Different signaling pathways are involved in cardiomyocyte survival induced by a Trypanosoma cruzi glycoprotein

We have recently reported that Trypanosoma cruzi infection protects cardiomyocytes against apoptosis induced by growth factor deprivation. Cruzipain, a major parasite antigen, reproduced this survival effect by a Bcl-2-dependent mechanism. In this study, we have investigated the molecular mechanisms...

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Autor principal: Aoki, M.d.P
Otros Autores: Cano, R.C, Pellegrini, A.V, Tanos, T., Guiñazú, N.L, Coso, O.A, Gea, S.
Formato: Capítulo de libro
Lenguaje:Inglés
Publicado: 2006
Acceso en línea:Registro en Scopus
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030 |a MCINF 
100 1 |a Aoki, M.d.P. 
245 1 0 |a Different signaling pathways are involved in cardiomyocyte survival induced by a Trypanosoma cruzi glycoprotein 
260 |c 2006 
270 1 0 |m Aoki, M.d.P.; CIBICI-CONICET, Departamento de Bioquímica Clínica, Facultad de Ciencias Químicas, Haya la Torre Medina Allende, CP 5000 Córdoba, Argentina; email: paoki@bioclin.fcq.unc.edu.ar 
506 |2 openaire  |e Política editorial 
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520 3 |a We have recently reported that Trypanosoma cruzi infection protects cardiomyocytes against apoptosis induced by growth factor deprivation. Cruzipain, a major parasite antigen, reproduced this survival effect by a Bcl-2-dependent mechanism. In this study, we have investigated the molecular mechanisms of cruzipain-induced cardiomyocyte protection. Neonatal BALB/c mouse cardiac myocytes were cultured under minimum serum conditions in the presence of cruzipain or T. cruzi (Tulahuen strain). Some cultures were pretreated with the phosphatidylinositol 3-kinase (PI3K) inhibitor Ly294002 or specific inhibitors of the mitogen-activated protein kinase (MAPK) family members such as the mitogen-activated protein kinase kinase (MEK1) inhibitor PD098059, Jun N-terminal kinase (JNK) inhibitor SP600125, p38 MAPK inhibitor SB203580. Inhibition of PI3K and MEK1 but not JNK or p38 MAPK increased the apoptotic rate of cardiomyocytes treated with cruzipain. Phosphorylation of Akt, a major target of PI3K, and ERK1/2, MEK1-targets, was achieved at 15 min and 5 min, respectively. In parallel, these kinases were strongly phosphorylated by T. cruzi infection. In cultures treated with cruzipain, cleavage of caspase 3 was considerably diminished after serum starvation; Bcl-2 overexpression was inhibited by PD098059 but not by Ly294002, whereas Bad phosphorylation and Bcl-xL expression were increased and differentially modulated by both inhibitors. The results suggest that cruzipain exerts its anti-apoptotic property in cardiac myocytes at least by PI3K/Akt and MEK1/ERK1/2 signaling pathways. We further identified a differential modulation of Bcl-2 family members by these two signaling pathways. © 2006 Elsevier SAS. All rights reserved.  |l eng 
536 |a Detalles de la financiación: Agencia Nacional de Promoción Científica y Tecnológica 
536 |a Detalles de la financiación: Fundación Antorchas 
536 |a Detalles de la financiación: Secretaria de Ciencia y Tecnología - Universidad Nacional de Córdoba 
536 |a Detalles de la financiación: This work was supported by grants from Agencia Nacional de Promoción Científica y Tecnológica (ANPCYT), Secretacía de Ciencia y Técnica-Universidad Nacional de Córdoba (SECYT-UNC) and Fundación Antorchas. M.P.A., O.A.C. and S.G. are Research Career Investigators from CONICET. T.T., A.V.P. and N.G. thank CONICET, for the fellowships granted. We thank Dr. C. Mas for excellent photographic assistance. 
