Base de dados : MEDLINE
Pesquisa : D03.383.725.676.925.750 [Categoria DeCS]
Referências encontradas : 568 [refinar]
Mostrando: 1 .. 10   no formato [Detalhado]

página 1 de 57 ir para página                         

  1 / 568 MEDLINE  
              next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28470825
[Au] Autor:Börner T; Rämisch S; Bartsch S; Vogel A; Adlercreutz P; Grey C
[Ad] Endereço:Department of Chemistry and Biotechnology, Institute of Materials Science, Nestlé Research Center, Route du Jorat 57, 1000, Lausanne 26, Switzerland.
[Ti] Título:Three in One: Temperature, Solvent and Catalytic Stability by Engineering the Cofactor-Binding Element of Amine Transaminase.
[So] Source:Chembiochem;18(15):1482-1486, 2017 08 04.
[Is] ISSN:1439-7633
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:Amine transaminase (ATA) catalyse enantioselectively the direct amination of ketones, but insufficient stability during catalysis limits their industrial applicability. Recently, we revealed that ATAs suffer from substrate-induced inactivation mechanism involving dissociation of the enzyme-cofactor intermediate. Here, we report on engineering the cofactor-ring-binding element, which also shapes the active-site entrance. Only two point mutations in this motif improved temperature and catalytic stability in both biphasic media and organic solvent. Thermodynamic analysis revealed a higher melting point for the enzyme-cofactor intermediate. The high cofactor affinity eliminates the need for pyridoxal 5'-phosphate supply, thus making large-scale reactions more cost effective. This is the first report on stabilising a tetrameric ATA by mutating a single structural element. As this structural "hotspot" is a common feature of other transaminases it could serve as a general engineering target.
[Mh] Termos MeSH primário: Transaminases/química
[Mh] Termos MeSH secundário: Sítios de Ligação
Dimetil Sulfóxido/química
Estabilidade Enzimática
Propilaminas/química
Engenharia de Proteínas
Estrutura Quaternária de Proteína
Fosfato de Piridoxal/química
Piridoxamina/análogos & derivados
Piridoxamina/química
Solventes/química
Temperatura Ambiente
Temperatura de Transição
Água/química
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Propylamines); 0 (Solvents); 059QF0KO0R (Water); 5V5IOJ8338 (Pyridoxal Phosphate); 6466NM3W93 (Pyridoxamine); EC 2.6.1.- (Transaminases); P8W26T4MTD (2-propylamine); QWW7V29814 (pyridoxamine phosphate); YOW8V9698H (Dimethyl Sulfoxide)
[Em] Mês de entrada:1712
[Cu] Atualização por classe:180122
[Lr] Data última revisão:
180122
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170505
[St] Status:MEDLINE
[do] DOI:10.1002/cbic.201700236


  2 / 568 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28816437
[Au] Autor:Mascarenhas R; Le HV; Clevenger KD; Lehrer HJ; Ringe D; Kelleher NL; Silverman RB; Liu D
[Ad] Endereço:Department of Chemistry and Biochemistry, Loyola University Chicago , Chicago, Illinois 60660, United States.
[Ti] Título:Selective Targeting by a Mechanism-Based Inactivator against Pyridoxal 5'-Phosphate-Dependent Enzymes: Mechanisms of Inactivation and Alternative Turnover.
[So] Source:Biochemistry;56(37):4951-4961, 2017 Sep 19.
[Is] ISSN:1520-4995
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Potent mechanism-based inactivators can be rationally designed against pyridoxal 5'-phosphate (PLP)-dependent drug targets, such as ornithine aminotransferase (OAT) or γ-aminobutyric acid aminotransferase (GABA-AT). An important challenge, however, is the lack of selectivity toward other PLP-dependent, off-target enzymes, because of similarities in mechanisms of all PLP-dependent aminotransferase reactions. On the basis of complex crystal structures, we investigate the inactivation mechanism of OAT, a hepatocellular carcinoma target, by (1R,3S,4S)-3-amino-4-fluorocyclopentane-1-carboxylic acid (FCP), a known inactivator of GABA-AT. A crystal structure of OAT and FCP showed the formation of a ternary adduct. This adduct can be rationalized as occurring via an enamine mechanism of inactivation, similar to that reported for GABA-AT. However, the crystal structure of an off-target, PLP-dependent enzyme, aspartate aminotransferase (Asp-AT), in complex with FCP, along with the results of attempted inhibition assays, suggests that FCP is not an inactivator of Asp-AT, but rather an alternate substrate. Turnover of FCP by Asp-AT is also supported by high-resolution mass spectrometry. Amid existing difficulties in achieving selectivity of inactivation among a large number of PLP-dependent enzymes, the obtained results provide evidence that a desirable selectivity could be achieved, taking advantage of subtle structural and mechanistic differences between a drug-target enzyme and an off-target enzyme, despite their largely similar substrate binding sites and catalytic mechanisms.
