Hacia una movilidad peatonal inclusiva en las periferias: anteproyecto para el barrio Narancay Alto, Cuenca, Ecuador.

El presente estudio se enfoca en las áreas periféricas de la ciudad de Cuenca, donde se han identificado vulnerabilidades, a menudo crónicas, con relación a la movilidad peatonal cotidiana de los vecinos y usuarios del espacio público. La falta de sistemas de circulación peatonal genera barreras físicas y un sistema de movilidad deficiente que no prioriza a los grupos vulnerables. El objetivo de esta investigación es analizar el comportamiento de los peatones en estas zonas, que presentan un contexto distinto al de las áreas centrales de las ciudades, para comprender así el entorno en el cual desarrollan sus rutinas diarias de desplazamiento a pie, con énfasis en el caso del barrio periférico Narancay Alto en la ciudad de Cuenca. De este modo, se llevó a cabo un diagnóstico de la infraestructura vial de la zona de estudio acotada al centro del barrio, poniendo énfasis en los factores de inclusividad definidos. A través del levantamiento del flujo de peatones en el área específica de estudio y las observaciones realizadas, se desarrolló un anteproyecto que atiende particularmente la condición de movilidad peatonal inclusiva de adultos mayores, niñas y niños, y personas con discapacidad.This study focuses on the peripheral areas of the city of Cuenca, where vulnerabilities have been identified, often chronic, in relation to the everyday pedestrian mobility of residents and users of public spaces. The lack of pedestrian circulation systems generates physical barriers and an inefficient mobility system that does not prioritize vulnerable groups. The objective of this research is to analyze the behavior of pedestrians in these areas, which have a different context from the central areas of cities, in order to understand the environment in which they carry out their daily walking routines, with an emphasis on the case of the peripheral neighborhood of Narancay Alto in the city of Cuenca. In this way, a diagnosis of the road infrastructure in the study area, specifically the center of the neighborhood, was carried out, focusing on the defined inclusivity factors. Through the collection of pedestrian flow data in the specific study area and the observations made, a preliminary design was developed that particularly addresses the condition of inclusive pedestrian mobility for older adults, children, and people with disabilities.0000-0001-7456-945

Genetic Structure and Expression of the Surface Glycoprotein GP82, the Main Adhesin of Trypanosoma cruzi Metacyclic Trypomastigotes

T. cruzi improves the likelihood of invading or adapting to the host through its capacity to present a large repertoire of surface molecules. the metacyclic stage-specific surface glycoprotein GP82 has been implicated in host cell invasion. GP82 is encoded by multiple genes from the trans-sialidase superfamily. GP82 shows a modular organization, with some variation of N-terminal region flanking a conserved central core where the binding sites to the mammalian cell and gastric mucin are located. the function of GP82 as adhesin in host cell invasion process could expose the protein to an intense conservative and selective pressure. GP82 is a GPI-anchored surface protein, synthesized as a 70 kDa precursor devoid of N-linked sugars. GPI-minus variants accumulate in the ER indicating that GPI anchor acts as a forward transport signal for progressing along the secretory pathway as suggested for T. cruzi mucins. It has been demonstrated that the expression of GP82 is constitutive and may be regulated at post-transcriptional level, for instance, at translational level and/or mRNA stabilization. GP82 mRNAs are mobilized to polysomes and consequently translated, but only in metacyclic trypomastigotes. Analysis of transgenic parasites indicates that the mechanism regulating GP82 expression involves multiple elements in the 3'UTR.Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)Universidade Federal de São Paulo, Escola Paulista Med, Dept Microbiol Imunol & Parasitol, BR-04023062 São Paulo, BrazilUniversidade Federal de São Paulo, Escola Paulista Med, Dept Microbiol Imunol & Parasitol, BR-04023062 São Paulo, BrazilWeb of Scienc

