ANTI-INFLAMMATORY ACTIVITY OF MANILKARA ZAPOTA LEAF EXTRACT

Objective: Manilkara zapota is a medicinal plant which is native to Mexico and Central America, and widely distributed in India. Various parts of this plant are traditionally used for treatment of several diseases, including inflammation-associated ailments. The main aim of the present study is to evaluate the anti-inflammatory potential of ethyl acetate and methanolic extracts of M. zapota leaf.Methods: In vitro secretary phospholipase A2 (PLA2) and 5-Lipoxygenase (5-LOX) assays and In vivo studies using carrageenan induced rat paw edema model were performed to assess the anti-inflammatory activity of M. zapota leaf extracts.Results: In vitro studies suggest that M. zapota leaf extracts exhibited significant SPLA2 and 5-LOX inhibitory activities. In in vivo studies M. zapota leaf extracts showed dose dependent inhibition of carrageenan induced paw edema in rats. The anti-inflammatory activity of ethyl acetate leaf extract was superior to methanolic extract.Conclusion: This study concluded that ethyl acetate leaf extract of M. zapotaexhibited significant anti-inflammatory activity and warranted further investigation to isolate and identify the components.Â

Kex2 protease converts the endoplasmic reticulum α1,2-mannosidase of Candida albicans into a soluble cytosolic form

Cytosolic α-mannosidases are glycosyl hydrolases that participate in the catabolism of cytosolic free N-oligosaccharides. Two soluble α-mannosidases (E-I and E-II) belonging to glycosyl hydrolases family 47 have been described in Candida albicans. We demonstrate that addition of pepstatin A during the preparation of cell homogenates enriched α-mannosidase E-I at the expense of E-II, indicating that the latter is generated by proteolysis during cell disruption. E-I corresponded to a polypeptide of 52 kDa that was associated with mannosidase activity and was recognized by an anti-α1,2-mannosidase antibody. The N-mannan core trimming properties of the purified enzyme E-I were consistent with its classification as a family 47 α1,2-mannosidase. Differential density-gradient centrifugation of homogenates revealed that α1,2-mannosidase E-I was localized to the cytosolic fraction and Golgi-derived vesicles, and that a 65 kDa membrane-bound α1,2-mannosidase was present in endoplasmic reticulum and Golgi-derived vesicles. Distribution of α-mannosidase activity in a kex2Δ null mutant or in wild-type protoplasts treated with monensin demonstrated that the membrane-bound α1,2-mannosidase is processed by Kex2 protease into E-I, recognizing an atypical cleavage site of the precursor. Analysis of cytosolic free N-oligosaccharides revealed that cytosolic α1,2-mannosidase E-I trims free Man8GlcNAc2 isomer B into Man7GlcNAc2 isomer B. This is believed to be the first report demonstrating the presence of soluble α1,2-mannosidase from the glycosyl hydrolases family 47 in a cytosolic compartment of the cell

Innovación del Diseño para el Desarrollo Social

Una labor de síntesis alrededor de la gran temática de este libro que surge a partir de una serie de reflexiones y propuestas encaminadas desde la innovación del diseño para el desarrollo social, refleja una invitación al lector para enunciar a partir de su lectura nuevas discusiones sobre el quehacer del diseño con una perspectiva de innovación para este tipo de desarrollo, es pues este texto una invitación a enunciar nuevos retos y diálogos partiendo de reconocer al desarrollo social como uno de los pilares fundamentales desde la Organización de las Naciones Unidas (ONU) como parte fundamental para garantizar el mejoramiento de la vida de las personas. Desde la disciplina del diseño y retomado como eje para su discusión se pretendería establecer una serie de reflexiones y acciones que permitan atender situaciones para grupos minoritarios y vulnerables, así como apoyar esfuerzos encaminados a mejorar la calidad de vida de los integrantes de grupos y sociedades establecidas y recuperar el patrimonio cultural como parte fundamental de las identidades culturales y por tanto de la historia de la humanidad.A lo largo de la historia, el diseño, en cualquiera de sus manifestaciones, ha estado presente en todos los ámbitos. Se ha convertido en una disciplina que evoluciona al ritmo de las sociedades, que se pone al servicio de las necesidades de mercado pero también de las que requieren un abordaje distinto, observadas desde una mirada que concierne a lo social, entendido éste como lo que se reproduce o se instaura en el colectivo, en el grupo, en las comunidades, en las sociedades como parte significativa de sus cotidianeidades. El Diseño desde esta perspectiva acompaña al ser humano produciendo una significación de los objetos como parte fundamental de sus vidas, que transforma una realidad deseada en una realidad concreta, de aquí la importancia de crear una conciencia social para la praxis laboral de esta disciplina. En este sentido el campo profesional, académico y de investigación del diseño debe ocuparse de crear, difundir y divulgar el quehacer de la misma, manifestando un equilibrio entre conciencia, racionalidad y la realidad. Desde el contexto planteado, la Universidad Autónoma del Estado de México, a través de su Facultad de Arquitectura y Diseño presenta en esta obra una serie de reflexiones en torno al papel que desempeña el diseño humanístico, científico y tecnológico desde un enfoque de vanguardia e innovación para el desarrollo social, como resultado de la experiencia vertida en el Coloquio Internacional de Diseño que organiza éste año este espacio académico, en donde cada una de las aportaciones refleja la experiencia de cada uno de sus participantes; con base en ello, el presente libro integrado por una compilación de trabajos ofrece descripciones, análisis y propuestas que contribuyen a la solución de problemas procurando un desarrollo social

