244 research outputs found

    The Quality of Student Services Provided by the Deanship of Student Affairs at Sultan Qaboos University

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    This study aimed to investigate the quality of student services provided by the Deanship of Student Affairs at the Sultan Qaboos University. The study sample consisted of 610 students. Data were collected using a questionnaire consisting of 59 items distributed in seven areas which are: social services, housing services, and food services, and counseling and religious guidance services, cultural and artistic services, sports activities, and sustainable training services. The results showed that the highest mean of the responses is in the counseling and religious guidance 3.79, while the lowest mean is for the area of student food services 2.82.the Results of (MANOVA) showed that the quality of services provided by the Deanship of Student Affairs for students for female was a higher level compared with males in the areas of social services, housing services and sustainable training services. As for the results on the year variable, the result of the study revealed that there are statistically significant differences (α=0.05) related to the field of social services in favor of the second year students. Also the results showed that there are statistically significant differences related to students' points of view in humanities colleges in the areas of social services 3.37, and sustainable training 3.27, while in the area of religious guidance services it is in favor of scientific colleges 3.87. Based on the results of this study, many recommendations and suggestions were developed

    Outline of fungi and fungus-like taxa

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    This article provides an outline of the classification of the kingdom Fungi (including fossil fungi. i.e. dispersed spores, mycelia, sporophores, mycorrhizas). We treat 19 phyla of fungi. These are Aphelidiomycota, Ascomycota, Basidiobolomycota, Basidiomycota, Blastocladiomycota, Calcarisporiellomycota, Caulochytriomycota, Chytridiomycota, Entomophthoromycota, Entorrhizomycota, Glomeromycota, Kickxellomycota, Monoblepharomycota, Mortierellomycota, Mucoromycota, Neocallimastigomycota, Olpidiomycota, Rozellomycota and Zoopagomycota. The placement of all fungal genera is provided at the class-, order- and family-level. The described number of species per genus is also given. Notes are provided of taxa for which recent changes or disagreements have been presented. Fungus-like taxa that were traditionally treated as fungi are also incorporated in this outline (i.e. Eumycetozoa, Dictyosteliomycetes, Ceratiomyxomycetes and Myxomycetes). Four new taxa are introduced: Amblyosporida ord. nov. Neopereziida ord. nov. and Ovavesiculida ord. nov. in Rozellomycota, and Protosporangiaceae fam. nov. in Dictyosteliomycetes. Two different classifications (in outline section and in discussion) are provided for Glomeromycota and Leotiomycetes based on recent studies. The phylogenetic reconstruction of a four-gene dataset (18S and 28S rRNA, RPB1, RPB2) of 433 taxa is presented, including all currently described orders of fungi.Fil: Wijayawardene, N. N.. Qujing Normal University; ChinaFil: Hyde, K. D.. Mae Fah Luang University; TailandiaFil: Al-Ani, L. K. T.. University of Baghdad; IraqFil: Tedersoo, L.. University of Tartu; EstoniaFil: Haelewaters, D.. University of South Bohemia; República Checa. Purdue University; Estados Unidos. Universidad Autónoma de Chiriquí; PanamáFil: Becerra, Alejandra Gabriela. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Instituto Multidisciplinario de Biología Vegetal. Universidad Nacional de Córdoba. Facultad de Ciencias Exactas Físicas y Naturales. Instituto Multidisciplinario de Biología Vegetal; ArgentinaFil: Schnittler, M.. Ernst Moritz Arndt University Greifswald; AlemaniaFil: Shchepin, O. N.. The Komarov Botanical Institute of the Russian Academy of Sciences; RusiaFil: Novozhilov, Y. K.. The Komarov Botanical Institute of the Russian Academy of Sciences; RusiaFil: Silva-Filho, A.G. S.. Universidade Federal do Rio Grande do Norte; BrasilFil: Gentekaki, E.. Mae Fah Luang University; TailandiaFil: Liu, P.. Jilin Agricultural University; ChinaFil: Cavender, J. C.. Ohio University; Estados UnidosFil: Kang, Y.. Guizhou Medical University; ChinaFil: Mohammad, S.. Iranian Research Organization for Science and Technology; IránFil: Zhang, L. F.. Qujing Normal University; ChinaFil: Xu, R. F.. Qujing Normal University; ChinaFil: Li, Y. M.. Qujing Normal University; ChinaFil: Dayarathne, M. C.. Guizhou University; ChinaFil: Ekanayaka, A. H.. Mae Fah Luang University; TailandiaFil: Wen, T. C.. Guizhou University; ChinaFil: Deng, C. Y.. Guizhou Academy of Science; ChinaFil: Pereira, O. L.. Universidade Federal de Viçosa; BrasilFil: Navathe, S.. Agharkar Research Institute; IndiaFil: Hawksworth, D. L.. The Natural History Museum; Reino UnidoFil: Fan, X. L.. Beijing Forestry University; ChinaFil: Dissanayake, L. S.. Guizhou University; ChinaFil: Kuhnert, E.. Leibniz University Hannover; AlemaniaFil: Grossart, H. P.. Leibnitz Institute of Freshwater Ecology and Inland Fisheries; AlemaniaFil: Thines, M.. Senckenberg Biodiversity and Climate Research Centre; Alemani

    SPARC 2018 Internationalisation and collaboration : Salford postgraduate annual research conference book of abstracts