[Mh] Termos MeSH primário: 4-Aminobutirato Transaminase/antagonistas & inibidores
Aspartato Aminotransferases/antagonistas & inibidores
Cicloleucina/análogos & derivados
Inibidores Enzimáticos/farmacologia
Modelos Moleculares
Ornitina-Oxo-Ácido Transaminase/antagonistas & inibidores
Fosfato de Piridoxal/metabolismo
[Mh] Termos MeSH secundário: 4-Aminobutirato Transaminase/química
4-Aminobutirato Transaminase/metabolismo
Aspartato Aminotransferases/química
Aspartato Aminotransferases/genética
Aspartato Aminotransferases/metabolismo
Sítios de Ligação
Domínio Catalítico
Cristalografia por Raios X
Cicloleucina/química
Cicloleucina/metabolismo
Cicloleucina/farmacologia
Bases de Dados de Compostos Químicos
Bases de Dados de Proteínas
Inibidores Enzimáticos/química
Inibidores Enzimáticos/metabolismo
Proteínas de Escherichia coli/antagonistas & inibidores
Proteínas de Escherichia coli/química
Proteínas de Escherichia coli/genética
Proteínas de Escherichia coli/metabolismo
Seres Humanos
Ligantes
Conformação Molecular
Ornitina-Oxo-Ácido Transaminase/química
Ornitina-Oxo-Ácido Transaminase/genética
Ornitina-Oxo-Ácido Transaminase/metabolismo
Conformação Proteica
Fosfato de Piridoxal/química
Piridoxamina/química
Piridoxamina/metabolismo
Proteínas Recombinantes/química
Proteínas Recombinantes/metabolismo
Homologia Estrutural de Proteína
Especificidade por Substrato
[Pt] Tipo de publicação:COMPARATIVE STUDY; JOURNAL ARTICLE
[Nm] Nome de substância:
0 (3-amino-4-fluorocyclopentane-1-carboxylic acid); 0 (Enzyme Inhibitors); 0 (Escherichia coli Proteins); 0 (Ligands); 0 (Recombinant Proteins); 0TQU7668EI (Cycloleucine); 5V5IOJ8338 (Pyridoxal Phosphate); 6466NM3W93 (Pyridoxamine); EC 2.6.1.1 (Aspartate Aminotransferases); EC 2.6.1.13 (Ornithine-Oxo-Acid Transaminase); EC 2.6.1.19 (4-Aminobutyrate Transaminase)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171003
[Lr] Data última revisão:
171003
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170818
[St] Status:MEDLINE
[do] DOI:10.1021/acs.biochem.7b00499


  3 / 568 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28420530
[Au] Autor:Schmidt A; Schreiner MG; Mayer HK
[Ad] Endereço:Department of Food Science and Technology, Food Chemistry Laboratory, BOKU - University of Natural Resources and Life Sciences Vienna, Muthgasse 11, A-1190 Vienna, Austria.
[Ti] Título:Rapid determination of the various native forms of vitamin B and B in cow's milk using ultra-high performance liquid chromatography.
[So] Source:J Chromatogr A;1500:89-95, 2017 Jun 02.
[Is] ISSN:1873-3778
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:As the formation of pyridoxal phosphate, the active cofactor of vitamin B , is dependent on riboflavin 5-phosphate, we propose a fast and simple ultra-high performance liquid chromatography method for the simultaneous determination of the native B vitamers pyridoxal, pyridoxine, pyridoxamine, their mono phosphorus esters and 4-pyridoxic acid as well as vitamin B as riboflavin and its phosphorus ester riboflavin 5-phosphate in milk. Separation was achieved under 6.0min by reversed-phase and pH gradient elution. Sample preparation was optimized regarding various acids and pH levels. Changes in those parameters led to significant deviations of sample matrix breakdown efficiency. The optimized method was then validated regarding specificity, accuracy, precision, linearity, range, detection and quantification limits. As the method performed satisfactory, is was used to study commercial liquid cow's milk (n=31), regarding effects of the employed preservation technique (pasteurization, extended shelf-life, ultra-high temperature) on the composition and content of B and B vitamers. In cow's milk, vitamin B mostly consists of pyridoxal and its phosphate ester, with pyridoxal phosphate being the bulk component. The catabolite of the vitamin B metabolism, 4-pyridoxic acid was present in significant amounts in all studied samples, with up to 2.69µmolL . Vitamin B was present as riboflavin and its phosphate ester up to 12.86µmolL .
