß-alanine levels and to significantly higher levels of carnosine and anserine in skeletal muscle and heart. By contrast, specific inhibition of GABA-T by vigabatrin did not affect carnosine and anserine levels in either tissue. Collectively, these data demonstrate that homeostasis of carnosine and anserine in mammalian skeletal muscle and heart is controlled by circulating ß-alanine levels, which are suppressed by hepatic and renal ß-alanine transamination upon oral ß-alanine intake.
[Mh] Termos MeSH primário: Anserina/metabolismo
Carnosina/metabolismo
Músculo Esquelético/metabolismo
Miocárdio/metabolismo
Transaminases/metabolismo
beta-Alanina/metabolismo
[Mh] Termos MeSH secundário: Ácido Amino-Oxiacético/farmacologia
Animais
Encéfalo/metabolismo
Inibidores Enzimáticos/farmacologia
GABAérgicos/farmacologia
Células HEK293
Homeostase
Seres Humanos
Rim/metabolismo
Fígado/metabolismo
Masculino
Camundongos Endogâmicos C57BL
RNA Mensageiro/metabolismo
Transaminases/antagonistas & inibidores
Transaminases/genética
Vigabatrina/farmacologia
beta-Alanina/sangue
beta-Alanina/urina
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Enzyme Inhibitors); 0 (GABA Agents); 0 (RNA, Messenger); 11P2JDE17B (beta-Alanine); 14I68GI3OQ (Aminooxyacetic Acid); 8HO6PVN24W (Carnosine); EC 2.6.1.- (Transaminases); EC 2.6.1.44 (Alanine-glyoxylate transaminase); GR120KRT6K (Vigabatrin); HDQ4N37UGV (Anserine)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170902
[Lr] Data última revisão:
170902
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160411
[St] Status:MEDLINE
[do] DOI:10.1113/JP272050


  8 / 823 MEDLINE  
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[PMID]:26960402
[Au] Autor:Zhang YM; Liu ZH; Yang RJ; Li GL; Guo XL; Zhang HN; Zhang HM; Di R; Zhao QS; Zhang MC
[Ad] Endereço:Institute of Genetics and Physiology, Plant Genetic Engineering Center of Hebei Province, Hebei Academy of Agriculture and Forestry Sciences, Shijiazhuang, 050051, China.
[Ti] Título:Improvement of soybean transformation via Agrobacterium tumefaciens methods involving α-aminooxyacetic acid and sonication treatments enlightened by gene expression profile analysis.
[So] Source:Plant Cell Rep;35(6):1259-71, 2016 Jun.
[Is] ISSN:1432-203X
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:KEY MESSAGE: Antagonists and sonication treatment relieved the structural barriers of Agrobacterium entering into cells; hindered signal perception and transmission; alleviated defense responses and increased cell susceptibility to Agrobacterium infection. Soybean gene expression analysis was performed to elucidate the general response of soybean plant to Agrobacterium at an early stage of infection. Agrobacterium infection stimulated the PAMPs-triggered immunity (BRI1, BAK1, BZR1, FLS2 and EFR) and effector-triggered immunity (RPM1, RPS2, RPS5, RIN4, and PBS1); up-regulated the transcript factors (WRKY25, WRKY29, MEKK1P, MKK4/5P and MYC2) in MAPK pathway; strengthened the biosynthesis of flavonoid and isoflavonoid in the second metabolism; finally led to a fierce defense response of soybean to Agrobacterium infection and thereby lower transformation efficiency. To overcome it, antagonist α-aminooxyacetic acid (AOA) and sonication treatment along with Agrobacterium infection were applied. This novel method dramatically decreased the expression of genes coding for F3'H, HCT, ß-glucosidase and IF7GT, etc., which are important for isoflavone biosynthesis or the interconversion of aglycones and glycon; genes coding for peroxidase, FLS2, PBS1 and transcription factor MYC2, etc., which are important components in plant-pathogen interaction; and genes coding for GPAT and α-L-fucosidase, which are important in polyesters formation in cell membrane and the degradation of fucose-containing glycoproteins and glycolipids on the external surface of cell membrane, respectively. This analysis implied that AOA and sonication treatment not only relieved the structural membrane barriers of Agrobacterium entering into cells, but also hindered the perception of 'invasion' signal on cell membrane and intercellular signal transmission, thus effectively alleviated the defense responses and increased the cell susceptibility to Agrobacterium infection. All these factors benefit the transformation process; other measures should also be further explored to improve soybean transformation.
