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Relevant bibliographies by topics / Glycosomes

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Academic literature on the topic 'Glycosomes'

Author: Grafiati

Published: 24 April 2022

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Journal articles on the topic "Glycosomes"

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Flaspohler, J. A., W. L. Rickoll, S. M. Beverley, and M. Parsons. "Functional identification of a Leishmania gene related to the peroxin 2 gene reveals common ancestry of glycosomes and peroxisomes." Molecular and Cellular Biology 17, no. 3 (1997): 1093–101. http://dx.doi.org/10.1128/mcb.17.3.1093.

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Glycosomes are membrane-bounded microbody organelles that compartmentalize glycolysis as well as other important metabolic processes in trypanosomatids. The compartmentalization of these enzymatic reactions is hypothesized to play a crucial role in parasite physiology. Although the metabolic role of glycosomes differs substantially from that of the peroxisomes that are found in other eukaryotes, similarities in signals targeting proteins to these organelles suggest that glycosomes and peroxisomes may have evolved from a common ancestor. To examine this hypothesis, as well as gain insights into

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Sommer, J. M., J. A. Thissen, M. Parsons, and C. C. Wang. "Characterization of an in vitro assay for import of 3-phosphoglycerate kinase into the glycosomes of Trypanosoma brucei." Molecular and Cellular Biology 10, no. 9 (1990): 4545–54. http://dx.doi.org/10.1128/mcb.10.9.4545.

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Glycosomes are microbody organelles found in kinetoplastida, where they serve to compartmentalize the enzymes of the glycolytic pathway. In order to identify the mechanism by which these enzymes are targeted to the glycosome, we have modified the in vitro import assay developed by Dovey et al. (Proc. Natl. Acad. Sci. USA 85:2598-2602, 1988). This assay measures the uptake of in vitro-translated Trypanosoma brucei glycosomal 3-phosphoglycerate kinase (gPGK) by purified glycosomes. Up to 50% of the total 35S-gPGK in the glycosomal fraction was resistant to extraction by 3 M urea or treatment wit

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Sommer, J. M., J. A. Thissen, M. Parsons, and C. C. Wang. "Characterization of an in vitro assay for import of 3-phosphoglycerate kinase into the glycosomes of Trypanosoma brucei." Molecular and Cellular Biology 10, no. 9 (1990): 4545–54. http://dx.doi.org/10.1128/mcb.10.9.4545-4554.1990.

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Glycosomes are microbody organelles found in kinetoplastida, where they serve to compartmentalize the enzymes of the glycolytic pathway. In order to identify the mechanism by which these enzymes are targeted to the glycosome, we have modified the in vitro import assay developed by Dovey et al. (Proc. Natl. Acad. Sci. USA 85:2598-2602, 1988). This assay measures the uptake of in vitro-translated Trypanosoma brucei glycosomal 3-phosphoglycerate kinase (gPGK) by purified glycosomes. Up to 50% of the total 35S-gPGK in the glycosomal fraction was resistant to extraction by 3 M urea or treatment wit

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Bauer, Sarah, James C. Morris, and Meredith T. Morris. "Environmentally Regulated Glycosome Protein Composition in the African Trypanosome." Eukaryotic Cell 12, no. 8 (2013): 1072–79. http://dx.doi.org/10.1128/ec.00086-13.

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ABSTRACT Trypanosomes compartmentalize many metabolic enzymes in glycosomes, peroxisome-related microbodies that are essential to parasite survival. While it is understood that these dynamic organelles undergo profound changes in protein composition throughout life cycle differentiation, the adaptations that occur in response to changes in environmental conditions are less appreciated. We have adopted a fluorescent-organelle reporter system in procyclic Trypanosoma brucei by expressing a fluorescent protein (FP) fused to a glycosomal targeting sequence (peroxisome-targeting sequence 2 [PTS2]).

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Durrani, Hina, Marshall Hampton, Jon N. Rumbley, and Sara L. Zimmer. "A Global Analysis of Enzyme Compartmentalization to Glycosomes." Pathogens 9, no. 4 (2020): 281. http://dx.doi.org/10.3390/pathogens9040281.

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In kinetoplastids, the first seven steps of glycolysis are compartmentalized into a glycosome along with parts of other metabolic pathways. This organelle shares a common ancestor with the better-understood eukaryotic peroxisome. Much of our understanding of the emergence, evolution, and maintenance of glycosomes is limited to explorations of the dixenous parasites, including the enzymatic contents of the organelle. Our objective was to determine the extent that we could leverage existing studies in model kinetoplastids to determine the composition of glycosomes in species lacking evidence of

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Dey, R., and S. C. Datta. "Leishmanial glycosomes contain superoxide dismutase." Biochemical Journal 301, no. 2 (1994): 317–19. http://dx.doi.org/10.1042/bj3010317.

