Characterization of poly(ADP-ribose)polymerase from Crithidia fasciculata: Enzyme inhibition by β-lapachone

Autores
Fernandez Villamil, Silvia Hebe; Podestá, Dolores; Molina Portela, María Del Pilar; Stoppani, Andres
Año de publicación
2001
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Crithidia fasciculata poly(ADP-ribose)polymerase (PARP) has been isolated and partially purified. This is the first PARP isolated from trypanosomatids; it requires DNA and histone for activity, using NAD+ as substrate. Thiol compounds specially dithiothreitol essentially contributed to PARP stability during purification and to PARP activity during assays. Nicotinamide, 3-aminobenzamide, theophylline, histamine, histidine, N-ethylmaleimide, p-chloromercuribenzoic acid, p-chloromercuriphenylsulfonic acid and o-iodosobenzoate inhibited PARP, thus confirming enzyme identity. PARP was also inhibited by the Fe(II)/H2O2 Fenton system. β-Lapachone inhibited PARP, apparently by direct interaction with the enzyme.
Fil: Fernandez Villamil, Silvia Hebe. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad de Buenos Aires. Facultad de Medicina; Argentina
Fil: Podestá, Dolores. Universidad de Buenos Aires. Facultad de Medicina; Argentina
Fil: Molina Portela, María Del Pilar. Universidad de Buenos Aires. Facultad de Medicina; Argentina
Fil: Stoppani, Andres. Universidad de Buenos Aires. Facultad de Medicina; Argentina
Materia
Crithidia Fasciculata
Oxidative Damage
Poly(Adp-Ribose)Polymerase
Trypanosomatids
Β--Lapachone
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/79351
Acceder
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oai_identifier_str oai:ri.conicet.gov.ar:11336/79351
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Characterization of poly(ADP-ribose)polymerase from Crithidia fasciculata: Enzyme inhibition by β-lapachoneFernandez Villamil, Silvia HebePodestá, DoloresMolina Portela, María Del PilarStoppani, AndresCrithidia FasciculataOxidative DamagePoly(Adp-Ribose)PolymeraseTrypanosomatidsΒ--Lapachonehttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1Crithidia fasciculata poly(ADP-ribose)polymerase (PARP) has been isolated and partially purified. This is the first PARP isolated from trypanosomatids; it requires DNA and histone for activity, using NAD+ as substrate. Thiol compounds specially dithiothreitol essentially contributed to PARP stability during purification and to PARP activity during assays. Nicotinamide, 3-aminobenzamide, theophylline, histamine, histidine, N-ethylmaleimide, p-chloromercuribenzoic acid, p-chloromercuriphenylsulfonic acid and o-iodosobenzoate inhibited PARP, thus confirming enzyme identity. PARP was also inhibited by the Fe(II)/H2O2 Fenton system. β-Lapachone inhibited PARP, apparently by direct interaction with the enzyme.Fil: Fernandez Villamil, Silvia Hebe. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad de Buenos Aires. Facultad de Medicina; ArgentinaFil: Podestá, Dolores. Universidad de Buenos Aires. Facultad de Medicina; ArgentinaFil: Molina Portela, María Del Pilar. Universidad de Buenos Aires. Facultad de Medicina; ArgentinaFil: Stoppani, Andres. Universidad de Buenos Aires. Facultad de Medicina; ArgentinaElsevier Science2001-12info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/79351Fernandez Villamil, Silvia Hebe; Podestá, Dolores; Molina Portela, María Del Pilar; Stoppani, Andres; Characterization of poly(ADP-ribose)polymerase from Crithidia fasciculata: Enzyme inhibition by β-lapachone; Elsevier Science; Molecular and Biochemical Parasitology; 115; 2; 12-2001; 249-2560166-6851CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/pii/S0166685101002912info:eu-repo/semantics/altIdentifier/doi/10.1016/S0166-6851(01)00291-2info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-29T10:03:55Zoai:ri.conicet.gov.ar:11336/79351instacron:CONICETInstitucionalhttp://ri.conicet.gov.ar/Organismo científico-tecnológicoNo correspondehttp://ri.conicet.gov.ar/oai/requestdasensio@conicet.gov.ar; lcarlino@conicet.gov.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:34982025-09-29 10:03:55.703CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Characterization of poly(ADP-ribose)polymerase from Crithidia fasciculata: Enzyme inhibition by β-lapachone
title Characterization of poly(ADP-ribose)polymerase from Crithidia fasciculata: Enzyme inhibition by β-lapachone
spellingShingle Characterization of poly(ADP-ribose)polymerase from Crithidia fasciculata: Enzyme inhibition by β-lapachone
Fernandez Villamil, Silvia Hebe
Crithidia Fasciculata
Oxidative Damage
Poly(Adp-Ribose)Polymerase
Trypanosomatids
Β--Lapachone
title_short Characterization of poly(ADP-ribose)polymerase from Crithidia fasciculata: Enzyme inhibition by β-lapachone