[Mh] Termos MeSH primário: Cromatografia Líquida de Alta Pressão/métodos
Leite/química
Riboflavina/análise
Vitamina B 6/análise
[Mh] Termos MeSH secundário: Animais
Bovinos
Seres Humanos
Piridoxal/análise
Fosfato de Piridoxal/análise
Piridoxamina/análise
[Pt] Tipo de publicação:EVALUATION STUDIES; JOURNAL ARTICLE
[Nm] Nome de substância:
3THM379K8A (Pyridoxal); 5V5IOJ8338 (Pyridoxal Phosphate); 6466NM3W93 (Pyridoxamine); 8059-24-3 (Vitamin B 6); TLM2976OFR (Riboflavin)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171113
[Lr] Data última revisão:
171113
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170420
[St] Status:MEDLINE


  4 / 568 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28359757
[Au] Autor:Dainin K; Ide R; Maeda A; Suyama K; Akagawa M
[Ad] Endereço:Department of Biological Chemistry, Division of Applied Life Science, Graduate School of Life and Environmental Sciences, Osaka Prefecture University, Sakai, Osaka 599-8531, Japan.
[Ti] Título:Pyridoxamine scavenges protein carbonyls and inhibits protein aggregation in oxidative stress-induced human HepG2 hepatocytes.
[So] Source:Biochem Biophys Res Commun;486(3):845-851, 2017 May 06.
[Is] ISSN:1090-2104
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Introduction of carbonyl groups into amino acid residues is a hallmark for oxidative damage to proteins by reactive oxygen species (ROS). Protein carbonylation can have deleterious effects on cell function and viability, since it is generally unrepairable by cells and can lead to protein dysfunction and to the production of potentially harmful protein aggregates. Meanwhile, pyridoxamine (PM) is known to scavenge various toxic carbonyl species derived from either glucose or lipid degradation through nucleophilic addition. PM is also demonstrated to catalyze non-enzymatic transamination reactions between amino and α-keto acids. Here, we found that PM scavenges protein carbonyls in oxidized BSA with concomitant generation of pyridoxal and recovers oxidized lysozyme activity. Moreover, we demonstrated that the treatment of H O -exposed HepG2 hepatocytes with PM significantly reduced levels of cellular carbonylated proteins and aggregated proteins, and also improved cell survival rate. Our results suggest that PM may have potential efficacy in ameliorating ROS-mediated cellular dysfunction.
[Mh] Termos MeSH primário: Antioxidantes/farmacologia
Peróxido de Hidrogênio/antagonistas & inibidores
Carbonilação Proteica/efeitos dos fármacos
Piridoxamina/farmacologia
Espécies Reativas de Oxigênio/antagonistas & inibidores
[Mh] Termos MeSH secundário: Células Hep G2
Seres Humanos
Peróxido de Hidrogênio/farmacologia
Muramidase/antagonistas & inibidores
Muramidase/metabolismo
Oxirredução/efeitos dos fármacos
Estresse Oxidativo/efeitos dos fármacos
Agregados Proteicos/efeitos dos fármacos
Espécies Reativas de Oxigênio/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antioxidants); 0 (Protein Aggregates); 0 (Reactive Oxygen Species); 6466NM3W93 (Pyridoxamine); BBX060AN9V (Hydrogen Peroxide); EC 3.2.1.17 (Muramidase)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:170602
[Lr] Data última revisão:
170602
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170401
[St] Status:MEDLINE


  5 / 568 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28042580
[Au] Autor:Abouzed TK; Munesue S; Harashima A; Masuo Y; Kato Y; Khailo K; Yamamoto H; Yamamoto Y
[Ad] Endereço:Department of Biochemistry and Molecular Vascular Biology, Kanazawa University Graduate School of Medical Sciences, 13-1 Takara-machi, Kanazawa 920-8640, Japan; Department of Biochemistry, Faculty of Veterinary Medicine, Kafrelsheikh University, Kafr El Sheikh 33516, Egypt.