Diterpenoids from Azorella compacta (Umbelliferae) active on Trypanosoma cruzi

The anti-Trypanosoma cruzi activity of natural products isolated from Azorella compacta was evaluated, with particular emphasis on their effect against intracellular amastigotes. Five diterpenoids from A. compacta derived from mulinane and azorellane were isolated and identified. Only two products, named azorellanol (Y-2) and mulin-11,3-dien-20-oic acid (Y-5), showed trypanocidal activity against all stages of T. cruzi including intracellular amastigotes. At 10 µM, these compounds displayed a strong lytic activity. It ranged from 88.4 ± 0.6 to 99.0 ± 1 % for all strains and stages evaluate, with an IC50 /18 h values of 20-84 µM and 41-87 µM, respectively. The development of intracellular amastigotes was also inhibited by nearly 60% at 25 µM. The trypanocidal molecules Y-2 and Y-5 did show different degrees of cytotoxicity depending on the cell line tested, with an IC50 /24 h ranging from 33.2 to 161.2 µM. We evaluated the effect of diterpenoids against intracellular T. cruzi forms by immunofluorescent identification of a specific membrane molecular marker (Ssp-4 antigen) of the T. cruzi amastigote forms. The accuracy and reproducibility of the measurements were found to be outstanding when examined by confocal microscopy.Universidad de Antofagasta Departamento de Tecnología Médica Unidad de ParasitologíaUniversidad de Antofagasta Departamento de Química Laboratorio de Productos NaturalesUniversidade Federal de São Paulo (UNIFESP), Escola Paulista de Medicina (EPM) Imunologia e ParasitologiaUNIFESP, EPM, Imunologia e ParasitologiaSciEL

The repetitive cytoskeletal protein H49 of Trypanosoma cruzi is a calpain-like protein located at the flagellum attachment zone

Paracoccidioides brasiliensis causes paracoccidioidomycosis, a systemic mycosis in Latin America. Formamidases hydrolyze formamide, putatively plays a role infungal nitrogen metabolism. An abundant 45-kDa protein was identified as the P. brasiliensis formamidase. In this study, recombinant formamidase was over-expressed in bacteria and a polyclonal antibody to this protein was produced. Weidentified a 180-kDa protein species reactive to the antibody produced in miceagainst the P. brasiliensis recombinant purified formamidase of 45 kDa. The180-kDa purified protein yielded a heat-denatured species of 45 kDa. Both protein species of 180 and 45 kDa were identified as formamidase by peptide massfinger printing using MS. The identical mass spectra generated by the 180 and the45-kDa protein species indicated that the fungal formamidase is most likely homotetrameric in its native conformation. Furthermore, the purified formami-dase migrated as a protein of 191 kDa in native polyacrylamide gel electrophoresis, thus revealing that the enzyme forms a homotetrameric structure in its native state. This enzyme is present in the fungus cytoplasm and the cell wall. Use of a yeast two-hybrid system revealed cell wall membrane proteins, in addition to cytosolic proteins interacting with formamidase. These data provide new insights intoformamidase structure as well as potential roles for formamidase and its interaction partners in nitrogen metabolism

5to. Congreso Internacional de Ciencia, Tecnología e Innovación para la Sociedad. Memoria académica

El V Congreso Internacional de Ciencia, Tecnología e Innovación para la Sociedad, CITIS 2019, realizado del 6 al 8 de febrero de 2019 y organizado por la Universidad Politécnica Salesiana, ofreció a la comunidad académica nacional e internacional una plataforma de comunicación unificada, dirigida a cubrir los problemas teóricos y prácticos de mayor impacto en la sociedad moderna desde la ingeniería. En esta edición, dedicada a los 25 años de vida de la UPS, los ejes temáticos estuvieron relacionados con la aplicación de la ciencia, el desarrollo tecnológico y la innovación en cinco pilares fundamentales de nuestra sociedad: la industria, la movilidad, la sostenibilidad ambiental, la información y las telecomunicaciones. El comité científico estuvo conformado formado por 48 investigadores procedentes de diez países: España, Reino Unido, Italia, Bélgica, México, Venezuela, Colombia, Brasil, Estados Unidos y Ecuador. Fueron recibidas un centenar de contribuciones, de las cuales 39 fueron aprobadas en forma de ponencias y 15 en formato poster. Estas contribuciones fueron presentadas de forma oral ante toda la comunidad académica que se dio cita en el Congreso, quienes desde el aula magna, el auditorio y la sala de usos múltiples de la Universidad Politécnica Salesiana, cumplieron respetuosamente la responsabilidad de representar a toda la sociedad en la revisión, aceptación y validación del conocimiento nuevo que fue presentado en cada exposición por los investigadores. Paralelo a las sesiones técnicas, el Congreso contó con espacios de presentación de posters científicos y cinco workshops en temáticas de vanguardia que cautivaron la atención de nuestros docentes y estudiantes. También en el marco del evento se impartieron un total de ocho conferencias magistrales en temas tan actuales como la gestión del conocimiento en la universidad-ecosistema, los retos y oportunidades de la industria 4.0, los avances de la investigación básica y aplicada en mecatrónica para el estudio de robots de nueva generación, la optimización en ingeniería con técnicas multi-objetivo, el desarrollo de las redes avanzadas en Latinoamérica y los mundos, la contaminación del aire debido al tránsito vehicular, el radón y los riesgos que representa este gas radiactivo para la salud humana, entre otros

