Base de dados : LILACS
Pesquisa : C16.320.565.398.500.330.500 [Categoria DeCS]
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Fotocópia
Id: lil-273181
Autor: Brites, Fernando D; Fernandez, Karina M; Yael, Mario J; Wikinski, Regina L. W.
Título: Evolución de una paciente con sindrome de deficiencia parcial de lecitina: colesterol aciltransferasa (LCAT) / Evolution of a patient with a partial deficiency of lecithin: cholesterol acyltransferase
Fonte: Medicina (B.Aires);60(3):406-7, 2000.
Idioma: es.
Descritores: Deficiência da Lecitina Colesterol Aciltransferase/sangue
Limites: Humanos
Feminino
Pessoa de Meia-Idade
Tipo de Publ: Carta
Relatos de Casos
Responsável: BR1.1 - BIREME


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Fotocópia
Id: lil-231919
Autor: Brites, Fernando D; Fernandez, Karina M; Zunino, Maria J; Yael, Mario J; Lardo, Mabel; Castro, Graciela R; Wikinski, Regina L. W.
Título: Sindrome de deficiencia parcial de lecitina-colesterol aciltransferasa (LCAT) / Partial lecithin-cholesterol acyltransferase (LCAT) deficiency syndrome
Fonte: Medicina (B.Aires);59(1):89-92, 1999. ilus, tab.
Idioma: es.
Resumo: El síndrome de deficiencia parcial de la enzima lecitina-colesterol aciltransferasa (LCAT) es una en tidad patológica de baja incidencia que afecta fundamentalmente el metabolismo de las lipoproteínas de alta densidad (HDL). Comunicamos el primer caso reportado en nuestro país. Se presentó en una mujer de 63 años de edad que tenía opacidad corneal bilateral y xantomas eruptivos en brazos y antebrazos. El estudio lipoproteico reveló hipertrigliceridemia severa t colesterolemia normal, aunque la proporción de colesterol esterificado se hallaba substancialmente disminuida. Es de notar que los niveles plasmáticos de colesterol-HDL y de sus apoproteínas mayoritarias, A-I y A-IIm fueron insualmente bajos. Se observó además intolerancia a la glucosa y alteraciones hematológicas relacionadas con una composición lipídica anormal de las membranas eritrocitarias. La actividad plasmática de la LCAT, evaluada por el método del sustrato exógeno, fue un 82 por ciento menor en la paciente que en un individuo control. Es de destacar que la paciente aquí descripta mostró antecedentes de episodios cardíacos e hipertensión arterial, lo cual difere de muchos de los casos de deficiencia parcial de la enzima (LCAT).
Descritores: HDL-Colesterol/sangue
Deficiência da Lecitina Colesterol Aciltransferase/sangue
-Fenofibrato/uso terapêutico
Deficiência da Lecitina Colesterol Aciltransferase/complicações
Deficiência da Lecitina Colesterol Aciltransferase/diagnóstico
Deficiência da Lecitina Colesterol Aciltransferase/tratamento farmacológico
Síndrome
Limites: Pessoa de Meia-Idade
Feminino
Humanos
Tipo de Publ: Relatos de Casos
Responsável: BR1.1 - BIREME


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Fotocópia
Chaves, M. E. C
Id: lil-187365
Autor: Lima, V. L. M; Harry, D. S; Mclntyre, N; Owen, J. S; Chaves, M. E. C.
Título: Characterization and potential uses of rabbit polyclonal antibodies against human plasma lecithin-cholesterol acyltransferase
Fonte: Braz. j. med. biol. res = Rev. bras. pesqui. méd. biol;29(8):957-68, Aug. 1996. ilus, tab, graf.
Idioma: en.
Resumo: Familial and secondary deficiency of plasma lecithin-cholesterol acyltransferase (LCAT) produce circulating lipoprotein particles with gross structural and compositional abnormalities; these have adverse effects on a variety of cellular functions. Factors affecting hepatic synthesis and secretion of this plasma enzyme are largely unknown but, potentially, some of them can be investigated with monospecific antibodies. In the present study, enzymically active LCAT was purified 40,000-fold from human plasma and then used to raise polyclonal antibodies in New Zealand White rabbits. Addition of this antiserum (1 mul) to human plasma (25 mul) completely inhibited LCAT activity, although it was less effective against plasma from other species. The antibodies appeared to be monospecific to plasma LCAT. They gave a single precipitin arc by crossed immunoelectrophoresis, while immunodiffusion established that there was no cross-reactivity with several apolipoproteins or with serum albumin. Moreover, the antiserum was successfully used to detect LCAT in normal human plasma by Laurell rocket immunoelectrophoresis. By contrast, Western blotting of plasma proteins using whole LCAT antiserum was largely unsuccessful because of high background staining, although this could be substantially reduced by use of an IgG fraction. However, the whole antiserum readily immunoprecipitated LCAT secreted into the culture medium of HepG2 cells, a human hepatoblastoma cell line, pre-labelled with [35S]methionine, the [(35)S]-labelled LCAT appearing as a narrow 65-kDa protein band by electrophoresis and fluorography. We conclude that polyclonal antibodies may be an important tool to investigate the characteristics and underlying mechanisms of secondary LCAT deficiencies, including those associated with hepatic cirrhosis and schistosomiasis.
Descritores: Anticorpos/administração & dosagem
Proteínas Sanguíneas/análise
Fosfatidilcolina-Esterol O-Aciltransferase/análise
Fosfatidilcolina-Esterol O-Aciltransferase/imunologia
-Western Blotting
Imunoeletroforese Bidimensional
Deficiência da Lecitina Colesterol Aciltransferase/imunologia
Deficiência da Lecitina Colesterol Aciltransferase/patologia
Limites: Humanos
Tipo de Publ: Research Support, Non-U.S. Gov't
Responsável: BR1.1 - BIREME



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