Poly(ADP-ribose) polymerase plays a differential role in DNA damage-response and cell death pathways in Trypanosoma cruzi

Poly(ADP-ribosyl)ation is a post-translational modification of proteins. Poly(ADP-ribose) polymerase (PARP) and poly(ADP-ribose) glycohydrolase (PARG) are the enzymes responsible for poly(ADP-ribose) (PAR) polymer metabolism and are present in most higher eukaryotes. The best understood role of PARP...

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Autores principales: Vilchez Larrea, S.C., Alonso, G.D., Schlesinger, M., Torres, H.N., Flawiá, M.M., Fernández Villamil, S.H.
Formato: JOUR
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DNA
Acceso en línea:http://hdl.handle.net/20.500.12110/paper_00207519_v41_n3_p405_VilchezLarrea
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spelling todo:paper_00207519_v41_n3_p405_VilchezLarrea2023-10-03T14:18:36Z Poly(ADP-ribose) polymerase plays a differential role in DNA damage-response and cell death pathways in Trypanosoma cruzi Vilchez Larrea, S.C. Alonso, G.D. Schlesinger, M. Torres, H.N. Flawiá, M.M. Fernández Villamil, S.H. Cell death DNA repair PARG PARP Trypanosoma cruzi hydrogen peroxide nicotinamide adenine dinucleotide adenosine diphosphate ribosyltransferase DNA eukaryote genotoxicity inhibitor metabolism parasite polymerase chain reaction protein apoptosis article cell growth cell nucleus controlled study cytosol DNA damage enzyme activation enzyme activity gene translocation nonhuman nuclear localization signal nucleotide sequence protein expression Trypanosoma cruzi ultraviolet radiation Animals Cell Death Cell Nucleus DNA Damage DNA Repair Glycoside Hydrolases Poly(ADP-ribose) Polymerases Protozoan Proteins Trypanosoma cruzi Eukaryota Protista Trypanosoma cruzi Poly(ADP-ribosyl)ation is a post-translational modification of proteins. Poly(ADP-ribose) polymerase (PARP) and poly(ADP-ribose) glycohydrolase (PARG) are the enzymes responsible for poly(ADP-ribose) (PAR) polymer metabolism and are present in most higher eukaryotes. The best understood role of PARP is the maintenance of genomic integrity either via promotion of DNA repair at low levels of genotoxic stress or via promotion of cell death at higher levels of damage. The unicellular eukaryote Trypanosoma cruzi, as opposed to humans and other organisms, has only one PARP (TcPARP) and one PARG (TcPARG). In the present study we show that under different DNA-damaging agents (H2O2 or UV-C radiation) TcPARP is activated and translocated from the cytosol to the nucleus, while TcPARG always shows a nuclear localisation. Parasites in the presence of PARP or PARG inhibitors, as well as parasites over-expressing either TcPARP or TcPARG, suggested that PAR metabolism could be involved in different phases of cell growth, even in the absence of DNA damage. We also believe that we provide the first reported evidence that different proteins could be poly(ADP-ribosyl)ated in response to different stimuli, leading to different cell death pathways. © 2010 Australian Society for Parasitology Inc. Fil:Alonso, G.D. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Torres, H.N. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Flawiá, M.M. 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_00207519_v41_n3_p405_VilchezLarrea
institution Universidad de Buenos Aires
institution_str I-28
repository_str R-134
collection Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA)
topic Cell death
DNA repair
PARG
PARP
Trypanosoma cruzi
hydrogen peroxide
nicotinamide adenine dinucleotide adenosine diphosphate ribosyltransferase
DNA
eukaryote
genotoxicity
inhibitor
metabolism
parasite
polymerase chain reaction
protein
apoptosis
article
cell growth
cell nucleus
controlled study
cytosol
DNA damage
enzyme activation
enzyme activity
gene translocation
nonhuman
nuclear localization signal
nucleotide sequence
protein expression
Trypanosoma cruzi
ultraviolet radiation
Animals
Cell Death
Cell Nucleus
DNA Damage
DNA Repair
Glycoside Hydrolases
Poly(ADP-ribose) Polymerases
Protozoan Proteins
Trypanosoma cruzi
Eukaryota
Protista
Trypanosoma cruzi
spellingShingle Cell death
DNA repair
PARG
PARP
Trypanosoma cruzi
hydrogen peroxide
nicotinamide adenine dinucleotide adenosine diphosphate ribosyltransferase
DNA
eukaryote
genotoxicity
inhibitor
metabolism
parasite
polymerase chain reaction
protein
apoptosis
article
cell growth
cell nucleus
controlled study
cytosol
DNA damage
enzyme activation
enzyme activity
gene translocation
nonhuman
nuclear localization signal
nucleotide sequence
protein expression
Trypanosoma cruzi
ultraviolet radiation
Animals
Cell Death
Cell Nucleus
DNA Damage
DNA Repair
Glycoside Hydrolases
Poly(ADP-ribose) Polymerases
Protozoan Proteins
Trypanosoma cruzi
Eukaryota
Protista
Trypanosoma cruzi
Vilchez Larrea, S.C.