[Ti] Título:Preventive Effect of Salicylate and Pyridoxamine on Diabetic Nephropathy.
[So] Source:J Diabetes Res;2016:1786789, 2016.
[Is] ISSN:2314-6753
[Cp] País de publicação:Egypt
[La] Idioma:eng
[Ab] Resumo:. Diabetic nephropathy is a life-threatening complication in patients with long-standing diabetes. Hemodynamic, inflammatory, and metabolic factors are considered as developmental factors for diabetic nephropathy. In this study, we evaluated whether pharmacological interventions with salicylate, compared to pyridoxamine, could prevent diabetic nephropathy in mice. . Male mice overexpressing inducible nitric oxide synthase in pancreatic -cells were employed as a diabetic model. Salicylate (3 g/kg diet) or pyridoxamine (1 g/L drinking water; ~200 mg/kg/day) was given for 16 weeks to assess the development of diabetic nephropathy. Treatment with long-acting insulin (Levemir 2 units/kg twice a day) was used as a control. . Although higher blood glucose levels were not significantly affected by pyridoxamine, early to late stage indices of nephropathy were attenuated, including kidney enlargement, albuminuria, and increased serum creatinine, glomerulosclerosis, and inflammatory and profibrotic gene expressions. Salicylate showed beneficial effects on diabetic nephropathy similar to those of pyridoxamine, which include lowering blood glucose levels and inhibiting macrophage infiltration into the kidneys. Attenuation of macrophage infiltration into the kidneys and upregulation of antiglycating enzyme gene expression were found only in the salicylate treatment group. . Treatment with salicylate and pyridoxamine could prevent the development of diabetic nephropathy in mice and, therefore, would be a potentially useful therapeutic strategy against kidney problems in patients with diabetes.
[Mh] Termos MeSH primário: Nefropatias Diabéticas/tratamento farmacológico
Nefropatias Diabéticas/prevenção & controle
Piridoxamina/uso terapêutico
Salicilatos/uso terapêutico
[Mh] Termos MeSH secundário: Albuminúria/etiologia
Animais
Anti-Inflamatórios não Esteroides/uso terapêutico
Glicemia/análise
Glicemia/metabolismo
Creatinina/sangue
Diabetes Mellitus Experimental/tratamento farmacológico
Diabetes Mellitus Experimental/metabolismo
Citometria de Fluxo
Hemodinâmica
Inflamação
Insulina de Ação Prolongada/farmacologia
Células Secretoras de Insulina/efeitos dos fármacos
Rim/metabolismo
Macrófagos/metabolismo
Masculino
Camundongos
Óxido Nítrico Sintase Tipo II/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Anti-Inflammatory Agents, Non-Steroidal); 0 (Blood Glucose); 0 (Insulin, Long-Acting); 0 (Salicylates); 6466NM3W93 (Pyridoxamine); AYI8EX34EU (Creatinine); EC 1.14.13.39 (Nitric Oxide Synthase Type II)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:170522
[Lr] Data última revisão:
170522
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170103
[St] Status:MEDLINE
[do] DOI:10.1155/2016/1786789


  6 / 568 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:27620210
[Au] Autor:Mori Y; Kakuta T; Miyakogawa T; Takekoshi S; Yuzawa H; Kobayashi H; Kawakami A; Miyata T; Fukagawa M
[Ad] Endereço:Department of Nephrology, Endocrinology and Metabolism, Tokai University School of Medicine, Isehara, Japan.
[Ti] Título:Effect of Scavenging Circulating Reactive Carbonyls by Oral Pyridoxamine in Uremic Rats on Peritoneal Dialysis.
[So] Source:Ther Apher Dial;20(6):645-654, 2016 Dec.
