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Abstract:

Chagas disease is caused by Trypanosoma cruzi and is endemic to North, Central and South American countries. Current therapy against this disease is only partially effective and produces adverse side effects. Studies on the metabolic pathways of T. cruzi, in particular those with no equivalent in mammalian cells, might identify targets for the development of new drugs. Ceramide is metabolized to inositolphosphoceramide (IPC) in T. cruzi and other kinetoplastid protists whereas in mammals it is mainly incorporated into sphingomyelin. In T. cruzi, in contrast to Trypanosoma brucei and Leishmania spp., IPC functions as lipid anchor constituent of glycoproteins and free glycosylinositolphospholipids (GIPLs). Inhibition of IPC and GIPLs biosynthesis impairs differentiation of trypomastigotes into the intracellular amastigote forms. The gene encoding IPC synthase in T. cruzi has been identified and the enzyme has been expressed in a cell-free system. The enzyme involved in IPC degradation and the remodelases responsible for the incorporation of ceramide into free GIPLs or into the glycosylphosphatidylinositols anchoring glycoproteins, and in fatty acid modifications of these molecules of T. cruzi have been understudied. Inositolphosphoceramide metabolism and remodeling could be exploited as targets for Chagas disease chemotherapy. © 2011 The Author(s).

Registro:

Documento: Artículo
Título:Inositolphosphoceramide metabolism in Trypanosoma cruzi as compared with other trypanosomatids
Autor:De Lederkremer, R.M.; Agusti, R.; Docampo, R.
Filiación:CHIDECAR, Facultad de Ciencias Exactas y Naturales, Universidad de Buenos Aires, Pabellon 2, Ciudad Universitaria, 1428 Buenos Aires, Argentina
Department of Cellular Biology, Center for Tropical and Emerging Global Diseases, University of Georgia, Athens, GA 30602, United States
Palabras clave:Glycosylinositolphospholipids; glycosylphosphatidylinositol; inositolphosphoceramide; phospholipase C; sphingolipids; Trypanosoma; ceramide; glycosphingolipid; inositolphosphoceramides; protozoal protein; cell organelle; drug; endemic species; enzyme activity; fatty acid; inhibition; lipid; mammal; metabolism; molecular analysis; parasitic disease; protein; protozoan; biosynthesis; comparative study; genetics; Kinetoplastida; metabolism; review; Trypanosoma cruzi; Biosynthetic Pathways; Ceramides; Glycosphingolipids; Protozoan Proteins; Trypanosoma cruzi; Trypanosomatina; Kinetoplastida; Mammalia; Protista; Trypanosoma; Trypanosoma brucei; Trypanosoma cruzi; Trypanosomatidae
Año:2011
Volumen:58
Número:2
Página de inicio:79
Página de fin:87
DOI: http://dx.doi.org/10.1111/j.1550-7408.2011.00533.x
Título revista:Journal of Eukaryotic Microbiology
Título revista abreviado:J. Eukaryotic Microbiol.
ISSN:10665234
CODEN:JEMIE
CAS:Ceramides; Glycosphingolipids; Protozoan Proteins; inositolphosphoceramides
Registro:https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_10665234_v58_n2_p79_DeLederkremer

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Citas:

---------- APA ----------
De Lederkremer, R.M., Agusti, R. & Docampo, R. (2011) . Inositolphosphoceramide metabolism in Trypanosoma cruzi as compared with other trypanosomatids. Journal of Eukaryotic Microbiology, 58(2), 79-87.
http://dx.doi.org/10.1111/j.1550-7408.2011.00533.x
---------- CHICAGO ----------
De Lederkremer, R.M., Agusti, R., Docampo, R. "Inositolphosphoceramide metabolism in Trypanosoma cruzi as compared with other trypanosomatids" . Journal of Eukaryotic Microbiology 58, no. 2 (2011) : 79-87.
http://dx.doi.org/10.1111/j.1550-7408.2011.00533.x
---------- MLA ----------
De Lederkremer, R.M., Agusti, R., Docampo, R. "Inositolphosphoceramide metabolism in Trypanosoma cruzi as compared with other trypanosomatids" . Journal of Eukaryotic Microbiology, vol. 58, no. 2, 2011, pp. 79-87.
http://dx.doi.org/10.1111/j.1550-7408.2011.00533.x
---------- VANCOUVER ----------
De Lederkremer, R.M., Agusti, R., Docampo, R. Inositolphosphoceramide metabolism in Trypanosoma cruzi as compared with other trypanosomatids. J. Eukaryotic Microbiol. 2011;58(2):79-87.
http://dx.doi.org/10.1111/j.1550-7408.2011.00533.x