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3.
Am J Med Genet B Neuropsychiatr Genet ; 118B(1): 36-40, 2003 Apr 01.
Artigo em Inglês | MEDLINE | ID: mdl-12627464

RESUMO

Suicide is an important public health problem, accounting for a significant proportion of total mortality among young people, particularly males. There is growing and consistent evidence suggesting that genetic factors play an important role in the predisposition to suicide. Based on several lines of evidence supporting a reduced serotonergic neurotransmission in subjects who committed suicide, we investigated variation at genes that code for serotonin receptor 1B (5-HTR1B), 1Dalpha (5-HTR1Dalpha), 1E (5-HTR1E), 1F (5-HTR1F), 2C (5-HTR2C), 5A (5-HTR5A), and 6 (5-HTR6) in a total sample of 106 suicide completers and 120 normal controls. No differences were observed in allelic or genotypic distributions between groups for any of the loci investigated. Moreover, further analysis according to suicide method or psychopathology also failed to reveal differences between groups. Our results do not support a substantial role of these serotonergic receptors in suicide completion.


Assuntos
Receptores de Serotonina/genética , Suicídio , Alelos , Frequência do Gene , Genótipo , Humanos , Polimorfismo Genético , Isoformas de Proteínas/genética
4.
Muscle Nerve ; 23(6): 967-9, 2000 Jun.
Artigo em Inglês | MEDLINE | ID: mdl-10842276

RESUMO

The effect of sepsis on the ubiquitously expressed ATP-sensitive potassium (uK(ATP)-1) channel expression was measured in Sprague-Dawley rat diaphragms. Rats were treated with either 0.5 ml saline or 20 mg/Kg E. coli lipopolysaccharides and sacrificed at 3, 6, 12, 24, or 48 h later. Reverse transcriptase-polymerase chain reaction (RT-PCR) analysis showed that channel mRNA expression was increased at 3 h and continued to rise up to 48 h. Western blotting analysis showed a approximately 9-fold increase in channel protein expression 24 h after sepsis. Our results demonstrate that sepsis upregulates the uK(ATP)-1 channel.


Assuntos
Diafragma/metabolismo , Endotoxemia/metabolismo , Canais de Potássio Corretores do Fluxo de Internalização , Canais de Potássio/genética , Trifosfato de Adenosina/metabolismo , Animais , Western Blotting , Diafragma/química , Endotoxemia/induzido quimicamente , Expressão Gênica/efeitos dos fármacos , Expressão Gênica/fisiologia , Lipopolissacarídeos/farmacologia , Masculino , Canais de Potássio/análise , RNA Mensageiro/análise , Ratos , Ratos Sprague-Dawley , Regulação para Cima/fisiologia
5.
FEBS Lett ; 402(1): 41-4, 1997 Jan 27.
Artigo em Inglês | MEDLINE | ID: mdl-9013855

RESUMO

Polyamines (PAs) are ubiquitous in cells of higher plants and play an important role in many biological functions. Because PAs affect photosynthetic oxygen evolution, this study is designed to investigate the interaction of spermine (Spm) and spermidine (Spd) cations with proteins of photosystem II (PSII) using PSII-enriched submembranes fraction with polyamine concentrations of 0.01-10 mM. Fourier transform infrared (FTIR) difference spectroscopy with its self-deconvolution and second derivative resolution enhancement as well as curve-fitting procedures was applied, in order to determine the cation binding mode, the protein conformational changes and the structural properties of cation-protein complexes. It is shown that at low polyamine concentration, cation-protein interaction (H-bonding) is through the polypeptide C=O groups with no major perturbation of the protein secondary structure. As cation concentration increases, the polyamine complexation causes significant alterations of the protein secondary structure with a decrease of the alpha-helical domains from 47% (uncomplexed PSII) up to 37% (cation complexes) and an increase in the beta-sheet structure from 18% (uncomplexed PSII) up to 29% (cation complexes). Correlations between the effects of polyamines on protein secondary structure and on the rate of oxygen evolution in PSII are also established.


Assuntos
Complexo de Proteínas do Centro de Reação Fotossintética/química , Complexo de Proteínas do Centro de Reação Fotossintética/metabolismo , Estrutura Secundária de Proteína/efeitos dos fármacos , Espermidina/farmacologia , Espermina/farmacologia , Cátions , Transporte de Elétrons/efeitos dos fármacos , Ligação de Hidrogênio , Oxigênio/metabolismo , Fotossíntese/efeitos dos fármacos , Complexo de Proteína do Fotossistema II , Espectroscopia de Infravermelho com Transformada de Fourier , Espermidina/metabolismo , Espermina/metabolismo
6.
Science ; 260(5111): 1165-6, 1993 May 21.
Artigo em Inglês | MEDLINE | ID: mdl-17806352
8.
Science ; 235(4785): 225-6, 1987 Jan 09.
Artigo em Inglês | MEDLINE | ID: mdl-17778638
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