Your browser doesn't support javascript.
loading
Mostrar: 20 | 50 | 100
Resultados 1 - 2 de 2
Filtrar
Más filtros










Base de datos
Intervalo de año de publicación
1.
Placenta ; 25(7): 608-22, 2004 Aug.
Artículo en Inglés | MEDLINE | ID: mdl-15193867

RESUMEN

Placental tissue protein 13 (PP-13), one of the 56 known placental proteins identified till today, was purified from placentas obtained from women at delivery, and used to evoke antibodies against it. The purified PP-13 was lysed to peptides, which were sequenced, leading to the full-length cDNA sequencing and its expression in Escherichia coli. Sequence analysis in databases showed homology to the galectin family. Of the various antibody preparations developed, a pair of monoclonal antibodies (MAbs) coupled to the recombinant PP-13 (PP-13-R) was used for the immunodetection of PP-13 in pregnant women's serum with the solid-phase ELISA format. With a dynamic range of 25-500 pg/mL with no background in non-pregnant women's serum and men's serum, the ELISA test was suitable for the detection of PP-13 in the 1st, 2nd, and 3rd trimesters. PP-13 levels slowly increase during pregnancy. In the 1st trimester, lower than normal PP-13 levels were found in fetal growth restriction (IUGR), preeclampsia (PE), and particularly in early PE (<34 weeks of gestation). In the 2nd and 3rd trimesters, higher than normal concentrations were found in PE, IUGR and in preterm delivery (PTD). Application of PP-13 to cultured trophoblasts elicited depolarization carried by calcium ions, followed by liberation of linoleic and arachidonic acids from the trophoblast membrane, and a subsequent elevation of prostacyclin and thromboxane. These effects were negligible when PP-13 derived from the placentas of patients with IUGR, PE or PTD was used. The results are discussed in view of the potential utilization of PP-13 for early serum screening to assess the risk to develop placental insufficiency, coupled to a differential analysis of the various pathologies by analyzing cultured trophoblasts.


Asunto(s)
Líquidos Corporales/química , Complicaciones del Embarazo/metabolismo , Proteínas Gestacionales/análisis , Proteínas Gestacionales/farmacología , Trofoblastos/efectos de los fármacos , Secuencia de Aminoácidos , Líquido Amniótico/química , Animales , Anticuerpos Monoclonales , Secuencia de Bases , Células Cultivadas , ADN Complementario/análisis , ADN Complementario/química , Ensayo de Inmunoadsorción Enzimática , Femenino , Retardo del Crecimiento Fetal/metabolismo , Galectinas , Edad Gestacional , Humanos , Ratones , Ratones Endogámicos BALB C , Datos de Secuencia Molecular , Trabajo de Parto Prematuro , Preeclampsia/metabolismo , Embarazo , Proteínas Gestacionales/genética , Radioinmunoensayo , Proteínas Recombinantes , Sensibilidad y Especificidad , Homología de Secuencia
2.
FEMS Immunol Med Microbiol ; 29(4): 295-301, 2000 Dec.
Artículo en Inglés | MEDLINE | ID: mdl-11118911

RESUMEN

Because previous studies have shown that a high molecular mass constituent of cranberry juice inhibited adhesion of Escherichia coli to epithelial cells and coaggregation of oral bacteria, we have examined its effect on the adhesion of Helicobacter pylori to immobilized human mucus and to erythrocytes. We employed three strains of H. pylori all of which bound to the mucus and agglutinated human erythrocytes via a sialic acid-specific adhesin. The results showed that a high molecular mass constituent derived from cranberry juice inhibits the sialic acid-specific adhesion of H. pylori to human gastric mucus and to human erythrocytes.


Asunto(s)
Adhesión Bacteriana , Bebidas , Eritrocitos/microbiología , Frutas/química , Helicobacter pylori/fisiología , Moco/microbiología , Estómago , Infecciones por Helicobacter/microbiología , Helicobacter pylori/patogenicidad , Humanos , Ácido N-Acetilneuramínico
SELECCIÓN DE REFERENCIAS
DETALLE DE LA BÚSQUEDA
...