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1.
Salud pública Méx ; 56(4): 402-404, jul.-ago. 2014. tab
Artículo en Español | LILACS | ID: lil-733306

RESUMEN

La fiebre chikungunya (CHIK) es una enfermedad viral transmitida al ser humano por el mismo vector del dengue, el mosquito Aedes. Además de fiebre y fuertes dolores articulares, produce otros síntomas como mialgias, cefalea, náuseas, cansancio y exantema. No tiene tratamiento específico; el manejo terapéutico de los pacientes se enfoca en el alivio de los síntomas. Históricamente se han reportado brotes de grandes proporciones; incluso desde 2010 se llegó a considerar como una potencial epidemia emergente. En 2013 se introdujo a las islas del Caribe y recientemente se ha reportado en el continente americano. En este trabajo se describe el primer caso confirmado de chikungunya en México, en el municipio de Tlajomulco de Zúñiga, Jalisco, en mayo de 2014, importado de la isla Antigua y Barbuda, en el Caribe, por una mujer de 39 años de edad.


Chikungunya fever (CHIK) is a viral disease transmitted to human beings by the same vector as dengue -the Aedes mosquito. Besides fever and severe pain in the joints, it produces other symptoms such as myalgias, headache, nausea, fatigue and exanthema. There is no specific treatment for it; the therapeutic management of patients focuses on symptom relief. Historically, outbreaks of large proportions have been reported; even since 2010 it was considered to be a potential emerging epidemic. In 2013 it was introduced into the islands of the Caribbean, and it has recently been reported in the American continent. This paper describes the first confirmed case of chikungunya in Mexico -in the municipality of Tlajomulco de Zúñiga, Jalisco, in May, 2014-, which was imported from the Caribbean island of Antigua and Barbuda by a 39 year-old woman.


Asunto(s)
Animales , Bovinos , Masculino , Ratas , Antídotos/farmacología , Calor , Imidazoles/toxicidad , Carne , Mitocondrias/metabolismo , Mutágenos/toxicidad , Consumo de Oxígeno/efectos de los fármacos , Ubiquinona/farmacología , Antídotos/administración & dosificación , Culinaria , Dieta , Complejo II de Transporte de Electrones , Complejo III de Transporte de Electrones/metabolismo , Complejo IV de Transporte de Electrones/metabolismo , Transporte de Electrón/efectos de los fármacos , Alimentos Fortificados , Mitocondrias Cardíacas/efectos de los fármacos , Mitocondrias Cardíacas/metabolismo , Mitocondrias Hepáticas/efectos de los fármacos , Mitocondrias Hepáticas/metabolismo , Mitocondrias Musculares/efectos de los fármacos , Mitocondrias Musculares/metabolismo , Complejos Multienzimáticos/metabolismo , NAD(P)H Deshidrogenasa (Quinona)/metabolismo , Oxidorreductasas/metabolismo , Ratas Wistar , Succinato Deshidrogenasa/metabolismo , Ubiquinona/administración & dosificación
2.
Experimental & Molecular Medicine ; : 222-229, 2007.
Artículo en Inglés | WPRIM | ID: wpr-90610

RESUMEN

trans-Resveratrol (t-RVT), a naturally occurring polyphenol found in Polygonum cuspidatum, grape, and red wine, has been reported to have anti- inflammatory, cardioprotective, and cancer chemopreventive properties. However antidiabetic effect of t-RVT has not yet been reported. In this study, we show that t-RVT increases glucose uptake in C2C12 myotubes by activating AMP-activated protein kinase (AMPK), uncovering an antidiabetic potential of t-RVT for the first time. AMPK plays a central role in the regulation of glucose and lipid metabolism, and hence it is considered a novel therapeutic target for metabolic syndrome such as type 2 diabetes. t-RVT significantly induced glucose uptake in C2C12 cells, via AMPK activation, but not a phosphatidylinositol-3 kinase (PI-3 kinase) signal pathway. The induced glucose uptake was attenuated by pretreatment with a pharmacological inhibitor for AMPK, indicating that the effect of t-RVT primarily depends on AMPK activation. However, in the presence of insulin, t-RVT also potentiated the effect of insulin on glucose uptake via AMPK activation, which led to further activation of PI-3 kinase/Akt signal pathway.


Asunto(s)
Animales , Ratones , Fosfatidilinositol 3-Quinasa/metabolismo , Proteínas Quinasas Activadas por AMP , Transporte Biológico/efectos de los fármacos , Línea Celular , Activación Enzimática/efectos de los fármacos , Glucosa/metabolismo , Insulina/metabolismo , Modelos Biológicos , Complejos Multienzimáticos/metabolismo , Fibras Musculares Esqueléticas/efectos de los fármacos , Proteínas Serina-Treonina Quinasas/metabolismo , Proteínas Proto-Oncogénicas c-akt/metabolismo , Estilbenos/farmacología
3.
Experimental & Molecular Medicine ; : 395-401, 2007.
Artículo en Inglés | WPRIM | ID: wpr-195954