593 |a CIBICI-CONICET, Departamento de Bioquímica Clínica, Facultad de Ciencias Químicas, Haya la Torre Medina Allende, CP 5000 Córdoba, Argentina 
593 |a IFIBYNE-CONICET, Laboratorio de Fisiología y Biología Molecular, Facultad de Ciencias Exactas y Naturales, Ciudad Universitaria Pabellon 2, Buenos Aires, Argentina 
690 1 0 |a CARDIOMYOCYTE 
690 1 0 |a MAPKS 
690 1 0 |a PI3K/AKT 
690 1 0 |a TRYPANOSOMA CRUZI 
690 1 0 |a 2 (2 AMINO 3 METHOXYPHENYL)CHROMONE 
690 1 0 |a 2 MORPHOLINO 8 PHENYLCHROMONE 
690 1 0 |a 4 (4 FLUOROPHENYL) 2 (4 METHYLSULFINYLPHENYL) 5 (4 PYRIDYL)IMIDAZOLE 
690 1 0 |a ANTHRA[1,9 CD]PYRAZOL 6(2H) ONE 
690 1 0 |a CRUZIPAIN 
690 1 0 |a GLYCOPROTEIN 
690 1 0 |a MITOGEN ACTIVATED PROTEIN KINASE 
690 1 0 |a MITOGEN ACTIVATED PROTEIN KINASE P38 
690 1 0 |a PHOSPHATIDYLINOSITOL 3 KINASE 
690 1 0 |a PROTEIN BAD 
690 1 0 |a PROTEIN BCL 2 
690 1 0 |a PROTEIN BCL XL 
690 1 0 |a PROTEIN KINASE B 
690 1 0 |a PROTOZOAL PROTEIN 
690 1 0 |a STRESS ACTIVATED PROTEIN KINASE 
690 1 0 |a ANIMAL CELL 
690 1 0 |a ANIMAL MODEL 
690 1 0 |a APOPTOSIS 
690 1 0 |a ARTICLE 
690 1 0 |a CELL PROTECTION 
690 1 0 |a CELL SURVIVAL 
690 1 0 |a CONTROLLED STUDY 
690 1 0 |a ENZYME INHIBITION 
690 1 0 |a ENZYME PHOSPHORYLATION 
690 1 0 |a HEART CELL CULTURE 
690 1 0 |a HEART MUSCLE CELL 
690 1 0 |a MOLECULAR MECHANICS 
690 1 0 |a MOUSE 
690 1 0 |a NEWBORN 
690 1 0 |a NONHUMAN 
690 1 0 |a PREMEDICATION 
690 1 0 |a PRIORITY JOURNAL 
690 1 0 |a PROTEIN EXPRESSION 
690 1 0 |a PROTOZOAL INFECTION 
690 1 0 |a SIGNAL TRANSDUCTION 
690 1 0 |a TRYPANOSOMA CRUZI 
690 1 0 |a 1-PHOSPHATIDYLINOSITOL 3-KINASE 
690 1 0 |a ANIMALS 
690 1 0 |a APOPTOSIS 
690 1 0 |a BCL-ASSOCIATED DEATH PROTEIN 
690 1 0 |a BCL-X PROTEIN 
690 1 0 |a CASPASE 3 
690 1 0 |a CASPASES 
690 1 0 |a CELL SURVIVAL 
690 1 0 |a CELLS, CULTURED 
690 1 0 |a CHROMONES 
690 1 0 |a CYSTEINE ENDOPEPTIDASES 
690 1 0 |a ENZYME INHIBITORS 
690 1 0 |a FLAVONOIDS 
690 1 0 |a GENE EXPRESSION 
690 1 0 |a GENES, BCL-2 
690 1 0 |a HUMANS 
690 1 0 |a IMIDAZOLES 
690 1 0 |a JNK MITOGEN-ACTIVATED PROTEIN KINASES 
690 1 0 |a MAP KINASE KINASE 1 
690 1 0 |a MICE 
690 1 0 |a MORPHOLINES 
690 1 0 |a MYOCYTES, CARDIAC 
690 1 0 |a P38 MITOGEN-ACTIVATED PROTEIN KINASES 
690 1 0 |a PHOSPHORYLATION 
690 1 0 |a PYRIDINES 
690 1 0 |a SIGNAL TRANSDUCTION 
690 1 0 |a TRYPANOSOMA CRUZI 
690 1 0 |a TRYPANOSOMA CRUZI 
700 1 |a Cano, R.C. 
700 1 |a Pellegrini, A.V. 
700 1 |a Tanos, T. 
700 1 |a Guiñazú, N.L. 
700 1 |a Coso, O.A. 
700 1 |a Gea, S. 
773 0 |d 2006  |g v. 8  |h pp. 1723-1731  |k n. 7  |p Microbes Infect.  |x 12864579  |w (AR-BaUEN)CENRE-6100  |t Microbes and Infection 
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856 4 0 |u https://doi.org/10.1016/j.micinf.2006.02.010  |y DOI 
856 4 0 |u https://hdl.handle.net/20.500.12110/paper_12864579_v8_n7_p1723_Aoki  |y Handle 
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