[Is] ISSN:1744-9987
[Cp] País de publicação:Australia
[La] Idioma:eng
[Ab] Resumo:Pyridoxamine, a reactive carbonyl (RCO) scavenger, can ameliorate peritoneal deterioration in uremic peritoneal dialysis (PD) rats when given via dialysate. We examined the effects of scavenging circulating RCOs by oral pyridoxamine. Rats underwent nephrectomy and 3 weeks of twice daily PD either alone or with once daily oral pyridoxamine. PD solution was supplemented with methylglyoxal, a major glucose-derived RCO, to quench intraperitoneal pyridoxamine. Oral pyridoxamine achieved comparable blood and dialysate pyridoxamine concentrations, suppressed pentosidine accumulation in the blood but not in the mesenterium or dialysate, and reduced the increases in small solute transport and mesenteric vessel densities, with no effects on submesothelial matrix layer thickening or serum creatinine. Thus, reducing circulating RCOs by giving oral pyridoxamine with PD provides limited peritoneal protection. However, orally given pyridoxamine efficiently reaches the peritoneal cavity and would eliminate intraperitoneal RCOs. Oral pyridoxamine is more clinically favorable and may be as protective as intraperitoneal administration.
[Mh] Termos MeSH primário: Soluções para Diálise/farmacologia
Falência Renal Crônica/terapia
Diálise Peritoneal
Piridoxamina/farmacologia
Uremia/terapia
Complexo Vitamínico B/farmacologia
[Mh] Termos MeSH secundário: Administração Oral
Animais
Modelos Animais de Doenças
Falência Renal Crônica/sangue
Masculino
Piridoxamina/sangue
Ratos
Ratos Sprague-Dawley
Uremia/sangue
Complexo Vitamínico B/sangue
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Dialysis Solutions); 12001-76-2 (Vitamin B Complex); 6466NM3W93 (Pyridoxamine)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171004
[Lr] Data última revisão:
171004
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160914
[St] Status:MEDLINE
[do] DOI:10.1111/1744-9987.12446


  7 / 568 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
PubMed Central Texto completo
Texto completo
[PMID]:27428057
[Au] Autor:Pereira-Simon S; Rubio GA; Xia X; Cai W; Choi R; Striker GE; Elliot SJ
[Ad] Endereço:Department of Surgery, University of Miami Miller School of Medicine, Miami, Florida, United States of America.
[Ti] Título:Inhibition of Advanced Glycation End Products (AGEs) Accumulation by Pyridoxamine Modulates Glomerular and Mesangial Cell Estrogen Receptor α Expression in Aged Female Mice.
[So] Source:PLoS One;11(7):e0159666, 2016.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Age-related increases in oxidant stress (OS) play a role in regulation of estrogen receptor (ER) expression in the kidneys. In this study, we establish that in vivo 17ß-estradiol (E2) replacement can no longer upregulate glomerular ER expression by 21 months of age in female mice (anestrous). We hypothesized that advanced glycation end product (AGE) accumulation, an important source of oxidant stress, contributes to these glomerular ER expression alterations. We treated 19-month old ovariectomized female mice with pyridoxamine (Pyr), a potent AGE inhibitor, in the presence or absence of E2 replacement. Glomerular ERα mRNA expression was upregulated in mice treated with both Pyr and E2 replacement and TGFß mRNA expression decreased compared to controls. Histological sections of kidneys demonstrated decreased type IV collagen deposition in mice receiving Pyr and E2 compared to placebo control mice. In addition, anti-AGE defenses Sirtuin1 (SIRT1) and advanced glycation receptor 1 (AGER1) were also upregulated in glomeruli following treatment with Pyr and E2. Mesangial cells isolated from all groups of mice demonstrated similar ERα, SIRT1, and AGER1 expression changes to those of whole glomeruli. To demonstrate that AGE accumulation contributes to the observed age-related changes in the glomeruli of aged female mice, we treated mesangial cells from young female mice with AGE-BSA and found similar downregulation of ERα, SIRT1, and AGER1 expression. These results suggest that inhibition of intracellular AGE accumulation with pyridoxamine may protect glomeruli against age-related oxidant stress by preventing an increase of TGFß production and by regulation of the estrogen receptor.