title_full Characterization of poly(ADP-ribose)polymerase from Crithidia fasciculata: Enzyme inhibition by β-lapachone
title_fullStr Characterization of poly(ADP-ribose)polymerase from Crithidia fasciculata: Enzyme inhibition by β-lapachone
title_full_unstemmed Characterization of poly(ADP-ribose)polymerase from Crithidia fasciculata: Enzyme inhibition by β-lapachone
title_sort Characterization of poly(ADP-ribose)polymerase from Crithidia fasciculata: Enzyme inhibition by β-lapachone
dc.creator.none.fl_str_mv Fernandez Villamil, Silvia Hebe
Podestá, Dolores
Molina Portela, María Del Pilar
Stoppani, Andres
author Fernandez Villamil, Silvia Hebe
author_facet Fernandez Villamil, Silvia Hebe
Podestá, Dolores
Molina Portela, María Del Pilar
Stoppani, Andres
author_role author
author2 Podestá, Dolores
Molina Portela, María Del Pilar
Stoppani, Andres
author2_role author
author
author
dc.subject.none.fl_str_mv Crithidia Fasciculata
Oxidative Damage
Poly(Adp-Ribose)Polymerase
Trypanosomatids
Β--Lapachone
topic Crithidia Fasciculata
Oxidative Damage
Poly(Adp-Ribose)Polymerase
Trypanosomatids
Β--Lapachone
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv Crithidia fasciculata poly(ADP-ribose)polymerase (PARP) has been isolated and partially purified. This is the first PARP isolated from trypanosomatids; it requires DNA and histone for activity, using NAD+ as substrate. Thiol compounds specially dithiothreitol essentially contributed to PARP stability during purification and to PARP activity during assays. Nicotinamide, 3-aminobenzamide, theophylline, histamine, histidine, N-ethylmaleimide, p-chloromercuribenzoic acid, p-chloromercuriphenylsulfonic acid and o-iodosobenzoate inhibited PARP, thus confirming enzyme identity. PARP was also inhibited by the Fe(II)/H2O2 Fenton system. β-Lapachone inhibited PARP, apparently by direct interaction with the enzyme.
Fil: Fernandez Villamil, Silvia Hebe. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad de Buenos Aires. Facultad de Medicina; Argentina
Fil: Podestá, Dolores. Universidad de Buenos Aires. Facultad de Medicina; Argentina
Fil: Molina Portela, María Del Pilar. Universidad de Buenos Aires. Facultad de Medicina; Argentina
Fil: Stoppani, Andres. Universidad de Buenos Aires. Facultad de Medicina; Argentina
description Crithidia fasciculata poly(ADP-ribose)polymerase (PARP) has been isolated and partially purified. This is the first PARP isolated from trypanosomatids; it requires DNA and histone for activity, using NAD+ as substrate. Thiol compounds specially dithiothreitol essentially contributed to PARP stability during purification and to PARP activity during assays. Nicotinamide, 3-aminobenzamide, theophylline, histamine, histidine, N-ethylmaleimide, p-chloromercuribenzoic acid, p-chloromercuriphenylsulfonic acid and o-iodosobenzoate inhibited PARP, thus confirming enzyme identity. PARP was also inhibited by the Fe(II)/H2O2 Fenton system. β-Lapachone inhibited PARP, apparently by direct interaction with the enzyme.
publishDate 2001
dc.date.none.fl_str_mv 2001-12
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/11336/79351
Fernandez Villamil, Silvia Hebe; Podestá, Dolores; Molina Portela, María Del Pilar; Stoppani, Andres; Characterization of poly(ADP-ribose)polymerase from Crithidia fasciculata: Enzyme inhibition by β-lapachone; Elsevier Science; Molecular and Biochemical Parasitology; 115; 2; 12-2001; 249-256
0166-6851
CONICET Digital
CONICET
url http://hdl.handle.net/11336/79351
identifier_str_mv Fernandez Villamil, Silvia Hebe; Podestá, Dolores; Molina Portela, María Del Pilar; Stoppani, Andres; Characterization of poly(ADP-ribose)polymerase from Crithidia fasciculata: Enzyme inhibition by β-lapachone; Elsevier Science; Molecular and Biochemical Parasitology; 115; 2; 12-2001; 249-256
0166-6851
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/pii/S0166685101002912
info:eu-repo/semantics/altIdentifier/doi/10.1016/S0166-6851(01)00291-2
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.format.none.fl_str_mv application/pdf
application/pdf
dc.publisher.none.fl_str_mv Elsevier Science
publisher.none.fl_str_mv Elsevier Science
dc.source.none.fl_str_mv reponame:CONICET Digital (CONICET)
instname:Consejo Nacional de Investigaciones Científicas y Técnicas
reponame_str CONICET Digital (CONICET)
collection CONICET Digital (CONICET)
instname_str Consejo Nacional de Investigaciones Científicas y Técnicas
repository.name.fl_str_mv CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicas
repository.mail.fl_str_mv dasensio@conicet.gov.ar; lcarlino@conicet.gov.ar
_version_ 1844613860379590656
score 13.070432

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