Inositolphosphoceramide metabolism in Trypanosoma cruzi as compared with other trypanosomatids

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 ma...

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Autor principal: De Lederkremer, R.M
Otros Autores: Agusti, R., Docampo, R.
Formato: Capítulo de libro
Lenguaje:Inglés
Publicado: 2011
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024 7 |2 scopus  |a 2-s2.0-79952786037 
024 7 |2 cas  |a Ceramides; Glycosphingolipids; Protozoan Proteins; inositolphosphoceramides 
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100 1 |a De Lederkremer, R.M. 
245 1 0 |a Inositolphosphoceramide metabolism in Trypanosoma cruzi as compared with other trypanosomatids 
260 |c 2011 
270 1 0 |m De Lederkremer, R. M.; CHIDECAR, Facultad de Ciencias Exactas y Naturales, Universidad de Buenos Aires, Pabellon 2, Ciudad Universitaria, 1428 Buenos Aires, Argentina; email: lederk@quimor.qo.fcen.uba.ar 
506 |2 openaire  |e Política editorial 
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520 3 |a 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).  |l eng 
593 |a CHIDECAR, Facultad de Ciencias Exactas y Naturales, Universidad de Buenos Aires, Pabellon 2, Ciudad Universitaria, 1428 Buenos Aires, Argentina 
593 |a Department of Cellular Biology, Center for Tropical and Emerging Global Diseases, University of Georgia, Athens, GA 30602, United States 
690 1 0 |a GLYCOSYLINOSITOLPHOSPHOLIPIDS 
690 1 0 |a GLYCOSYLPHOSPHATIDYLINOSITOL 
690 1 0 |a INOSITOLPHOSPHOCERAMIDE 
690 1 0 |a PHOSPHOLIPASE C 
690 1 0 |a SPHINGOLIPIDS 
690 1 0 |a TRYPANOSOMA 
690 1 0 |a CERAMIDE 
690 1 0 |a GLYCOSPHINGOLIPID 
690 1 0 |a INOSITOLPHOSPHOCERAMIDES 
690 1 0 |a PROTOZOAL PROTEIN 
690 1 0 |a CELL ORGANELLE 
690 1 0 |a DRUG 
690 1 0 |a ENDEMIC SPECIES 
690 1 0 |a ENZYME ACTIVITY 
690 1 0 |a FATTY ACID 
690 1 0 |a INHIBITION 
690 1 0 |a LIPID 
690 1 0 |a MAMMAL 
690 1 0 |a METABOLISM 
690 1 0 |a MOLECULAR ANALYSIS 
690 1 0 |a PARASITIC DISEASE 
690 1 0 |a PROTEIN 
690 1 0 |a PROTOZOAN 
690 1 0 |a BIOSYNTHESIS 
690 1 0 |a COMPARATIVE STUDY 
690 1 0 |a GENETICS 
690 1 0 |a KINETOPLASTIDA 
690 1 0 |a METABOLISM 
690 1 0 |a REVIEW 
690 1 0 |a TRYPANOSOMA CRUZI 
690 1 0 |a BIOSYNTHETIC PATHWAYS 
690 1 0 |a CERAMIDES 
690 1 0 |a GLYCOSPHINGOLIPIDS 
690 1 0 |a PROTOZOAN PROTEINS 
690 1 0 |a TRYPANOSOMA CRUZI 
690 1 0 |a TRYPANOSOMATINA 
690 1 0 |a KINETOPLASTIDA 
690 1 0 |a MAMMALIA 
690 1 0 |a PROTISTA 
690 1 0 |a TRYPANOSOMA 
690 1 0 |a TRYPANOSOMA BRUCEI 
690 1 0 |a TRYPANOSOMA CRUZI 
690 1 0 |a TRYPANOSOMATIDAE 
700 1 |a Agusti, R. 
700 1 |a Docampo, R. 
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