Alonso, G.D.
Schlesinger, M.
Torres, H.N.
Flawiá, M.M.
Fernández Villamil, S.H.
Poly(ADP-ribose) polymerase plays a differential role in DNA damage-response and cell death pathways in Trypanosoma cruzi
topic_facet Cell death
DNA repair
PARG
PARP
Trypanosoma cruzi
hydrogen peroxide
nicotinamide adenine dinucleotide adenosine diphosphate ribosyltransferase
DNA
eukaryote
genotoxicity
inhibitor
metabolism
parasite
polymerase chain reaction
protein
apoptosis
article
cell growth
cell nucleus
controlled study
cytosol
DNA damage
enzyme activation
enzyme activity
gene translocation
nonhuman
nuclear localization signal
nucleotide sequence
protein expression
Trypanosoma cruzi
ultraviolet radiation
Animals
Cell Death
Cell Nucleus
DNA Damage
DNA Repair
Glycoside Hydrolases
Poly(ADP-ribose) Polymerases
Protozoan Proteins
Trypanosoma cruzi
Eukaryota
Protista
Trypanosoma cruzi
description Poly(ADP-ribosyl)ation is a post-translational modification of proteins. Poly(ADP-ribose) polymerase (PARP) and poly(ADP-ribose) glycohydrolase (PARG) are the enzymes responsible for poly(ADP-ribose) (PAR) polymer metabolism and are present in most higher eukaryotes. The best understood role of PARP is the maintenance of genomic integrity either via promotion of DNA repair at low levels of genotoxic stress or via promotion of cell death at higher levels of damage. The unicellular eukaryote Trypanosoma cruzi, as opposed to humans and other organisms, has only one PARP (TcPARP) and one PARG (TcPARG). In the present study we show that under different DNA-damaging agents (H2O2 or UV-C radiation) TcPARP is activated and translocated from the cytosol to the nucleus, while TcPARG always shows a nuclear localisation. Parasites in the presence of PARP or PARG inhibitors, as well as parasites over-expressing either TcPARP or TcPARG, suggested that PAR metabolism could be involved in different phases of cell growth, even in the absence of DNA damage. We also believe that we provide the first reported evidence that different proteins could be poly(ADP-ribosyl)ated in response to different stimuli, leading to different cell death pathways. © 2010 Australian Society for Parasitology Inc.
format JOUR
author Vilchez Larrea, S.C.
Alonso, G.D.
Schlesinger, M.
Torres, H.N.
Flawiá, M.M.
Fernández Villamil, S.H.
author_facet Vilchez Larrea, S.C.
Alonso, G.D.
Schlesinger, M.
Torres, H.N.
Flawiá, M.M.
Fernández Villamil, S.H.
author_sort Vilchez Larrea, S.C.
title Poly(ADP-ribose) polymerase plays a differential role in DNA damage-response and cell death pathways in Trypanosoma cruzi
title_short Poly(ADP-ribose) polymerase plays a differential role in DNA damage-response and cell death pathways in Trypanosoma cruzi
title_full Poly(ADP-ribose) polymerase plays a differential role in DNA damage-response and cell death pathways in Trypanosoma cruzi
title_fullStr Poly(ADP-ribose) polymerase plays a differential role in DNA damage-response and cell death pathways in Trypanosoma cruzi
title_full_unstemmed Poly(ADP-ribose) polymerase plays a differential role in DNA damage-response and cell death pathways in Trypanosoma cruzi
title_sort poly(adp-ribose) polymerase plays a differential role in dna damage-response and cell death pathways in trypanosoma cruzi
url http://hdl.handle.net/20.500.12110/paper_00207519_v41_n3_p405_VilchezLarrea
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