Study on the processing of the surface glycoprotein of 82 kDa(GP82) from metacyclic trypomastigotes of Trypanosoma cruzi

Os tripomastigotas metaciclicos de Trypanosoma cruzi sintetizam uma glicoproteina de superficie estagio-especifica de 82 kDa (GP82) que esta envolvida na entrada do parasita nas celulas hospedeiras. A GP82 encontra-se ligada a superficie celular por uma ancora de glicosilfosfatidilinositol (GPI). As proteinas ligadas por GPI sao sintetizadas com uma extremidade C-terminal que e substituida por uma ancora GPI numa reacao de transamidacao que acontece pos-traducionalmente. A sequencia da GP82 que determina a adicao da ancora GPI contem 25 aminoacidos distribuidos no sitio w, seguindo-se uma sequencia espacadora (7 aminoacidos) e uma regiao mais hidrofobica (15 aminoacidos). O sitio w, reponsavel pela clivagem e adicao da ancora GPI, e composto por 3 aminoacidos: o aminoacido w ao qual a ancora GPI e tranferida, e Asp; o aminoacido w+1 e Gly e o aminoacido w+2 e Ser. Visando determinar experimentalmente a sequencia para ancoragem por GPI em T. cruzi, fizemos uma mutacao no putativo sitio de clivagem e adicao (sitio w) da ancora. Por meio de mutacao sitio-dirigida foi gerada uma substituicao do aminoacido no sitio w (posicao 492), onde o codon GAC foi trocado por TCC, assim o motivo de clivagem e adicao Asp-Gly-Ser presente na proteina nativa foi substituido por Ser-Gly-Ser. Para avaliar o processamento de uma proteina com sinal defectiva para adicao de GPI, geramos uma GP82 truncada, eliminando todo o sinal C-terminal incluindo-se o sitio c). As duas construcoes foram clonadas no vetor pTEX e inseridas em epimastigotas (cepa G) por meio de eletroporacao. A incorporacao do plasmidio foi confirmada por analise de Southern blot apos diGestão com Xho I, e a transcricao dos genes transfectados por analise de northem blot. A traducao dos genes exogenos foi analisada por western blot empregando um anticorpo monoclonal especifico para GP82 (MAb-3F6), e a localizacao celular dos produtos traduzidos foi feita por imunofluorescencia e...(au)BV UNIFESP: Teses e dissertaçõe

Soluciones corporativas de inteligencia de negocios en las pequeñas y medianas empresas

The objective was based on determining the intelligent system that adjusts to the operation of Comercializadora "Cordero", located in Azogues, Cañar province, Ecuador. The method is non-experimental and of mixed approach. It was discovered that there are a small number of SMEs that use the BI system, and those that use this technology, most use the balanced scorecard tool, which is aligned in a greater percentage to the financial components, clients, internal processes and learning in organizations. The study on business intelligence shows the administration that this technological tool allows a better analysis of the information in a faster way, also significantly improved the quality of the information, making the reports generated from it more reliable, providing support for decision making in companies.El objetivo se basó en determinar el sistema inteligente que se ajuste a la operatividad de Comercializadora “Cordero”, ubicada en Azogues, provincia de Cañar, Ecuador. El método es de tipo no experimental y de enfoque mixto. Se descubrió que existe un número reducido de pymes que utilizan el sistema BI, y las que utilizan esta tecnología la mayoría emplea la herramienta de cuadro de mando integral, la misma que se alinea en mayor porcentaje a los compones financiero, clientes, procesos internos y aprendizaje en las organizaciones. El estudio sobre la inteligencia de negocios demuestra a la administración que esta herramienta tecnológica permite un mejor análisis de la información de forma más rápida, asimismo mejoró significativamente la calidad de la información haciendo más confiables los reportes generados a partir de ella, brindando un soporte para la toma de decisiones en las empresas

Lysophosphatidylcholine Triggers TLR2- and TLR4- Mediated Signaling Pathways but Counteracts LPSInduced NO Synthesis in Peritoneal Macrophages by Inhibiting NF-κB Translocation and MAPK/ERK Phosphorylation

