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spelling paper:paper_10665234_v58_n2_p79_DeLederkremer2023-06-08T16:04:18Z Inositolphosphoceramide metabolism in Trypanosoma cruzi as compared with other trypanosomatids Muchnik de Lederkremer, Rosa María Agustí, Rosalía 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 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). Fil:De Lederkremer, R.M. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Agusti, R. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. 2011 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_10665234_v58_n2_p79_DeLederkremer http://hdl.handle.net/20.500.12110/paper_10665234_v58_n2_p79_DeLederkremer
institution Universidad de Buenos Aires
institution_str I-28
repository_str R-134
collection Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA)
topic 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
spellingShingle 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
Muchnik de Lederkremer, Rosa María
Agustí, Rosalía
Inositolphosphoceramide metabolism in Trypanosoma cruzi as compared with other trypanosomatids
topic_facet 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
description 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).
author Muchnik de Lederkremer, Rosa María
Agustí, Rosalía
author_facet Muchnik de Lederkremer, Rosa María
Agustí, Rosalía
author_sort Muchnik de Lederkremer, Rosa María
title Inositolphosphoceramide metabolism in Trypanosoma cruzi as compared with other trypanosomatids
title_short Inositolphosphoceramide metabolism in Trypanosoma cruzi as compared with other trypanosomatids
title_full Inositolphosphoceramide metabolism in Trypanosoma cruzi as compared with other trypanosomatids
title_fullStr Inositolphosphoceramide metabolism in Trypanosoma cruzi as compared with other trypanosomatids
title_full_unstemmed Inositolphosphoceramide metabolism in Trypanosoma cruzi as compared with other trypanosomatids
title_sort inositolphosphoceramide metabolism in trypanosoma cruzi as compared with other trypanosomatids
publishDate 2011
url https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_10665234_v58_n2_p79_DeLederkremer
http://hdl.handle.net/20.500.12110/paper_10665234_v58_n2_p79_DeLederkremer
work_keys_str_mv AT muchnikdelederkremerrosamaria inositolphosphoceramidemetabolismintrypanosomacruziascomparedwithothertrypanosomatids
AT agustirosalia inositolphosphoceramidemetabolismintrypanosomacruziascomparedwithothertrypanosomatids
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