Your browser doesn't support javascript.
loading
Mostrar: 20 | 50 | 100
Resultados 1 - 3 de 3
Filtrar
Mais filtros











Intervalo de ano de publicação
1.
Rev. cuba. hematol. inmunol. hemoter ; 26(2): 28-32, Mayo-ago. 2010.
Artigo em Espanhol | LILACS | ID: lil-584693

RESUMO

La enfermedad celíaca es una enfermedad autoinmune que cursa con procesos inflamatorios en la mucosa del intestino delgado. Se produce por la ingesta de una fracción proteica del gluten de la dieta en individuos genéticamente predispuestos. Tiene diferentes formas de presentación que van desde la sintomática, típica o atípica, hasta la silente. La detección de autoanticuerpos con diversas especificidades debe ser considerada como indispensable en todos aquellos enfermos donde predominan síntomas digestivos y afectaciones nutricionales, aunque no deben descartarse otras sintomatologías atípicas como son el retraso en el crecimiento y desarrollo. En nuestro trabajo se estudió la presencia de anticuerpos antigliadina y antitransglutaminasa en el suero de 110 enfermos con clínica sugestiva de enfermedad celíaca, y se detectaron anticuerpos en 23 enfermos: 11 con antigliadina, antitransglutaminasa y biopsia positiva; 6 con antigliadina positiva, antitransglutaminasa negativa y biopsia positiva y 6 con antigliadina positiva, antitransglutaminasa negativa y biopsia negativa.


Celiac disease is an autoimmune entity with inflammatory processes in small intestine. It is caused by ingesta of gluten protein fraction in the diet of subjects with genetic predisposition subjects and has different ways of presentation including the symptomatic, typical or atypical and silent type. The detection of autoantibodies with diverse specificities must to be considered as essential in all those patients where there is predominance of digestive symptoms and nutritional affections without to rule out other atypical symptomatologies including the growth and development retard. The objective of present paper was to study the presence of anti-gliadin and anti-transglutaminase in serum of 110 patients presenting with celiac disease and it was possible to detect antibodies in 23 patients: 11 with anti-gliadin and anti-transglutaminase and a positive biopsy; 6 with positive anti-gliadin, negative anti-transglutaminase and a positive biopsy, negative anti-transglutaminase and also a negative biopsy.


Assuntos
Humanos , Masculino , Feminino , Doença Celíaca/imunologia , Gliadina/sangue , Glutaminase/sangue , Anticorpos , Estudos de Casos e Controles
2.
Am J Physiol ; 273(4): C1124-9, 1997 10.
Artigo em Inglês | MEDLINE | ID: mdl-9357754

RESUMO

The capacity of rat neutrophils to utilize glutamine was investigated by 1) determination of oxygen consumption in the presence of glucose or glutamine, 2) measurement of maximal activity of phosphate-dependent glutaminase, 3) Northern blot, Western blot, and immunocytochemical detection of glutaminase, and 4) measurement of glutamine utilization and also production of ammonia, glutamate, aspartate, alanine, and lactate and decarboxylation of [U-14C]glutamine in cells incubated for 1 h. The rate of respiration by isolated neutrophils in the absence of added substrate was 5.0 nmol x min(-1) x 10(7) cells(-1). Maximal activity of phosphate-dependent glutaminase was 56 nmol x min(-1) x mg protein(-1) in freshly obtained neutrophils; the Michaelis-Menten constant was 3.5 mM for glutamine. This enzyme activity was inhibited by 2 mM glutamate, 2 mM oxoglutarate, and 2 mM NH4Cl. The presence of glutaminase protein (65 kDa) was confirmed by Western blot and immunocytochemical detection and the presence of the mRNA (6.0 kb) by Northern blot analysis. Glutamine was utilized by neutrophils incubated for 1 h at a rate of 12.8 nmol x min(-1) x mg protein(-1) when the amino acid was added to the medium at 2 mM, which is three to four times higher than the physiological concentration. In the presence of 0.5 mM glutamine, the amino acid was utilized at a rate of 2.9 nmol x min(-1) x mg protein(-1). The addition of 0.5 mM glutamate to the incubation medium caused a marked reduction (by 70%) in glutamine utilization by neutrophils. Glucose was utilized at 7.7 nmol x min(-1) x mg protein(-1) when cells were incubated in 5 mM glucose. The conversion of [U-14C]glutamine to 14CO2 was very low: <1% was totally oxidized. The formation of ammonia was approximately 27% of glutamine utilization, and the conversion of glutamine to glutamate, aspartate, alanine, and lactate accounted for approximately 84.6% of the total amino acid utilized by neutrophils. In this study, evidence is presented that, in addition to lymphocytes and macrophages, neutrophils also utilize glutamine.


Assuntos
Glutaminase/sangue , Glutamina/sangue , Neutrófilos/metabolismo , Animais , Glicemia/metabolismo , Western Blotting , Glutaminase/biossíntese , Técnicas In Vitro , Cinética , Masculino , Consumo de Oxigênio , RNA Mensageiro/biossíntese , Ratos , Ratos Wistar , Transcrição Gênica
SELEÇÃO DE REFERÊNCIAS
DETALHE DA PESQUISA