Made available in DSpace on 2015-09-28T13:02:39Z (GMT). No. of bitstreams: 2 license.txt: 1914 bytes, checksum: 7d48279ffeed55da8dfe2f8e81f3b81f (MD5) igor_almeida_etal_IOC_2013.pdf: 680569 bytes, checksum: 68dcc939113bc5eb10c5deee819a7ff8 (MD5) Previous issue date: 2013Universidade Federal do Rio de Janeiro. Centro de Ciências da Saúde. Instituto de Bioquímica Médica. Programa de Biologia Molecular e Biotecnologia. Instituto Nacional de Ciência e Tecnologia em Entomologia Molecular- INCT-EM. Rio de Janeiro, RJ, Brasil.Universidade Federal do Rio de Janeiro. Centro de Ciências da Saúde. Instituto de Bioquímica Médica. Programa de Biologia Molecular e Biotecnologia. Instituto Nacional de Ciência e Tecnologia em Entomologia Molecular- INCT-EM. Rio de Janeiro, RJ, Brasil.University of Texas at El Paso. Department of Biological Sciences. The Border Biomedical Research Center. El Paso, Texas, USA.University of Texas at El Paso. Department of Biological Sciences. The Border Biomedical Research Center. El Paso, Texas, USA / Universidade de São Paulo. Faculdade de Medicina de Ribeirão Preto. Departamento de Biologia Celular e Molecular Patogênicos. Ribeirão Preto, SP, Brasil.University of Texas at El Paso. Department of Biological Sciences. The Border Biomedical Research Center. El Paso, Texas, USA.University of Texas at El Paso. Department of Biological Sciences. The Border Biomedical Research Center. El Paso, Texas, USA / Universidade de São Paulo. Faculdade de Medicina de Ribeirão Preto. Departamento de Biologia Celular e Molecular Patogênicos. Ribeirão Preto, SP, Brasil.Fundação Oswaldo Cruz. Instituto Oswaldo Cruz. Laboratório de Imunofarmacologia. Rio de Janeiro, RJ, Brasil.Universidade Federal do Rio de Janeiro. Centro de Ciências da Saúde. Instituto de Biofísica Carlos Chagas Filho. Laboratório de Parasitologia Molecular. Rio de Janeiro, RJ, Brasil.Universidade Federal do Rio de Janeiro. Centro de Ciências da Saúde. Instituto de Bioquímica Médica. Programa de Biologia Molecular e Biotecnologia. Instituto Nacional de Ciência e Tecnologia em Entomologia Molecular- INCT-EM. Rio de Janeiro, RJ, Brasil.Fundação Oswaldo Cruz. Instituto Oswaldo Cruz. Laboratório de Imunofarmacologia. Rio de Janeiro, RJ, Brasil.Universidade Federal do Rio de Janeiro. Centro de Ciências da Saúde. Instituto de Bioquímica Médica. Programa de Biologia Molecular e Biotecnologia. Instituto Nacional de Ciência e Tecnologia em Entomologia Molecular- INCT-EM. Rio de Janeiro, RJ, Brasil.Background: Lysophosphatidylcholine (LPC) is the main phospholipid component of oxidized low-density lipoprotein (oxLDL) and is usually noted as a marker of several human diseases, such as atherosclerosis, cancer and diabetes. Some studies suggest that oxLDL modulates Toll-like receptor (TLR) signaling. However, effector molecules that are present in oxLDL particles and can trigger TLR signaling are not yet clear. LPC was previously described as an attenuator of sepsis and as an immune suppressor. In the present study, we have evaluated the role of LPC as a dual modulator of the TLR-mediated signaling pathway. Methodology/Principal Findings: HEK 293A cells were transfected with TLR expression constructs and stimulated with LPC molecules with different fatty acid chain lengths and saturation levels. All LPC molecules activated both TLR4 and TLR2-1 signaling, as evaluated by NF-қB activation and IL-8 production. These data were confirmed by Western blot analysis of NF-қB translocation in isolated nuclei of peritoneal murine macrophages. However, LPC counteracted the TLR4 signaling induced by LPS. In this case, NF-қB translocation, nitric oxide (NO) synthesis and the expression of inducible nitric oxide synthase (iNOS) were blocked. Moreover, LPC activated the MAP Kinases p38 and JNK, but not ERK, in murine macrophages. Interestingly, LPC blocked LPS-induced ERK activation in peritoneal macrophages but not in TLR-transfected cells. Conclusions/Significance: The above results indicate that LPC is a dual-activity ligand molecule. It is able to trigger a classical proinflammatory phenotype by activating TLR4- and TLR2-1-mediated signaling. However, in the presence of classical TLR ligands, LPC counteracts some of the TLR-mediated intracellular responses, ultimately inducing an anti-inflammatory phenotype; LPC may thus play a role in the regulation of cell immune responses and disease progression