Spermidine is essential for normal proliferation of trypanosomatid protozoa

Trypanosomatid parasites containing a metabolically unstable ornithine decarboxylase (ODC) are naturally resistant to high levels of α-difluoromethylornithine (DFMO) because this ODC inhibitor, though causing a drastic reduction of intracellular putrescine, elicits only a moderate decrease of the sp...

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Autores principales: González, N.S., Huber, A., Algranati, I.D.
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Acceso en línea:http://hdl.handle.net/20.500.12110/paper_00145793_v508_n3_p323_Gonzalez
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spelling todo:paper_00145793_v508_n3_p323_Gonzalez2023-10-03T14:13:08Z Spermidine is essential for normal proliferation of trypanosomatid protozoa González, N.S. Huber, A. Algranati, I.D. Cyclohexylamine Polyamine Spermidine Spermidine synthase Trypanosomatid proliferation eflornithine eticyclidine ornithine decarboxylase putrescine spermidine article cell proliferation controlled study Crithidia fasciculata enzyme stability nonhuman priority journal protozoon Trypanosoma cruzi Animals Crithidia fasciculata Cyclohexylamines Eflornithine Enzyme Inhibitors Ornithine Decarboxylase Putrescine Spermidine Spermidine Synthase Spermine Trypanosoma cruzi Protozoa Trypanosomatidae Trypanosomatid parasites containing a metabolically unstable ornithine decarboxylase (ODC) are naturally resistant to high levels of α-difluoromethylornithine (DFMO) because this ODC inhibitor, though causing a drastic reduction of intracellular putrescine, elicits only a moderate decrease of the spermidine endogenous pool. In this study we have used a combination of DFMO with cyclohexylamine (CHA; bis-cyclohexylammonium sulfate), an inhibitor of spermidine synthase, to reach a more complete depletion of spermidine. Under these conditions we have observed the arrest of proliferation not only in trypanosomatids with stable ODC but also in parasites with an enzyme of high turnover rate. In all cases the reinitiation of proliferation occurred only after the addition of exogenous spermidine, and neither putrescine nor spermine were able to induce the same effect. © 2001 Federation of European Biochemical Societies. Published by Elsevier Science B.V. All rights reserved. Fil:González, N.S. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Algranati, I.D. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. JOUR info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by/2.5/ar http://hdl.handle.net/20.500.12110/paper_00145793_v508_n3_p323_Gonzalez
institution Universidad de Buenos Aires
institution_str I-28
repository_str R-134
collection Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA)
topic Cyclohexylamine
Polyamine
Spermidine
Spermidine synthase
Trypanosomatid proliferation
eflornithine
eticyclidine
ornithine decarboxylase
putrescine
spermidine
article
cell proliferation
controlled study
Crithidia fasciculata
enzyme stability
nonhuman
priority journal
protozoon
Trypanosoma cruzi
Animals
Crithidia fasciculata
Cyclohexylamines
Eflornithine
Enzyme Inhibitors
Ornithine Decarboxylase
Putrescine
Spermidine
Spermidine Synthase
Spermine
Trypanosoma cruzi
Protozoa
Trypanosomatidae
spellingShingle Cyclohexylamine
Polyamine
Spermidine
Spermidine synthase
Trypanosomatid proliferation
eflornithine
eticyclidine
ornithine decarboxylase
putrescine
spermidine
article
cell proliferation
controlled study
Crithidia fasciculata
enzyme stability
nonhuman
priority journal
protozoon
Trypanosoma cruzi
Animals
Crithidia fasciculata
Cyclohexylamines
Eflornithine
Enzyme Inhibitors
Ornithine Decarboxylase
Putrescine
Spermidine
Spermidine Synthase
Spermine
Trypanosoma cruzi
Protozoa
Trypanosomatidae
González, N.S.
Huber, A.
Algranati, I.D.
Spermidine is essential for normal proliferation of trypanosomatid protozoa
topic_facet Cyclohexylamine
Polyamine
Spermidine
Spermidine synthase
Trypanosomatid proliferation
eflornithine
eticyclidine
ornithine decarboxylase
putrescine
spermidine
article
cell proliferation
controlled study
Crithidia fasciculata
enzyme stability
nonhuman
priority journal
protozoon
Trypanosoma cruzi
Animals
Crithidia fasciculata
Cyclohexylamines
Eflornithine
Enzyme Inhibitors
Ornithine Decarboxylase
Putrescine
Spermidine
Spermidine Synthase
Spermine
Trypanosoma cruzi
Protozoa
Trypanosomatidae
description Trypanosomatid parasites containing a metabolically unstable ornithine decarboxylase (ODC) are naturally resistant to high levels of α-difluoromethylornithine (DFMO) because this ODC inhibitor, though causing a drastic reduction of intracellular putrescine, elicits only a moderate decrease of the spermidine endogenous pool. In this study we have used a combination of DFMO with cyclohexylamine (CHA; bis-cyclohexylammonium sulfate), an inhibitor of spermidine synthase, to reach a more complete depletion of spermidine. Under these conditions we have observed the arrest of proliferation not only in trypanosomatids with stable ODC but also in parasites with an enzyme of high turnover rate. In all cases the reinitiation of proliferation occurred only after the addition of exogenous spermidine, and neither putrescine nor spermine were able to induce the same effect. © 2001 Federation of European Biochemical Societies. Published by Elsevier Science B.V. All rights reserved.
format JOUR
author González, N.S.
Huber, A.
Algranati, I.D.
author_facet González, N.S.
Huber, A.
Algranati, I.D.
author_sort González, N.S.
title Spermidine is essential for normal proliferation of trypanosomatid protozoa
title_short Spermidine is essential for normal proliferation of trypanosomatid protozoa
title_full Spermidine is essential for normal proliferation of trypanosomatid protozoa
title_fullStr Spermidine is essential for normal proliferation of trypanosomatid protozoa
title_full_unstemmed Spermidine is essential for normal proliferation of trypanosomatid protozoa
title_sort spermidine is essential for normal proliferation of trypanosomatid protozoa
url http://hdl.handle.net/20.500.12110/paper_00145793_v508_n3_p323_Gonzalez
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