[Mh] Termos MeSH primário: Agrobacterium tumefaciens/patogenicidade
Tumores de Planta/microbiologia
Feijão de Soja/microbiologia
[Mh] Termos MeSH secundário: Ácido Amino-Oxiacético/farmacologia
Perfilação da Expressão Gênica
Regulação da Expressão Gênica de Plantas/efeitos dos fármacos
Regulação da Expressão Gênica de Plantas/fisiologia
Análise de Sequência de DNA
Sonicação
Feijão de Soja/genética
Feijão de Soja/fisiologia
Transformação Genética/efeitos dos fármacos
Transformação Genética/fisiologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
14I68GI3OQ (Aminooxyacetic Acid)
[Em] Mês de entrada:1703
[Cu] Atualização por classe:171004
[Lr] Data última revisão:
171004
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160311
[St] Status:MEDLINE
[do] DOI:10.1007/s00299-016-1958-2


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[PMID]:26593431
[Au] Autor:Dugbartey GJ; Talaei F; Houwertjes MC; Goris M; Epema AH; Bouma HR; Henning RH
[Ad] Endereço:Department of Clinical Pharmacy and Pharmacology, University of Groningen, University Medical Center Groningen, Groningen, The Netherlands.
[Ti] Título:Dopamine treatment attenuates acute kidney injury in a rat model of deep hypothermia and rewarming - The role of renal H2S-producing enzymes.
[So] Source:Eur J Pharmacol;769:225-33, 2015 Dec 15.
[Is] ISSN:1879-0712
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Hypothermia and rewarming produces organ injury through the production of reactive oxygen species. We previously found that dopamine prevents hypothermia and rewarming-induced apoptosis in cultured cells through increased expression of the H2S-producing enzyme cystathionine ß-Synthase (CBS). Here, we investigate whether dopamine protects the kidney in deep body cooling and explore the role of H2S-producing enzymes in an in vivo rat model of deep hypothermia and rewarming. In anesthetized Wistar rats, body temperature was decreased to 15°C for 3h, followed by rewarming for 1h. Rats (n≥5 per group) were treated throughout the procedure with vehicle or dopamine infusion, and in the presence or absence of a non-specific inhibitor of H2S-producing enzymes, amino-oxyacetic acid (AOAA). Kidney damage and renal expression of three H2S-producing enzymes (CBS, CSE and 3-MST) was quantified and serum H2S level measured. Hypothermia and rewarming induced renal damage, evidenced by increased serum creatinine, renal reactive oxygen species production, KIM-1 expression and influx of immune cells, which was accompanied by substantially lowered renal expression of CBS, CSE, and 3-MST and lowered serum H2S levels. Infusion of dopamine fully attenuated renal damage and maintained expression of H2S-producing enzymes, while normalizing serum H2S. AOAA further decreased the expression of H2S-producing enzymes and serum H2S level, and aggravated renal damage. Hence, dopamine preserves renal integrity during deep hypothermia and rewarming likely by maintaining the expression of renal H2S-producing enzymes and serum H2S.