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In this work we report that superoxide dismutase is entrapped in a microbody-like organelle, the glycosome, present in Leishmania spp. Studies on the sensitivity of the enzyme to various inhibitors indicated that glycosomal superoxide dismutase is predominantly of the Cu/Zu type. Localization of superoxide dismutase in glycosomes points to the major importance of this organelle in the survival of this pathogen, suggesting a new approach towards chemotherapy for leishmaniasis.

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Banerjee, Hiren, Barbara Knoblach, and Richard A. Rachubinski. "The early-acting glycosome biogenic protein Pex3 is essential for trypanosome viability." Life Science Alliance 2, no. 4 (2019): e201900421. http://dx.doi.org/10.26508/lsa.201900421.

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Trypanosomatid parasites are infectious agents for diseases such as African sleeping sickness, Chagas disease, and leishmaniasis that threaten millions of people, mostly in the emerging world. Trypanosomes compartmentalize glycolytic enzymes to an organelle called the glycosome, a specialized peroxisome. Functionally intact glycosomes are essential for trypanosomatid viability, making glycosomal proteins as potential drug targets against trypanosomatid diseases. Peroxins (Pex), of which Pex3 is the master regulator, control glycosome biogenesis. Although Pex3 has been found throughout the euka

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Crowe, Logan P., and Meredith T. Morris. "Glycosome heterogeneity in kinetoplastids." Biochemical Society Transactions 49, no. 1 (2021): 29–39. http://dx.doi.org/10.1042/bst20190517.

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Kinetoplastid parasites have essential organelles called glycosomes that are analogous to peroxisomes present in other eukaryotes. While many of the processes that regulate glycosomes are conserved, there are several unique aspects of their biology that are divergent from other systems and may be leveraged as therapeutic targets for the treatment of kinetoplastid diseases. Glycosomes are heterogeneous organelles that likely exist as sub-populations with different protein composition and function in a given cell, between individual cells, and between species. However, the limitations posed by t

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Häusler, T., Y. D. Stierhof, E. Wirtz, and C. Clayton. "Import of a DHFR hybrid protein into glycosomes in vivo is not inhibited by the folate-analogue aminopterin." Journal of Cell Biology 132, no. 3 (1996): 311–24. http://dx.doi.org/10.1083/jcb.132.3.311.

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Dihydrofolate reductase fusion proteins have been widely used to study conformational properties of polypeptides translocated across membranes. We have studied the import of dihydrofolate reductase fusion proteins into glycosomes and mitochondria of Trypanosoma brucei. As signal sequences we used the last 22 carboxy-terminal amino acids of glycosomal phosphoglycerate kinase for glycosomes, and the cleavable presequences of yeast cytochrome b2 or cytochrome oxidase subunit IV for mitochondria. Upon addition of aminopterin, a folate analogue that stabilizes the dihydrofolate reductase moiety, im

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Sommer, J. M., Q. L. Cheng, G. A. Keller, and C. C. Wang. "In vivo import of firefly luciferase into the glycosomes of Trypanosoma brucei and mutational analysis of the C-terminal targeting signal." Molecular Biology of the Cell 3, no. 7 (1992): 749–59. http://dx.doi.org/10.1091/mbc.3.7.749.

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The compartmentalization of glycolytic enzymes into specialized organelles, the glycosomes, allows the bloodstream form of Trypanosoma brucei to rely solely on glycolysis for its energy production. The biogenesis of glycosomes in these parasites has been studied intensively as a potential target for chemotherapy. We have adapted the recently developed methods for stable transformation of T. brucei to the in vivo analysis of glycosomal protein import. Firefly luciferase, a peroxisomal protein in the lantern of the insect, was expressed in stable transformants of the procyclic form of T. brucei,

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Dissertations / Theses on the topic "Glycosomes"

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Villafraz, Oriana. "UDP-glucose pyrophosphorylase (UGP) : import dans les glycosomes et implication dans la biosynthèse glycosomale et cytosolique des sucres nucléotidiques chez Trypanosoma brucei." Thesis, Bordeaux, 2020. http://www.theses.fr/2020BORD0215.