[Mh] Termos MeSH primário: Envelhecimento/metabolismo
Antioxidantes/farmacologia
Receptor alfa de Estrogênio/genética
Produtos Finais de Glicação Avançada/antagonistas & inibidores
Glomérulos Renais/efeitos dos fármacos
Piridoxamina/farmacologia
[Mh] Termos MeSH secundário: Envelhecimento/genética
Animais
Colágeno Tipo IV/genética
Colágeno Tipo IV/metabolismo
Estradiol/farmacologia
Receptor alfa de Estrogênio/agonistas
Receptor alfa de Estrogênio/metabolismo
Feminino
Regulação da Expressão Gênica
Produtos Finais de Glicação Avançada/genética
Produtos Finais de Glicação Avançada/metabolismo
Produtos Finais de Glicação Avançada/farmacologia
Terapia de Reposição Hormonal
Glomérulos Renais/metabolismo
Glomérulos Renais/patologia
Células Mesangiais/efeitos dos fármacos
Células Mesangiais/metabolismo
Células Mesangiais/patologia
Camundongos
Camundongos Endogâmicos C57BL
Ovariectomia
Estresse Oxidativo
Cultura Primária de Células
RNA Mensageiro/genética
RNA Mensageiro/metabolismo
Receptor para Produtos Finais de Glicação Avançada/genética
Receptor para Produtos Finais de Glicação Avançada/metabolismo
Soroalbumina Bovina/antagonistas & inibidores
Soroalbumina Bovina/farmacologia
Transdução de Sinais
Sirtuína 1/genética
Sirtuína 1/metabolismo
Fator de Crescimento Transformador beta/antagonistas & inibidores
Fator de Crescimento Transformador beta/genética
Fator de Crescimento Transformador beta/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Ager protein, mouse); 0 (Antioxidants); 0 (Collagen Type IV); 0 (Estrogen Receptor alpha); 0 (Glycation End Products, Advanced); 0 (RNA, Messenger); 0 (Receptor for Advanced Glycation End Products); 0 (Transforming Growth Factor beta); 0 (advanced glycation end products-bovine serum albumin); 27432CM55Q (Serum Albumin, Bovine); 4TI98Z838E (Estradiol); 6466NM3W93 (Pyridoxamine); EC 3.5.1.- (Sirt1 protein, mouse); EC 3.5.1.- (Sirtuin 1)
[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:160719
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0159666


  8 / 568 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:27302825
[Au] Autor:Assimos DG
[Ti] Título:Re: Pyridoxamine and Pyridoxal are More Effective than Pyridoxine in Rescuing Folding-Defective Variants of Human Alanine:Glyoxylate Aminotransferase Causing Primary Hyperoxaluria Type I.
[So] Source:J Urol;195(4 Pt 1):1170-1, 2016 04.
[Is] ISSN:1527-3792
[Cp] País de publicação:United States
[La] Idioma:eng
[Mh] Termos MeSH primário: Hiperoxalúria Primária
Piridoxamina
[Mh] Termos MeSH secundário: Alanina
Seres Humanos
Hiperoxalúria
Piridoxal
Piridoxina
[Pt] Tipo de publicação:JOURNAL ARTICLE; COMMENT
[Nm] Nome de substância:
3THM379K8A (Pyridoxal); 6466NM3W93 (Pyridoxamine); KV2JZ1BI6Z (Pyridoxine); OF5P57N2ZX (Alanine)
[Em] Mês de entrada:1612
[Cu] Atualização por classe:161230
[Lr] Data última revisão:
161230
[Sb] Subgrupo de revista:AIM; IM
[Da] Data de entrada para processamento:160616
[St] Status:MEDLINE


  9 / 568 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:27283678
[Au] Autor:Chen J; Cai D; Zhang Y
[Ad] Endereço:Zhejiang Key Laboratory for Agro-Food Processing, Zhejiang R & D Centre for Food Technology and Equipment, Fuli Institute of Food Science, Zhejiang University, 866 Yuhangtang Road, Hangzhou 310058, China.
[Ti] Título:Rapid determination of lipid peroxidation using a novel pyridoxamine-participating ferrous oxidation-sulfosalicylic acid spectrophotometric method.
[So] Source:Food Chem;211:637-44, 2016 Nov 15.
[Is] ISSN:0308-8146
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:A novel method is developed to rapidly analyze lipid peroxidation in edible oils and fatty foods at room temperature, which is called the pyridoxamine-participating ferrous oxidation-sulfosalicylic acid (PFOS) method. The PFOS method evaluates the lipid peroxide value colorimetrically via detecting the pyridoxamine-mediated pigment produced by 5-sulfosalicylic acid and Fe(3+) at 500nm, while the latter is converted from Fe(2+) in the presence of lipid peroxides. The optimized formulation was ethanol (70%, v/v), Fe(2+) (4mmol/L), 5-sulfosalicylic acid (40mmol/L) and pyridoxamine (18mmol/L). The limit of quantitation is 0.087mmol Fe(3+)/L with acceptable reproducibility. In addition, current method has a significant linear correlation with both conventional thiobarbituric acid (R(2)=0.9999) and ferric thiocyanate assays (R(2)=0.9675). This method offers a rapid technique for evaluating lipid peroxidation without heating and sophisticated instrumental procedures. Besides, current method provides a new option to evaluate the lipid peroxidation state and improve the reproducibility of ferrous-oxidation.