CARACTERIZACIÓN MOLECULAR DE AISLADOS DE Sclerotium cepivorum MEDIANTE ANÁLISIS DEL POLIMORFISMO DE LOS FRAGMENTOS AMPLIFICADOS AL AZAR CARACTERIZACIÓN MOLECULAR DE AISLADOS DE Sclerotium cepivorum MEDIANTE ANÁLISIS DEL POLIMORFISMO DE LOS FRAGMENTOS AMPLIFICADOS AL AZAR

Sclerotium cepivorum is the etiologic agent of garlic "white rot". Knowledge of genetic variability of the fungus may help to design efficient strategies for its control. For this study, 47 isolates obtained from Aguascalientes, Guanajuato and Zacatecas as well as 7 reference strains were used. Morphological characterization was that established for this organism. PCR amplification of ribosomal 18S gene generated a DNA fragment of a size close to 2.2 Kb in all isolates and reference strains, as compared to that of 1.8 Kb amplified in control fungi. Variability was analyzed by Random Amplified Polymorphism Distance (RAPD). Isolates exhibited a similar gene pattern with an average dissimilitud of 9.4%. Some of the bands identified here can be useful as molecular markers in identification studies of this plant pathogen. Dendogram analysis of data revealed a tendency of isolates to group according to their geographic procedence.Sclerotium cepivorum es el agente causal de la "pudrición blanca" del ajo. El conocer su variabilidad genética permitirá buscar estrategias de control mas eficientes. Se utilizaron 47 aislados de S. cepivorum provenientes de Aguascalientes, Guanajuato, Zacatecas y 7 cepas de referencia. El análisis morfológico correspondió al establecido para este hongo. Se amplificó el gen ribosomal 18S dando un tamaño cercano a 2.2 kb en todos los aislados y cepas de S. cepivorum, en los hongos control fue de aproximadamente 18 kb. El grado de variabilidad se analizó por medio del Polimorfismo de los Fragmentos Amplificados al Azar (RAPD). Los aislados de S. cepivorum dieron un patrón génico similar, pero muy diferente al que muestran los otros hongos fitopatógenos. La disimilitud genética promedio fue de 9.4%. Se proponen algunas bandas como marcadores moleculares para identificar al fitopatógeno. En el dendograma se aprecia que hay tendencia de los aislados a agruparse según el estado de donde provienen.</p

Heterologous expression and biochemical characterization of an 1,2-mannosidase encoded by the Candida albicans MNS1 gene

Protein glycosylation pathways, commonly found in fungal pathogens, offer an attractive new area of study for the discovery of antifungal targets. In particular, these post-translational modifications are required for virulence and proper cell wall assembly in Candida albicans , an opportunistic human pathogen. The C. albicans MNS1 gene is predicted to encode a member of the glycosyl hydrolase family 47, with 1,2-mannosidase activity. In order to characterise its activity, we first cloned the C. albicans MNS1 gene into Escherichia coli, then expressed and purified the enzyme. The recombinant Mns1 was capable of converting a Man9GlcNAc2 N-glycan core into Man8GlcNAc2 isomer B, but failed to process a Man5GlcNAc2-Asn N-oligosaccharide. These properties are similar to those displayed by Mns1 purified from C. albicansmembranes and strongly suggest that the enzyme is an α1,2-mannosidase that is localised to the endoplasmic reticulum and involved in the processing of N-linked mannans. Polyclonal antibodies specifically raised against recombinant Mns1 also immunoreacted with the soluble α1,2-mannosidases E-I and E-II, indicating that Mns1 could share structural similarities with both soluble enzymes. Due to the high degree of similarity between the members of family 47, it is conceivable that these antibodies may recognise α1,2-mannosidases in other biological systems as well

Developmental regulation of cmp1, a gene encoding a multidomain conidiospore surface protein of Trichoderma

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The Sporothrix schenckii Gene Encoding for the Ribosomal Protein L6 Has Constitutive and Stable Expression and Works as an Endogenous Control in Gene Expression Analysis

Sporothrix schenckii is one of the causative agents of sporotrichosis, a worldwide-distributed mycosis that affects humans and other mammals. The interest in basic and clinical features of this organism has significantly increased in the last years, yet little progress in molecular aspects has been reported. Gene expression analysis is a set of powerful tools that helps to assess the cell response to changes in the extracellular environment, the genetic networks controlling metabolic pathways, and the adaptation to different growth conditions. Most of the quantitative methodologies used nowadays require data normalization, and this is achieved measuring the expression of endogenous control genes. Reference genes, whose expression is assumed to suffer minimal changes regardless the cell morphology, the stage of the cell cycle or the presence of harsh extracellular conditions are commonly used as controls in Northern blotting assays, microarrays, and semi-quantitative or quantitative RT-PCR. Since the biology of the organisms is usually species specific, it is difficult to find a reliable group of universal genes that can be used as controls for data normalization in experiments addressing the gene expression, regardless the taxonomic classification of the organism under study. Here, we compared the transcriptional stability of the genes encoding for elongation factor 1A, Tfc1, a protein involved in transcription initiation on Pol III promoters, ribosomal protein L6, histone H2A, β-actin, β-tubulin, glyceraldehyde 3-phosphate dehydrogenase, UAF30, the upstream activating factor 30, and the transcription initiation factor TFIID subunit 10, during the fungal growth in different culture media and cell morphologies. Our results indicated that only the gene encoding for the ribosomal protein L6 showed a stable and constant expression. Furthermore, it displayed not transcriptional changes when S. schenckii infected larvae of Galleria mellonella or interacted with immune cells. Therefore, this gene could be used as control for data normalization in expression assays. As a proof of concept, this gene was used to assess the expression of genes encoding for glycosidases involved in the protein N-linked glycosylation pathway, a histidine kinase whose expression is regulated during the fungal dimorphism, and a glycosidase that participates in sucrose assimilation