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1.
Artículo en Inglés | MEDLINE | ID: mdl-30041062

RESUMEN

Hypoxia inducible factor-1 (HIF-1) is a transcriptional factor that induces genes involved in glucose metabolism. HIF-1 is formed by a regulatory α-subunit (HIF-1α) and a constitutive ß-subunit (HIF-1ß). The white spot syndrome virus (WSSV) induces a shift in glucose metabolism and oxidative stress. HIF-1α is associated with the induction of metabolic changes in tissues of WSSV-infected shrimp. However, the contributions of HIF-1 to viral load and antioxidant responses in WSSV-infected shrimp have been not examined. In this study, the effect of HIF-1 silencing on viral load and the expression and activity of antioxidant enzymes (superoxide dismutase-SOD, glutathione S-transferase-GST, and catalase) along with oxidative damage (lipid peroxidation and protein carbonyl) in tissues of white shrimp infected with the WSSV were studied. The viral load increased in hepatopancreas and muscle after WSSV infection, and the accumulative mortality was of 100% at 72 h post-infection. The expression and activity of SOD, catalase, and GST decreased in each tissue evaluated after WSSV infection. Protein carbonyl concentrations increased in each tissue after WSSV infection, while lipid peroxidation increased in hepatopancreas, but not in muscle. Silencing of HIF-1α decreased the WSSV viral load in hepatopancreas and muscle of infected shrimp along with shrimp mortality. Silencing of HIF-1α ameliorated the antioxidant response in a tissue-specific manner, which translated to a decrease in oxidative damage. These results suggest that HIF-1 is essential for restoring the antioxidant response, which counters the oxidative injury associated with WSSV infection.


Asunto(s)
Regulación del Desarrollo de la Expresión Génica , Subunidad alfa del Factor 1 Inducible por Hipoxia/antagonistas & inhibidores , Penaeidae/virología , Virus del Síndrome de la Mancha Blanca 1/patogenicidad , Animales , Acuicultura , ADN Viral/aislamiento & purificación , Silenciador del Gen , Hepatopáncreas/crecimiento & desarrollo , Hepatopáncreas/metabolismo , Hepatopáncreas/virología , Subunidad alfa del Factor 1 Inducible por Hipoxia/genética , Subunidad alfa del Factor 1 Inducible por Hipoxia/metabolismo , Inyecciones Intramusculares , Peroxidación de Lípido , México , Músculos/metabolismo , Músculos/virología , Especificidad de Órganos , Estrés Oxidativo , Oxidorreductasas/genética , Oxidorreductasas/metabolismo , Penaeidae/crecimiento & desarrollo , Penaeidae/metabolismo , Carbonilación Proteica , Interferencia de ARN , ARN Bicatenario/administración & dosificación , ARN Bicatenario/metabolismo , Carga Viral , Virus del Síndrome de la Mancha Blanca 1/aislamiento & purificación , Virus del Síndrome de la Mancha Blanca 1/fisiología
2.
Biomed Res Int ; 2014: 984785, 2014.
Artículo en Inglés | MEDLINE | ID: mdl-25147829

RESUMEN

The pathologic cardiac remodeling has been widely documented; however, the physiological cardiac remodeling induced by pregnancy and its reversion in postpartum are poorly understood. In the present study we investigated the changes in collagen I (Col I) and collagen III (Col III) mRNA and protein levels in left ventricle from rat heart during pregnancy and postpartum. Col I and Col III mRNA expression in left ventricle samples during pregnancy and postpartum were analyzed by using quantitative PCR. Data obtained from gene expression show that Col I and Col III in left ventricle are upregulated during pregnancy with reversion in postpartum. In contrast to gene expression, the protein expression evaluated by western blot showed that Col I is downregulated and Col III is upregulated in left ventricle during pregnancy. In conclusion, the pregnancy differentially regulates collagens types I and III in heart; this finding could be an important molecular mechanism that regulates the ventricular stiffness in response to blood volume overload present during pregnancy which is reversed in postpartum.


Asunto(s)
Colágeno Tipo III/genética , Colágeno Tipo III/metabolismo , Colágeno Tipo I/genética , Colágeno Tipo I/metabolismo , Ventrículos Cardíacos/metabolismo , Animales , Regulación hacia Abajo/genética , Femenino , Expresión Génica/genética , Periodo Posparto/genética , Embarazo , ARN Mensajero/genética , Ratas , Ratas Sprague-Dawley , Regulación hacia Arriba/genética
3.
Protein Pept Lett ; 13(1): 71-5, 2006.
Artículo en Inglés | MEDLINE | ID: mdl-16454673

RESUMEN

Shrimp High Density Lipoprotein-beta-Glucan Binding Protein (HDL/BGBP) has been studied by its role in nutrition and innate defense. Although the mechanisms of lipid loading are still unknown, HDL-BGBP binds and aggregates phospholipids vesicles in vitro. To gain insights into the HDL-BGBP mechanism of interaction with membranes, we have used fluorescence spectroscopy and electron microscopy. Data show that HDL-BGBP does not induce membrane fusion, leakage nor lipid exchange, although microstructural changes are clearly observed. This work supports a model where protein aggregation leads to liposome clustering. Such interaction may be a critical factor for the activation of the shrimp blood cell in vivo.


Asunto(s)
Proteínas Portadoras/química , HDL-Colesterol/química , Lectinas/química , Animales , Fenómenos Biofísicos , Biofisica , Proteínas Portadoras/ultraestructura , Crustáceos , Lectinas/ultraestructura , Liposomas , Lípidos de la Membrana/química , Microscopía Electrónica , Espectrometría de Fluorescencia
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