5 research outputs found
Proyecto: agencia turÃstica, Guayaquil, ciudad del rÃo
El producto de la Agencia TurÃstica Ciudad del RÃo nace en razón de la necesidad y la importancia de promover internamente la ciudad de guayaquil y sus alrededores y de la comunicación en el turismo, el producto que ofrece ésta empresa es fundamentalmente una variedad de tours a través de los cuales se otorga a los ciudadanos y turistas la opción de conocer y recorrer importantes atractivos turÃsticos, ofreciendo a las personas una forma diferente y divertida de compartir un momento agradable con familiares o amigos mientras se culturiza y aprende un poco del lugar en el que viven o del sitio que visitan, y de su historia. Asà también, le da al turista, la opción de asistir a un paseo organizado por guÃas especializados que lo llevarán a recorrer por sitios que éste estarÃa encantado de conocer, lo que permite que el turista saque provecho de su tiempo de estancia en la ciudad a través del cronograma de actividades y lugares a visitar que promueve el tour, ya que por el contrario, un turista que desconoce un lugar muy probablemente se lo encontrará dando vueltas inciertas desconociendo cuales son los sitios dignos de conocer y admirar a los que podrÃa asistir.
Se ha desarrollado una investigación de mercado a una muestra de 500 personas con el objeto de obtener una correcta interpretación, descripción y evaluación de la información obtenida a través de la búsqueda de datos que permiten tomar medidas apropiadas para llevar a cabo la constitución y el desarrollo de la empresa: Agencia TurÃstica Ciudad del RÃo.
La estrategia de posicionamiento que la Agencia TurÃstica Ciudad del RÃo pretende establecer es la de Posicionamiento con relación a un mercado Meta, la misma considera que lo más importante es la satisfacción de las necesidades del consumidor y pretende que el producto se encuentre posicionado en la mente de los consumidores de modo que, cuando las personas piensen en el producto que les ofrece la agencia turÃstica Ciudad del RÃo, piensen en un producto que les ofrece precisamente las caracterÃsticas y atributos que ellos desean y consideran necesarias, es decir: recreación y diversión, enseñanza y culturización
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ER-stress mobilization of death-associated protein kinase-1-dependent xenophagy counteracts mitochondria stress-induced epithelial barrier dysfunction.
The gut microbiome contributes to inflammatory bowel disease (IBD), in which bacteria can be present within the epithelium. Epithelial barrier function is decreased in IBD, and dysfunctional epithelial mitochondria and endoplasmic reticulum (ER) stress have been individually associated with IBD. We therefore hypothesized that the combination of ER and mitochondrial stresses significantly disrupt epithelial barrier function. Here, we treated human colonic biopsies, epithelial colonoids, and epithelial cells with an uncoupler of oxidative phosphorylation, dinitrophenol (DNP), with or without the ER stressor tunicamycin and assessed epithelial barrier function by monitoring internalization and translocation of commensal bacteria. We also examined barrier function and colitis in mice exposed to dextran sodium sulfate (DSS) or DNP and co-treated with DAPK6, an inhibitor of death-associated protein kinase 1 (DAPK1). Contrary to our hypothesis, induction of ER stress (i.e. the unfolded protein response) protected against decreased barrier function caused by the disruption of mitochondrial function. ER stress did not prevent DNP-driven uptake of bacteria; rather, specific mobilization of the ATF6 arm of ER stress and recruitment of DAPK1 resulted in enhanced autophagic killing (xenophagy) of bacteria. Of note, epithelia with a Crohn's disease-susceptibility mutation in the autophagy gene ATG16L1 exhibited less xenophagy. Systemic delivery of the DAPK1 inhibitor DAPK6 increased bacterial translocation in DSS- or DNP-treated mice. We conclude that promoting ER stress-ATF6-DAPK1 signaling in transporting enterocytes counters the transcellular passage of bacteria evoked by dysfunctional mitochondria, thereby reducing the potential for metabolic stress to reactivate or perpetuate inflammation
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ER-stress mobilization of death-associated protein kinase-1-dependent xenophagy counteracts mitochondria stress-induced epithelial barrier dysfunction.
The gut microbiome contributes to inflammatory bowel disease (IBD), in which bacteria can be present within the epithelium. Epithelial barrier function is decreased in IBD, and dysfunctional epithelial mitochondria and endoplasmic reticulum (ER) stress have been individually associated with IBD. We therefore hypothesized that the combination of ER and mitochondrial stresses significantly disrupt epithelial barrier function. Here, we treated human colonic biopsies, epithelial colonoids, and epithelial cells with an uncoupler of oxidative phosphorylation, dinitrophenol (DNP), with or without the ER stressor tunicamycin and assessed epithelial barrier function by monitoring internalization and translocation of commensal bacteria. We also examined barrier function and colitis in mice exposed to dextran sodium sulfate (DSS) or DNP and co-treated with DAPK6, an inhibitor of death-associated protein kinase 1 (DAPK1). Contrary to our hypothesis, induction of ER stress (i.e. the unfolded protein response) protected against decreased barrier function caused by the disruption of mitochondrial function. ER stress did not prevent DNP-driven uptake of bacteria; rather, specific mobilization of the ATF6 arm of ER stress and recruitment of DAPK1 resulted in enhanced autophagic killing (xenophagy) of bacteria. Of note, epithelia with a Crohn's disease-susceptibility mutation in the autophagy gene ATG16L1 exhibited less xenophagy. Systemic delivery of the DAPK1 inhibitor DAPK6 increased bacterial translocation in DSS- or DNP-treated mice. We conclude that promoting ER stress-ATF6-DAPK1 signaling in transporting enterocytes counters the transcellular passage of bacteria evoked by dysfunctional mitochondria, thereby reducing the potential for metabolic stress to reactivate or perpetuate inflammation