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Sent on Friday, 2010 Jun 18Search kinetoplastids OR kinetoplastid OR Kinetoplastida OR "trypanosoma brucei" OR leishmania OR brucei OR leishmaniasis OR "African trypanosomiasis"
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| PubMed Results |
| 1. | Int J Antimicrob Agents. 2010 May 27. [Epub ahead of print]Therapeutic evaluation of free and liposome-loaded furazolidone in experimental visceral leishmaniasis.Tempone AG, Mortara RA, de Andrade HF Jr, Reimão JQ.Laboratory of Applied Toxinology on Antiparasitic Drugs, Department of Parasitology, Instituto Adolfo Lutz, Av. Dr Arnaldo 355, 8 degrees andar, CEP 01246-000 São Paulo, SP, Brazil. AbstractDrug delivery systems are promising pharmaceutical formulations used to improve the therapeutic index of drugs. In this study, we developed a liposomal formulation of furazolidone that targets Leishmania (Leishmania) chagasi amastigotes in a hamster model. Using laser scanning confocal microscopy, it was demonstrated that the liposomal drug co-localised with L. (L.) chagasi amastigotes within macrophages. Liposomal furazolidone administered intraperitoneally at 0.5mg/kg for 12 consecutive days reduced spleen (74%) and liver (32%) parasite burden at a 100-fold lower dose than the free drug. Free furazolidone (50mg/kg) also effectively reduced spleen (82.5%) and liver (85%) parasites; its in vitro activity against promastigotes and intracellular amastigotes demonstrated a high degree of parasite selectivity. Thus, furazolidone, both in the free and liposome-loaded formulation, is an effective inhibitor of L. (L.) chagasi, representing a possible cost-effective drug candidate for the treatment of visceral leishmaniasis. Copyright © 2010 Elsevier B.V. and the International Society of Chemotherapy. All rights reserved. |
| PMID: 20554161 [PubMed - as supplied by publisher] | |
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| 2. | Exp Parasitol. 2010 Jun 5. [Epub ahead of print]Leishmania (Viannia) braziliensis: influence of successive in vitro cultivation o n the expression of promastigote proteinases.Rebello KM, Britto C, Pereira BA, de Pita-Pereira D, Moraes MO, Ferreira AB, Cysne-Finkelstein L, Otto TD, de Castro Cortês LM, da-Silva GG, Alves CR.Laboratório de Biologia Molecular e Doenças Endêmicas - Instituto Oswaldo Cruz, FIOCRUZ - Rio de Janeiro, Brasil. AbstractCysteine proteinases are an important virulence factor in Leishmania parasites. In this study we analyzed the cysteine proteinase expression of infective L. (V.) braziliensis promastigotes, examining the expression induced by successive in vitro passages in culture. We observed that this parasite presents a decrease in its virulence over BALB/c macrophages, after successive passages in culture, but still they present proteinase activity, being capable of hydrolyzing the substrate pGlu-Phe-Leu-p Nitroanilide at pH 7.0. This proteinase activity also decreases in the course of the successive passages. Additionally, the decrease in the amount of CPB proteins following successive passages of promastigotes was verified by immunoblotting assays, using an anti-CPB antiserum. Real Time PCR assays were performed to assess the relative cpb expression when compared to a housekeeping gene in promastigote cDNA preparations from the first, fourth and seventh passages. Interestingly, the data indicate a relative increase in cpb gene transcripts as the promastigotes were maintained under in vitro culture: 2.2 times higher for fourth and 2.7 times higher for seventh passages when compared to the first passage. Thus, the information gathered here shows that the expression of cysteine proteinases is modified during in vitro cultivation of L. (V.) braziliensis promastigotes. Copyright © 2010. Published by Elsevier Inc. |
| PMID: 20553928 [PubMed - as supplied by publisher] | |