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    Welcome to the Book of Abstracts for the 2018 SPARC conference. This year we not only celebrate the work of our PGRs but also the launch of our Doctoral School, which makes this year’s conference extra special. Once again we have received a tremendous contribution from our postgraduate research community; with over 100 presenters, the conference truly showcases a vibrant PGR community at Salford. These abstracts provide a taster of the research strengths of their works, and provide delegates with a reference point for networking and initiating critical debate. With such wide-ranging topics being showcased, we encourage you to take up this great opportunity to engage with researchers working in different subject areas from your own. To meet global challenges, high impact research inevitably requires interdisciplinary collaboration. This is recognised by all major research funders. Therefore engaging with the work of others and forging collaborations across subject areas is an essential skill for the next generation of researchers

    SPARC 2016 Salford postgraduate annual research conference book of abstracts

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    The N-Terminal Domain and Glycosomal Localization of Leishmania Initial Acyltransferase LmDAT Are Important for Lipophosphoglycan Synthesis

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    Ether glycerolipids of Leishmania major are important membrane components as well as building blocks of various virulence factors. In L. major, the first enzyme of the ether glycerolipid biosynthetic pathway, LmDAT, is an unusual, glycosomal dihydroxyacetonephosphate acyltransferase important for parasite's growth and survival during the stationary phase, synthesis of ether lipids, and virulence. The present work extends our knowledge of this important biosynthetic enzyme in parasite biology. Site-directed mutagenesis of LmDAT demonstrated that an active enzyme was critical for normal growth and survival during the stationary phase. Deletion analyses showed that the large N-terminal extension of this initial acyltransferase may be important for its stability or activity. Further, abrogation of the C-terminal glycosomal targeting signal sequence of LmDAT led to extraglycosomal localization, did not impair its enzymatic activity but affected synthesis of the ether glycerolipid-based virulence factor lipophosphoglycan. In addition, expression of this recombinant form of LmDAT in a null mutant of LmDAT did not restore normal growth and survival during the stationary phase. These results emphasize the importance of this enzyme's compartmentalization in the glycosome for the generation of lipophosphoglycan and parasite's biology

    Leishmania amazonensis Arginase Compartmentalization in the Glycosome Is Important for Parasite Infectivity

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    In Leishmania, de novo polyamine synthesis is initiated by the cleavage of L-arginine to urea and L-ornithine by the action of arginase (ARG, E.C. 3.5.3.1). Previous studies in L. major and L. mexicana showed that ARG is essential for in vitro growth in the absence of polyamines and needed for full infectivity in animal infections. The ARG protein is normally found within the parasite glycosome, and here we examined whether this localization is required for survival and infectivity. First, the localization of L. amazonensis ARG in the glycosome was confirmed in both the promastigote and amastigote stages. As in other species, arg− L. amazonensis required putrescine for growth and presented an attenuated infectivity. Restoration of a wild type ARG to the arg− mutant restored ARG expression, growth and infectivity. In contrast, restoration of a cytosol-targeted ARG lacking the glycosomal SKL targeting sequence (argΔSKL) restored growth but failed to restore infectivity. Further study showed that the ARGΔSKL protein was found in the cytosol as expected, but at very low levels. Our results indicate that the proper compartmentalization of L. amazonensis arginase in the glycosome is important for enzyme activity and optimal infectivity. Our conjecture is that parasite arginase participates in a complex equilibrium that defines the fate of L-arginine and that its proper subcellular location may be essential for this physiological orchestration

    Mast cell tryptase stimulates myoblast proliferation; a mechanism relying on protease-activated receptor-2 and cyclooxygenase-2

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    <p>Abstract</p> <p>Background</p> <p>Mast cells contribute to tissue repair in fibrous tissues by stimulating proliferation of fibroblasts through the release of tryptase which activates protease-activated receptor-2 (PAR-2). The possibility that a tryptase/PAR-2 signaling pathway exists in skeletal muscle cell has never been investigated. The aim of this study was to evaluate whether tryptase can stimulate myoblast proliferation and determine the downstream cascade.</p> <p>Methods</p> <p>Proliferation of L6 rat skeletal myoblasts stimulated with PAR-2 agonists (tryptase, trypsin and SLIGKV) was assessed. The specificity of the tryptase effect was evaluated with a specific inhibitor, APC-366. Western blot analyses were used to evaluate the expression and functionality of PAR-2 receptor and to assess the expression of COX-2. COX-2 activity was evaluated with a commercial activity assay kit and by measurement of PGF<sub>2</sub>α production. Proliferation assays were also performed in presence of different prostaglandins (PGs).</p> <p>Results</p> <p>Tryptase increased L6 myoblast proliferation by 35% above control group and this effect was completely inhibited by APC-366. We confirmed the expression of PAR-2 receptor <it>in vivo </it>in skeletal muscle cells and in satellite cells and <it>in vitro </it>in L6 cells, where PAR-2 was found to be functional. Trypsin and SLIGKV increased L6 cells proliferation by 76% and 26% above control, respectively. COX-2 activity was increased following stimulation with PAR-2 agonist but its expression remained unchanged. Inhibition of COX-2 activity by NS-398 abolished the stimulation of cell proliferation induced by tryptase and trypsin. Finally, 15-deoxy-Δ-<sup>12,14</sup>-prostaglandin J<sub>2 </sub>(15Δ-PGJ<sub>2</sub>), a product of COX-2-derived prostaglandin D<sub>2</sub>, stimulated myoblast proliferation, but not PGE<sub>2 </sub>and PGF<sub>2</sub>α.</p> <p>Conclusions</p> <p>Taken together, our data show that tryptase can stimulate myoblast proliferation and this effect is part of a signaling cascade dependent on PAR-2 activation and on the downstream activation of COX-2.</p
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