Transduction mechanisms in trypanosma

The presence of a nitric oxide (NO) pathway in Trypanosoma cruzi epimastigotes was demonstrated. The following components of that pathway were found: glutamate/NMDA receptors, a soluble Ca2+ calmodulin-dependent NO synthase and a soluble Na nitroprussideactivated guanylyl cyclase. In epimastigotes,...

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Autores principales: Torres, Héctor Norberto, Pereira, Claudio Alejandro, Alonso, Guillermo Daniel, Paveto, María Cristina, Espinosa, Joaquín Maximiliano, Portal, Daniel, Flawiá, Mirtha María
Publicado: 1998
Acceso en línea:https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_08926638_v12_n8_p_Torres
http://hdl.handle.net/20.500.12110/paper_08926638_v12_n8_p_Torres
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Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) de Universidad de Buenos Aires
id paper:paper_08926638_v12_n8_p_Torres
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spelling paper:paper_08926638_v12_n8_p_Torres2023-06-08T15:47:21Z Transduction mechanisms in trypanosma Torres, Héctor Norberto Pereira, Claudio Alejandro Alonso, Guillermo Daniel Paveto, María Cristina Espinosa, Joaquín Maximiliano Portal, Daniel Flawiá, Mirtha María The presence of a nitric oxide (NO) pathway in Trypanosoma cruzi epimastigotes was demonstrated. The following components of that pathway were found: glutamate/NMDA receptors, a soluble Ca2+ calmodulin-dependent NO synthase and a soluble Na nitroprussideactivated guanylyl cyclase. In epimastigotes, glutamate or NMDA stimulated the conversion of L-arginine to citrulline and increased cell motility. These stimulations could be blocked by MK-801 and ketamine and enhanced by glycine or serine. Motility was also stimulated by L-arginine and Na nitroprusside. In T. cruzi epimastigotes, a specific, Na+-independent, L-arginine transport system was also found. After L-arginine uptake, P-arginine was generated; a L-arginine kinase activity was characterized. Using murine cDNA probes of c-fos and c-jun at low stringency, hybridization signals were detected in restriction fragments of T. cruzi DNA. Employing polyclonal sera raised against human c-fos and c-jun, specific polypeptide bands of about 36 and 40-50 kDa, respectively, were observed in Western blots of cytosolic or nuclear extracts. Moreover, in electrophoretic mobility shift assays using a TRE probe, three specific complexes were obtained which were increased by oxidative stress induced by hydrogen peroxide, and by the entrance of the culture into the stationary phase. (Supported by CONICET, UBA, F. Antorchas and ICGEB). Fil:Torres, H. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Pereira, C. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Alonso, G. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Paveto, C. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Espinosa, J. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Portal, D. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Flawià, M. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. 1998 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_08926638_v12_n8_p_Torres http://hdl.handle.net/20.500.12110/paper_08926638_v12_n8_p_Torres
institution Universidad de Buenos Aires
institution_str I-28
repository_str R-134
collection Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA)
description The presence of a nitric oxide (NO) pathway in Trypanosoma cruzi epimastigotes was demonstrated. The following components of that pathway were found: glutamate/NMDA receptors, a soluble Ca2+ calmodulin-dependent NO synthase and a soluble Na nitroprussideactivated guanylyl cyclase. In epimastigotes, glutamate or NMDA stimulated the conversion of L-arginine to citrulline and increased cell motility. These stimulations could be blocked by MK-801 and ketamine and enhanced by glycine or serine. Motility was also stimulated by L-arginine and Na nitroprusside. In T. cruzi epimastigotes, a specific, Na+-independent, L-arginine transport system was also found. After L-arginine uptake, P-arginine was generated; a L-arginine kinase activity was characterized. Using murine cDNA probes of c-fos and c-jun at low stringency, hybridization signals were detected in restriction fragments of T. cruzi DNA. Employing polyclonal sera raised against human c-fos and c-jun, specific polypeptide bands of about 36 and 40-50 kDa, respectively, were observed in Western blots of cytosolic or nuclear extracts. Moreover, in electrophoretic mobility shift assays using a TRE probe, three specific complexes were obtained which were increased by oxidative stress induced by hydrogen peroxide, and by the entrance of the culture into the stationary phase. (Supported by CONICET, UBA, F. Antorchas and ICGEB).
author Torres, Héctor Norberto
Pereira, Claudio Alejandro
Alonso, Guillermo Daniel
Paveto, María Cristina
Espinosa, Joaquín Maximiliano
Portal, Daniel
Flawiá, Mirtha María
spellingShingle Torres, Héctor Norberto
Pereira, Claudio Alejandro
Alonso, Guillermo Daniel
Paveto, María Cristina
Espinosa, Joaquín Maximiliano
Portal, Daniel
Flawiá, Mirtha María
Transduction mechanisms in trypanosma
author_facet Torres, Héctor Norberto
Pereira, Claudio Alejandro
Alonso, Guillermo Daniel
Paveto, María Cristina
Espinosa, Joaquín Maximiliano
Portal, Daniel
Flawiá, Mirtha María
author_sort Torres, Héctor Norberto
title Transduction mechanisms in trypanosma
title_short Transduction mechanisms in trypanosma
title_full Transduction mechanisms in trypanosma
title_fullStr Transduction mechanisms in trypanosma
title_full_unstemmed Transduction mechanisms in trypanosma
title_sort transduction mechanisms in trypanosma
publishDate 1998
url https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_08926638_v12_n8_p_Torres
http://hdl.handle.net/20.500.12110/paper_08926638_v12_n8_p_Torres
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