RESUMEN

It is well known that exercise can have beneficial effects on insulin resistance by activation of glucose transporter. Following up our previous report that caveolin-1 plays an important role in glucose uptake in L6 skeletal muscle cells, we examined whether exercise alters the expression of caveolin-1, and whether exercise-caused changes are muscle fiber and exercise type specific. Fifity week-old Sprague Dawley (SD) rats were trained to climb a ladder and treadmill for 8 weeks and their soleus muscles (SOL) and extensor digitorum longus muscles (EDL) were removed after the last bout of exercise and compared with those from non-exercised animals. We found that the expression of insulin related proteins and caveolins did not change in SOL muscles after exercise. However, in EDL muscles, the expression of insulin receptor beta (IRbeta) and glucose transporter-4 (GLUT-4) as well as phosphorylation of AKT and AMPK increased with resistance exercise but not with aerobic exercise. Also, caveolin-1 and caveolin-3 increased along with insulin related proteins only in EDL muscles by resistance exercise. These results suggest that upregulation of caveolin-1 in the skeletal muscle is fiber specific and exercise type specific, implicating the requirement of the specific mode of exercise to improve insulin sensitivity.


Asunto(s)
Animales , Femenino , Ratas , Proteínas Quinasas Activadas por AMP , Caveolina 1/biosíntesis , Caveolina 3/metabolismo , Transportador de Glucosa de Tipo 4/biosíntesis , Insulina/fisiología , Complejos Multienzimáticos/metabolismo , Fibras Musculares Esqueléticas/metabolismo , Músculo Esquelético/metabolismo , Fosforilación , Condicionamiento Físico Animal , Proteínas Serina-Treonina Quinasas/metabolismo , Proteínas Proto-Oncogénicas c-akt/metabolismo , Ratas Sprague-Dawley , Receptor de Insulina/biosíntesis , Regulación hacia Arriba
4.
Genet. mol. res. (Online) ; 2(4): 348-359, Dec. 2003.
Artículo en Inglés | LILACS | ID: lil-417595

RESUMEN

Lactococcus lactis, the most extensively characterized lactic acid bacterium, is a mesophilic- and microaerophilic-fermenting microorganism widely used for the production of fermented food products. During industrial processes, L. lactis is often exposed to multiple environmental stresses (low and high temperature, low pH, high osmotic pressure, nutrient starvation and oxidation) that can cause loss or reduction of bacterial viability, reproducibility, as well as organoleptic and/or fermentative qualities. Among these stress factors, oxidation can be considered one of the most deleterious to the cell, causing cellular damage at both molecular and metabolic levels. During the last two decades, considerable efforts have been made to improve our knowledge of oxidative stress in L. lactis. Many genes involved with both oxidative stress resistance and control mechanisms have been identified; functionally they seem to overlap. The finding of new genes, and a better understanding of the molecular mechanisms of stress resistance in L. lactis and other lactic acid bacterium, will lead to the construction and isolation of stress-resistant strains. Such strains could be exploited for both traditional and probiotic uses


Asunto(s)
Estrés Oxidativo/fisiología , Lactococcus lactis/metabolismo , Complejos Multienzimáticos/metabolismo , Estrés Oxidativo/genética , Genes Bacterianos/genética , Lactococcus lactis/genética , NADH NADPH Oxidorreductasas/metabolismo , Peroxidasas/metabolismo , Rec A Recombinasas/metabolismo , Supervivencia Celular/genética , Superóxido Dismutasa/metabolismo
5.
Journal of Korean Medical Science ; : 135-139, 2001.
Artículo en Inglés | WPRIM | ID: wpr-179362

RESUMEN

MDM2 is a substrate of caspase-3 in p53-mediated apoptosis. In addition, MDM2 mediates its own ubiquitination in a RING finger-dependent manner. Thus, we investigated whether MDM2 is degraded through a ubiquitin-dependent proteasome pathway in the absence of p53. When HL-60 cells, p53 null, were treated with etoposide, MDM2 was markedly decreased prior to caspase-3-dependent retinoblastoma tumor suppressor protein (pRb) and poly (ADP- ribose) polymerase (PARP) cleavages. Moreover, down-regulation of MDM2 level was not coupled with its mRNA down-regulation. However, the level of MDM2 was partially restored by proteasome inhibitors such as LLnL and lactacystin, even in the presence of etoposide. Our results suggest that, in the p53 null status, MDM2 protein level is decreased by proteasome-mediated proteolysis prior to caspase-3-dependent PARP and pRb cleavages.