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Trypanosoma brucei, un protiste responsable de la Trypanosomose Humaine Africaine, également connue sous le nom de la maladie du sommeil, est transmis par la mouche tsé-tsé (Glossina sp.). La découverte d'organites de type peroxysome spécialisés dans la glycolyse, appelés glycosomes, a soulevé un certain nombre de questions sur le rôle de cet organite dans la biologie des trypanosomes. Plusieurs voies métaboliques présentes dans le cytosol d'autres eucaryotes, comme la glycolyse et la biosynthèse des sucres nucléotidiques, sont compartimentées dans les glycosomes. Les raisons et les avantages

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Silva, Maria Fernanda Laranjeira da. "Relação entre a localização celular da enzima arginase de Leishmania (Leishmania) amazonensis e seu papel na infecção de macrófagos murinos." Universidade de São Paulo, 2010. http://www.teses.usp.br/teses/disponiveis/41/41135/tde-21072010-135930/.

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Nos hospedeiros mamíferos, os parasitas do gênero Leishmania vivem nos macrófagos se evadindo de mecanismos microbicidas dessas células, tais como a produção de óxido nítrico (NO). A produção de NO pela enzima óxido nítrico sintase induzida (iNOS) nos macrófagos requer L-arginina como substrato, o mesmo aminoácido utilizado pela arginase para produzir ornitina e uréia. Logo, a arginase pode atuar na sobrevivência de Leishmania no hospedeiro competindo com a iNOS, reduzindo a produção de NO, além de seu papel na via de poliaminas, essencial para a replicação dessas células. Com isso, o objetivo

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Kalel, Vishal C. [Verfasser], Ralf [Gutachter] Erdmann, and Mathias [Gutachter] Lübben. "Glycosome biogenesis in trypanosomes / Vishal C. Kalel ; Gutachter: Ralf Erdmann, Mathias Lübben." Bochum : Ruhr-Universität Bochum, 2017. http://d-nb.info/1125106484/34.

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Kalel, Vishal [Verfasser], Ralf [Gutachter] Erdmann, and Mathias [Gutachter] Lübben. "Glycosome biogenesis in trypanosomes / Vishal C. Kalel ; Gutachter: Ralf Erdmann, Mathias Lübben." Bochum : Ruhr-Universität Bochum, 2017. http://d-nb.info/1125106484/34.

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Cyr, Normand. "Role of «Leishmania donovani» peroxin 14 in glycosomal import machinery." Thesis, McGill University, 2013. http://digitool.Library.McGill.CA:80/R/?func=dbin-jump-full&object_id=114123.

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Peroxisomes are organelles found in eukaryotic cells where several oxidative processes take place. Enzymes destined for the peroxisome generally contain either a C-terminal or a N-terminal peroxisomal targeting signal, named PTS1 and PTS2 respectively. These signals are cytosolically recognized by their correspondent receptors PEX5 and PEX7 prior to being recruited at the surface of the peroxisomal membrane where the complex docks onto PEX14. Then, enzymes are transported in a natively folded fashion inside the organelle where they are released. In trypanosomatids, other metabolic pathways, in

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Nyisztor, Michael. "The Leishmania donovani peroxin 14 N-terminal region is important for glycosomal localization." Thesis, McGill University, 2007. http://digitool.Library.McGill.CA:80/R/?func=dbin-jump-full&object_id=100200.

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Glycosomes are subcellular organelles that are evolutionarily related to the peroxisomes of higher eukaryotes. The Leishmania glycosome performs various metabolic processes that are essential for the survival of these parasites, such as the glycolytic process. Proteins that are destined for import into the glycosome interact selectively with specific cytosolic receptors peroxin 5(PEX5) or PEX7. The PEX5-protein complex migrates toward the glycosomal membrane where it interacts with PEX14, a vital step for protein important into the glycosome.<br>This project investigated the interaction mechan

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Pilar, Ana Victoria. "Biochemical and molecular characterization of the glycosomal PTS2 import receptor peroxin 7 in «Leishmania donovani»." Thesis, McGill University, 2009. http://digitool.Library.McGill.CA:80/R/?func=dbin-jump-full&object_id=32255.

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The Leishmania peroxin 7 (LmPEX7 or LdPEX7) is the receptor that translocates PTS2 signal-containing proteins into the glycosome. This microbody is unique to and crucial for the survival of trypanosomatids which include Leishmania and Trypanosoma, the causative agents of leishmaniasis and African sleeping sickness, respectively. Proteins are imported into the glycosome via two pathways, PTS1 and PTS2, which involves the formation of a PTS-receptor complex in the cytosol, docking of the complex on a transl

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Madrid, Kleber Patricio. "The molecular and structural characterization of the PTS1 glycosomal protein import pathway in Leishmania donovani /." Thesis, McGill University, 2005. http://digitool.Library.McGill.CA:80/R/?func=dbin-jump-full&object_id=100649.

