Spermidine is essential for normal proliferation of trypanosomatid protozoa

Autores
González, N.S.; Huber, A.; Algranati, I.D.
Año de publicación
2001
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
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.
Fuente
FEBS Lett. 2001;508(3):323-326
Materia
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
Nivel de accesibilidad
acceso abierto
Condiciones de uso
http://creativecommons.org/licenses/by/2.5/ar
Repositorio
Biblioteca Digital (UBA-FCEN)
Institución
Universidad Nacional de Buenos Aires. Facultad de Ciencias Exactas y Naturales
OAI Identificador
paperaa:paper_00145793_v508_n3_p323_Gonzalez
Acceder
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oai_identifier_str paperaa:paper_00145793_v508_n3_p323_Gonzalez
network_acronym_str BDUBAFCEN
repository_id_str 1896
network_name_str Biblioteca Digital (UBA-FCEN)
spelling Spermidine is essential for normal proliferation of trypanosomatid protozoaGonzález, N.S.Huber, A.Algranati, I.D.CyclohexylaminePolyamineSpermidineSpermidine synthaseTrypanosomatid proliferationeflornithineeticyclidineornithine decarboxylaseputrescinespermidinearticlecell proliferationcontrolled studyCrithidia fasciculataenzyme stabilitynonhumanpriority journalprotozoonTrypanosoma cruziAnimalsCrithidia fasciculataCyclohexylaminesEflornithineEnzyme InhibitorsOrnithine DecarboxylasePutrescineSpermidineSpermidine SynthaseSpermineTrypanosoma cruziProtozoaTrypanosomatidaeTrypanosomatid 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.2001info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfhttp://hdl.handle.net/20.500.12110/paper_00145793_v508_n3_p323_GonzalezFEBS Lett. 2001;508(3):323-326reponame:Biblioteca Digital (UBA-FCEN)instname:Universidad Nacional de Buenos Aires. Facultad de Ciencias Exactas y Naturalesinstacron:UBA-FCENenginfo:eu-repo/semantics/openAccesshttp://creativecommons.org/licenses/by/2.5/ar2025-09-29T13:42:51Zpaperaa:paper_00145793_v508_n3_p323_GonzalezInstitucionalhttps://digital.bl.fcen.uba.ar/Universidad públicaNo correspondehttps://digital.bl.fcen.uba.ar/cgi-bin/oaiserver.cgiana@bl.fcen.uba.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:18962025-09-29 13:42:53.259Biblioteca Digital (UBA-FCEN) - Universidad Nacional de Buenos Aires. Facultad de Ciencias Exactas y Naturalesfalse
dc.title.none.fl_str_mv Spermidine is essential for normal proliferation of trypanosomatid protozoa
title Spermidine is essential for normal proliferation of trypanosomatid protozoa
spellingShingle Spermidine is essential for normal proliferation of trypanosomatid protozoa
González, N.S.
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
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
dc.creator.none.fl_str_mv González, N.S.
Huber, A.
Algranati, I.D.
author González, N.S.
author_facet González, N.S.
Huber, A.
Algranati, I.D.
author_role author
author2 Huber, A.
Algranati, I.D.
author2_role author
author
dc.subject.none.fl_str_mv 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
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
dc.description.none.fl_txt_mv 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.
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.
publishDate 2001
dc.date.none.fl_str_mv 2001
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
http://purl.org/coar/resource_type/c_6501
info:ar-repo/semantics/articulo
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv http://hdl.handle.net/20.500.12110/paper_00145793_v508_n3_p323_Gonzalez
url http://hdl.handle.net/20.500.12110/paper_00145793_v508_n3_p323_Gonzalez
dc.language.none.fl_str_mv eng
language eng
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
http://creativecommons.org/licenses/by/2.5/ar
eu_rights_str_mv openAccess
rights_invalid_str_mv http://creativecommons.org/licenses/by/2.5/ar
dc.format.none.fl_str_mv application/pdf
dc.source.none.fl_str_mv FEBS Lett. 2001;508(3):323-326
reponame:Biblioteca Digital (UBA-FCEN)
instname:Universidad Nacional de Buenos Aires. Facultad de Ciencias Exactas y Naturales
instacron:UBA-FCEN
reponame_str Biblioteca Digital (UBA-FCEN)
collection Biblioteca Digital (UBA-FCEN)
instname_str Universidad Nacional de Buenos Aires. Facultad de Ciencias Exactas y Naturales
instacron_str UBA-FCEN
institution UBA-FCEN
repository.name.fl_str_mv Biblioteca Digital (UBA-FCEN) - Universidad Nacional de Buenos Aires. Facultad de Ciencias Exactas y Naturales
repository.mail.fl_str_mv ana@bl.fcen.uba.ar
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score 13.070432

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