Asunto(s)
Humanos , Antineoplásicos Fitogénicos/farmacología , Apoptosis/efectos de los fármacos , Caspasas/metabolismo , Cisteína Endopeptidasas/metabolismo , Regulación hacia Abajo/fisiología , Etopósido/farmacología , Células HL-60 , Complejos Multienzimáticos/metabolismo , ADP Ribosa Transferasas/metabolismo , Proteínas Proto-Oncogénicas/metabolismo , Proteína de Retinoblastoma/metabolismo
6.
Indian J Exp Biol ; 2000 Aug; 38(8): 807-13
Artículo en Inglés | IMSEAR | ID: sea-59462

RESUMEN

Protoplasts isolated from Cuscuta reflexa exhibited a higher rate of exogenous NADH oxidation as compared to NADPH in the dark. NAD(P)H oxidation was monitored by measuring the rate of oxygen consumption and this oxidase system was sensitive to blue light. Both NADH oxidase and its blue light sensitivity were inhibited by -SH group reacting agents. The corresponding changes occurring in H+-extrusion activity and intracellular ATP levels were also monitored. Stimulation of NADH oxidation under blue light corresponded to increased rate of H+-extrusion and intracellular ATP level, the converse was also true under NADH oxidase inhibitory conditions. These observations suggested a close functional association between blue light-sensitive plasma membrane bound redox activity and H+-ATPase in this tissue. Further, concanavalin A binding of protoplasts resulted in a loss in NADH oxidase activity and its blue light sensitivity suggesting apoplastic location and glycoprotein nature of the blue light sensitive NADH oxidase system in Cuscuta.


Asunto(s)
Membrana Celular/enzimología , Cuscuta/enzimología , Luz , Complejos Multienzimáticos/metabolismo , NAD/metabolismo , NADH NADPH Oxidorreductasas/metabolismo , Oxidación-Reducción
7.
Experimental & Molecular Medicine ; : 65-71, 1998.
Artículo en Inglés | WPRIM | ID: wpr-70157

RESUMEN

Preparation of a pure autoantigen by way of recombinant DNA technology has an important value in an accurate diagnosis or prognosis of an autoimmune disease. BCOADC-E2 subunit, a mitochondrial protein, has been known to be the autoantigen of primary biliary cirrhosis (PBC), a chronic autoimmune liver disease, as well as idiopathic dilated cardiomypathy (IDCM), a chronic autoimmune heart disease. Recombinant form of this molecule had been expressed in E. coli but with low yield and severe degradation. Furthermore, sera from IDCM patients failed to recognized BCOADC-E2 molecule produced in prokaryotic expression system. In this study, a recombinant bovine BCOADC-E2 fusion protein has been expressed in insect cells using baculovirus expression system and analyzed anti-BCOADC-E2 reactivity in sera from patients with PBC or with IDCM. Optimal production of the recombinant fusion protein has been achieved at 20 multiplicity of infection (MOI), and the protein was affinity-purified using metal-binding resins. The affinity-purified BCOADC-E2 protein was successfully recognized by sera from PBC patients, but not by sera from IDCM patients suggesting that the different auto-immune response against BCOADC-E2 is needed to be elucidated in terms of epitope recognition.


Asunto(s)
Bovinos , Humanos , Acetiltransferasas/metabolismo , Acetiltransferasas/inmunología , Acetiltransferasas/genética , Animales , Baculoviridae/genética , Cardiomiopatía Dilatada/inmunología , Sueros Inmunes , Insectos/citología , Cetona Oxidorreductasas/metabolismo , Cetona Oxidorreductasas/inmunología , Cetona Oxidorreductasas/genética , Cirrosis Hepática Biliar/inmunología , Complejos Multienzimáticos/metabolismo , Complejos Multienzimáticos/inmunología , Complejos Multienzimáticos/genética , Ingeniería de Proteínas/métodos , Proteínas Recombinantes/aislamiento & purificación , Proteínas Recombinantes/inmunología , Proteínas Recombinantes/genética
8.
Indian J Biochem Biophys ; 1994 Aug; 31(4): 215-20
Artículo en Inglés | IMSEAR | ID: sea-27990

RESUMEN

Calvin cycle multienzyme complex, consisting of phosphoriboisomerase, phosphoribulokinase and ribulose-1,5-bisphosphate carboxylase (Rubisco), shows ribose-5-phosphate + ATP dependent CO2 fixation activity with a small but discernible lag. Transient time analysis showed that the lag at pH 7 was independent of multienzyme concentration and was significantly lower than the expected transient time calculated from Km and Vmax of the individual enzymes, indicative of channeling of the intermediates in the enzyme complex. Channeling of ribulose-1,5-bisphosphate was found to offer a catalytic advantage to Rubisco. Rubisco shows a decrease in activity during catalysis in ribulose-1,5-bisphosphate dependent CO2 fixation reaction, due to the formation of the catalytic inhibitor. Such a decrease of Rubisco activity was not observed in ribose-5-phosphate + ATP dependent CO2 fixation reaction and the catalytic inhibitor was also not detected. These results suggested that the intermediates are channeled in the complex and channeling offers a catalytic facilitation to Rubisco.


Asunto(s)
Isomerasas Aldosa-Cetosa , Carbohidrato Epimerasas/metabolismo , Catálisis , Complejos Multienzimáticos/metabolismo , Fosfotransferasas (Aceptor de Grupo Alcohol)/metabolismo , Hojas de la Planta , Ribulosa-Bifosfato Carboxilasa/metabolismo , Spinacia oleracea
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