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| 3. | Mol Biochem Parasitol. 2010 May 26. [Epub ahead of print]Elevated levels of tryparedoxin peroxidase in antimony unresponsiv e Leishmania donovani field isolates.Wyllie S, Mandal G, Singh N, Sundar S, Fairlamb AH, Chatterjee M.Division of Biological Chemistry and Drug Discovery, College of Life Sciences, University of Dundee, Dow Street, Dundee DD1 5EH, Scotland, U.K. AbstractEnhancement of the anti-oxidant metabolism of Leishmania parasites, dependent upon the unique dithiol trypanothione, has been implicated in laboratory-generated antimony resistance. Here, the role of the trypanothione-dependent anti-oxidant pathway is studied in antimony-resistant clinical isolates. Elevated levels of tryparedoxin and tryparedoxin peroxidase, key enzymes in hydroperoxide detoxification, were observed in antimonial resistant parasites resulting in an increased metabolism of peroxides. These data suggest that enhanced anti-oxidant defences may play significant in clinical resistance to antimonials. Copyright © 2010. Published by Elsevier B.V. |
| PMID: 20553768 [PubMed - as supplied by publisher] | |
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| 4. | J Eur Acad Dermatol Venereol. 2010 Jun 9. [Epub ahead of print]The p ractical use of cytology for diagnosis in dermatology.Ruocco E, Brunetti G, Del Vecchio M, Ruocco V.Department of Dermatology, 2nd University of Naples, Naples, Italy. AbstractAbstract Exfoliative cytology for diagnostic purposes is rarely used in Dermatology despite the rapid and reliable results which this procedure can offer in many clinical conditions. This simple procedure may prove advantageous in a wide range of skin diseases, including genodermatoses (Hailey-Hailey disease), infections (mainly herpetic infections, molluscum contagiosum, leishmaniasis), immune disorders (early oral pemphigus) and tumours (basal and squamous cell carcinomas, Paget disease, erythroplasia of Queyrat, and others). The specific circumstances where cytological examination provides a very helpful and practical aid to confirmation or exclusion of a clinically suspected diagnosis are briefly reviewed. Cytological patterns, along with some technical hints on how to take and stain Tzanck smears correctly, are described in connection with the diseases considered. |
| PMID: 20553359 [PubMed - as supplied by publisher] | |
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| 5. | J Biol Chem. 2010 May 28;285(22):16643-50. Epub 2010 Apr 2.Stress-induced synthesis of phosphatidylinositol 3-phosphate in mycobacteria.Morita YS, Yamaryo-Botte Y, Miyanagi K, Callaghan JM, Patterson JH, Crellin PK, Coppel RL, Billman-Jacobe H, Kinoshita T, McConville MJ.Department of Biochemistry and Molecular Biology, Bio21 Molecular Science and Biotechnology Institute, Parkville, Victoria 3010, Australia. ymorita@biken.osaka-u.ac.jp AbstractPhosphoinositides play key roles in regulating membrane dynamics and intracellular signaling in eukaryotic cells. However, comparable lipid-based signaling pathways have not been identified in bacteria. Here we show that Mycobacterium smegmatis and other Actinomycetes bacteria can synthesize the phosphoinositide, phosphatidylinositol 3-phosphate (PI3P). This lipid was transiently labeled with [(3)H]inositol. Sensitivity of the purified lipid to alkaline phosphatase, headgroup analysis by high-pressure liquid chromatography, and mass spectrometry demonstrated that it had the structure 1,2-[tuberculostearoyl, octadecenoyl]-sn-glycero 3-phosphoinositol 3-phosphate. Synthesis of PI3P was elevated by salt stress but not by exposure to high concentrations of non-ionic solutes. Synthesis of PI3P in a cell-free system was stimulated by the synthesis of CDP-diacylglycerol, a lipid substrate for phosphatidylinositol (PI) biosynthesis, suggesting that efficient cell-free PI3P synthesis is dependent on de novo PI synthesis. In vitro experiments further indicated that the rapid turnover of this lipid was mediated, at least in part, by a vanadate-sensitive phosphatase. This is the first example of de novo synthesis of PI3P in bacteria, and the transient synthesis in response to environmental stimuli suggests that some bacteria may have evolved similar lipid-mediated signaling pathways to those observed in eukaryotic cells. |
| PMID: 20364020 [PubMed - indexed for MEDLINE] | |
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