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In Leishmania glycosomes compartmentalize a variety of essential biochemical and metabolic pathways required for parasite viability. Biogenesis and maintenance of glycosomes involves a family of proteins called peroxins, however the molecular mechanisms governing the early events of this pathway have not been fully established.<br>A structural-functional analysis of the receptor LdPEX5 revealed the formation of a tetrameric structure stabilized by coiled-coil motifs. A biophysical approach showed that the tetrameric structure of LdPEX5 dissociates to dimers upon binding to the PTS1 ligand. How

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Strasser, Rona. "Protein-protein interactions of receptors LdPEX5 and LPEX7 with PTS1 and PTS2 cargo proteins, and with glycosomal docking protein LdPEX14 for protein import into «Leishmania donovani»." Thesis, McGill University, 2014. http://digitool.Library.McGill.CA:80/R/?func=dbin-jump-full&object_id=122960.

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A unique subcellular structure found in Leishmania donovani is the glycosome. This organelle compartmentalizes the enzymatic machinery required for multiple metabolic pathways, including glycolysis. Correct targeting of glycosomal enzymes is essential for parasite viability. Proteins targeted to the glycosome have either a C-terminal PTS1 or N-terminal PTS2 topogenic signal sequence, which is recognized by cytosolic receptors LdPEX5 or LPEX7, respectively. These cargo-loaded receptors interact with the peroxin protein LdPEX14, located on the cytosolic face of the glycosomal membrane, an event

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Book chapters on the topic "Glycosomes"

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Acosta, Héctor, and Wilfredo Quiñones. "Isolation of Glycosomes from Trypanosoma cruzi." In Methods in Molecular Biology. Springer US, 2020. http://dx.doi.org/10.1007/978-1-0716-0294-2_37.

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Opperdoes, F. R. "Biogenesis of Glycosomes (Microbodies) in the Trypanosomatidae." In Proceedings in Life Sciences. Springer Berlin Heidelberg, 1987. http://dx.doi.org/10.1007/978-3-642-71325-5_46.

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Brennand, Ana, Eva Rico, Melisa Gualdrón-López, and Paul A. M. Michels. "Turnover of Glycosomes in Trypanosomes - Perspectives for Drug Discovery." In Comprehensive Analysis of Parasite Biology: From Metabolism to Drug Discovery. Wiley-VCH Verlag GmbH & Co. KGaA, 2016. http://dx.doi.org/10.1002/9783527694082.ch10.

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Gualdrón-López, Melisa, Paul A. M. Michels, Wilfredo Quiñones, Ana J. Cáceres, Luisana Avilán, and Juan-Luis Concepción. "Function of Glycosomes in the Metabolism of Trypanosomatid Parasites and the Promise of Glycosomal Proteins as Drug Targets." In Trypanosomatid Diseases. Wiley-VCH Verlag GmbH & Co. KGaA, 2013. http://dx.doi.org/10.1002/9783527670383.ch7.

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Borst, P., and B. W. Swinkels. "The Evolutionary Origin of Glycosomes: How Glycolysis Moved from Cytosol to Organelle in Evolution." In Evolutionary Tinkering in Gene Expression. Springer US, 1989. http://dx.doi.org/10.1007/978-1-4684-5664-6_16.

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Opperdoes, Fred R. "The Glycosome of Trypanosomatids." In Microbiology Monographs. Springer Berlin Heidelberg, 2010. http://dx.doi.org/10.1007/978-3-642-12863-9_12.

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Opperdoes, Fred R. "The Glycosome of Leishmania as a Possible Target for Chemotherapeutic Attack." In Leishmaniasis. Springer US, 1989. http://dx.doi.org/10.1007/978-1-4613-1575-9_107.

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Fairlamb, Alan H., and Fred R. Opperdoes. "Carbohydrate Metabolism in African Trypanosomes, with Special Reference to the Glycosome." In Carbohydrate Metabolism in Cultured Cells. Springer US, 1986. http://dx.doi.org/10.1007/978-1-4684-7679-8_6.

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"Glycosomes." In Encyclopedia of Parasitology. Springer Berlin Heidelberg, 2016. http://dx.doi.org/10.1007/978-3-662-43978-4_1309.

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"Glycosome." In Encyclopedia of Genetics, Genomics, Proteomics and Informatics. Springer Netherlands, 2008. http://dx.doi.org/10.1007/978-1-4020-6754-9_7011.

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