[Mh] Termos MeSH primário: Dopamina/farmacologia
Sulfeto de Hidrogênio/metabolismo
Hipotermia/enzimologia
Rim/enzimologia
Rim/lesões
Reaquecimento/efeitos adversos
[Mh] Termos MeSH secundário: Ácido Amino-Oxiacético/farmacologia
Anestesia Geral
Animais
Inibidores Enzimáticos/farmacologia
Regulação Enzimológica da Expressão Gênica/efeitos dos fármacos
Hemodinâmica/efeitos dos fármacos
Sulfeto de Hidrogênio/sangue
Hipotermia/metabolismo
Hipotermia/patologia
Hipotermia/fisiopatologia
Rim/efeitos dos fármacos
Rim/fisiopatologia
Masculino
Ratos
Ratos Wistar
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Enzyme Inhibitors); 14I68GI3OQ (Aminooxyacetic Acid); VTD58H1Z2X (Dopamine); YY9FVM7NSN (Hydrogen Sulfide)
[Em] Mês de entrada:1609
[Cu] Atualização por classe:151215
[Lr] Data última revisão:
151215
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:151124
[St] Status:MEDLINE


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[PMID]:26476584
[Au] Autor:Hadadha M; Vakili A; Bandegi AR
[Ad] Endereço:Laboratory of Cerebrovascular Research, Research Center and Department of Physiology, School of Medicine, Semnan University of Medical Sciences, Semnan, Iran.
[Ti] Título:Effect of the Inhibition of Hydrogen Sulfide Synthesis on Ischemic Injury and Oxidative Stress Biomarkers in a Transient Model of Focal Cerebral Ischemia in Rats.
[So] Source:J Stroke Cerebrovasc Dis;24(12):2676-84, 2015 Dec.
[Is] ISSN:1532-8511
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:OBJECTIVE: Hydrogen sulfide (H2S) plays multiple roles in the function of the central nervous system in physiological and pathological conditions, such as cerebral ischemia. Recent studies have reported controversial results about the role of H2S in cerebral ischemia. The aim of this study was to evaluate the effects of amino-oxyacetic acid (AOAA), an inhibitor of H2S synthesis, on ischemic injury in an experimental model of stroke. METHODS: Using laser Doppler monitoring, cerebral ischemia was induced by transient middle cerebral artery occlusion (MCAO) for 1 hour in rats. AOAA (.025, .05, .1, and .5 mmol/kg intraperitoneally [i.p.]) was injected at the beginning of MCAO. Infarct volume, cerebral edema, and activity of antioxidant enzymes were measured using the standard methods 24 hours after ischemia. RESULTS: The administration of AOAA at doses .025, .05, and .1 mmol/kg significantly reduced the infarct volume (P < .001). Furthermore, .025 and .05 mmol/kg of AOAA significantly reduced brain edema and improved the neurological outcome (P < .001). The administration of AOAA did not significantly change the malondialdehyde content, activities of superoxide dismutase, or glutathione peroxidase antioxidant enzymes in the brain tissue (P > .05). CONCLUSION: The results showed that AOAA administered at a low dose has protective effects; however, at higher doses it did not exert any protective effect against cerebral ischemia and even worsened the ischemic injury. This finding suggests that H2S might be both beneficial and harmful in cerebral ischemic injury depending on its concentration in transient model of focal cerebral ischemia.
[Mh] Termos MeSH primário: Ácido Amino-Oxiacético/uso terapêutico
Isquemia Encefálica/terapia
Encéfalo/efeitos dos fármacos
Inibidores Enzimáticos/uso terapêutico
Sulfeto de Hidrogênio/metabolismo
Estresse Oxidativo/efeitos dos fármacos
[Mh] Termos MeSH secundário: Ácido Amino-Oxiacético/farmacologia
Animais
Biomarcadores/metabolismo
Encéfalo/metabolismo
Encéfalo/patologia
Isquemia Encefálica/metabolismo
Isquemia Encefálica/patologia
Modelos Animais de Doenças
Inibidores Enzimáticos/farmacologia
Glutationa Peroxidase/metabolismo
Masculino
Malondialdeído/metabolismo
Estresse Oxidativo/fisiologia
Ratos
Ratos Wistar
Superóxido Dismutase/metabolismo
Resultado do Tratamento
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Biomarkers); 0 (Enzyme Inhibitors); 14I68GI3OQ (Aminooxyacetic Acid); 4Y8F71G49Q (Malondialdehyde); EC 1.11.1.9 (Glutathione Peroxidase); EC 1.15.1.1 (Superoxide Dismutase); YY9FVM7NSN (Hydrogen Sulfide)
[Em] Mês de entrada:1610
[Cu] Atualização por classe:161230
[Lr] Data última revisão:
161230
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:151019
[St] Status:MEDLINE



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