[Mh] Termos MeSH primário: Benzenossulfonatos/química
Compostos Ferrosos/química
Peroxidação de Lipídeos/fisiologia
Peróxidos Lipídicos/análise
Piridoxamina/química
Salicilatos/química
[Mh] Termos MeSH secundário: Animais
Proteínas Anticongelantes Tipo I
Oxirredução
Reprodutibilidade dos Testes
Espectrofotometria/métodos
Suínos
Fatores de Tempo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antifreeze Proteins, Type I); 0 (Benzenesulfonates); 0 (Ferrous Compounds); 0 (Lipid Peroxides); 0 (Salicylates); 6466NM3W93 (Pyridoxamine); G7036X8B5H (ferrous oxide); L8XED79U3U (sulfosalicylic acid)
[Em] Mês de entrada:1701
[Cu] Atualização por classe:170119
[Lr] Data última revisão:
170119
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160611
[St] Status:MEDLINE


  10 / 568 MEDLINE  
              first record previous record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:27194713
[Au] Autor:Skrypnyk NI; Voziyan P; Yang H; de Caestecker CR; Theberge MC; Drouin M; Hudson B; Harris RC; de Caestecker MP
[Ad] Endereço:Division of Nephrology, Department of Medicine, Vanderbilt University Medical Center, Nashville, Tennessee;
[Ti] Título:Pyridoxamine reduces postinjury fibrosis and improves functional recovery after acute kidney injury.
[So] Source:Am J Physiol Renal Physiol;311(2):F268-77, 2016 Aug 01.
[Is] ISSN:1522-1466
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Acute kidney injury (AKI) is a common and independent risk factor for death and chronic kidney disease (CKD). Despite promising preclinical data, there is no evidence that antioxidants reduce the severity of injury, increase recovery, or prevent CKD in patients with AKI. Pyridoxamine (PM) is a structural analog of vitamin B6 that interferes with oxidative macromolecular damage via a number of different mechanisms and is in a phase 3 clinical efficacy trial to delay CKD progression in patients with diabetic kidney disease. Because oxidative stress is implicated as one of the main drivers of renal injury after AKI, the ability of PM to interfere with multiple aspects of oxidative damage may be favorable for AKI treatment. In these studies we therefore evaluated PM treatment in a mouse model of AKI. Pretreatment with PM caused a dose-dependent reduction in acute tubular injury, long-term postinjury fibrosis, as well as improved functional recovery after ischemia-reperfusion AKI (IR-AKI). This was associated with a dose-dependent reduction in the oxidative stress marker isofuran-to-F2-isoprostane ratio, indicating that PM reduces renal oxidative damage post-AKI. PM also reduced postinjury fibrosis when administered 24 h after the initiating injury, but this was not associated with improvement in functional recovery after IR-AKI. This is the first report showing that treatment with PM reduces short- and long-term injury, fibrosis, and renal functional recovery after IR-AKI. These preclinical findings suggest that PM, which has a favorable clinical safety profile, holds therapeutic promise for AKI and, most importantly, for prevention of adverse long-term outcomes after AKI.
[Mh] Termos MeSH primário: Lesão Renal Aguda/tratamento farmacológico
Piridoxamina/uso terapêutico
Complexo Vitamínico B/uso terapêutico
[Mh] Termos MeSH secundário: Lesão Renal Aguda/patologia
Animais
Relação Dose-Resposta a Droga
Fibrose
Isoprostanos/metabolismo
Túbulos Renais/patologia
Masculino
Camundongos
Camundongos Endogâmicos BALB C
Estresse Oxidativo/efeitos dos fármacos
Piridoxamina/sangue
Recuperação de Função Fisiológica
Complexo Vitamínico B/sangue
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Isoprostanes); 12001-76-2 (Vitamin B Complex); 6466NM3W93 (Pyridoxamine)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:170801
[Lr] Data última revisão:
170801
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160520
[St] Status:MEDLINE
[do] DOI:10.1152/ajprenal.00056.2016



página 1 de 57 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