Control of Trypanosoma cruzi epimastigote motility through the nitric oxide pathway

Trypanosoma cruzi epimastigote motility can be enhanced by addition of L-arginine, to the culture. This effect is blocked by N-methyl-L-arginine, a competitive inhibitor of the nitric oxide synthase. N-methyl-D-aspartate and L-glutamate, two agonists of the NMDA/L glutamate receptor, also enhanced m...

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Autores principales: Pereira, C., Paveto, C., Espinosa, J., Alonso, G., Flawiá, M.M., Torres, H.N.
Formato: JOUR
Materias:
Cyclic GMP
guanylyl cyclase
nitric oxide synthase
NMDA/L-glutamate receptors
Acceso en línea:http://hdl.handle.net/20.500.12110/paper_10665234_v44_n2_p155_Pereira
Aporte de:
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) de Universidad de Buenos Aires
id todo:paper_10665234_v44_n2_p155_Pereira
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spelling todo:paper_10665234_v44_n2_p155_Pereira2023-10-03T16:02:06Z Control of Trypanosoma cruzi epimastigote motility through the nitric oxide pathway Pereira, C. Paveto, C. Espinosa, J. Alonso, G. Flawiá, M.M. Torres, H.N. Cyclic GMP guanylyl cyclase nitric oxide synthase NMDA/L-glutamate receptors Trypanosoma cruzi epimastigote motility can be enhanced by addition of L-arginine, to the culture. This effect is blocked by N-methyl-L-arginine, a competitive inhibitor of the nitric oxide synthase. N-methyl-D-aspartate and L-glutamate, two agonists of the NMDA/L glutamate receptor, also enhanced motility. This stimulation is blocked by MK-801 a noncompetitive antagonist of the NMDA receptor. In addition, sodium nitroprusside, a guanylyl cyclase stimulator and 8-Br cyclic GMP, an analog of cyclic GMP, also stimulated epimastigote motility. It is suggested that an increase of intracellular cyclic GMP levels mediated by nitric oxide may be responsible for the increase in epimastigote motility. JOUR info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by/2.5/ar http://hdl.handle.net/20.500.12110/paper_10665234_v44_n2_p155_Pereira
institution Universidad de Buenos Aires
institution_str I-28
repository_str R-134
collection Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA)
topic Cyclic GMP
guanylyl cyclase
nitric oxide synthase
NMDA/L-glutamate receptors
spellingShingle Cyclic GMP
guanylyl cyclase
nitric oxide synthase
NMDA/L-glutamate receptors
Pereira, C.
Paveto, C.
Espinosa, J.
Alonso, G.
Flawiá, M.M.
Torres, H.N.
Control of Trypanosoma cruzi epimastigote motility through the nitric oxide pathway
topic_facet Cyclic GMP
guanylyl cyclase
nitric oxide synthase
NMDA/L-glutamate receptors
description Trypanosoma cruzi epimastigote motility can be enhanced by addition of L-arginine, to the culture. This effect is blocked by N-methyl-L-arginine, a competitive inhibitor of the nitric oxide synthase. N-methyl-D-aspartate and L-glutamate, two agonists of the NMDA/L glutamate receptor, also enhanced motility. This stimulation is blocked by MK-801 a noncompetitive antagonist of the NMDA receptor. In addition, sodium nitroprusside, a guanylyl cyclase stimulator and 8-Br cyclic GMP, an analog of cyclic GMP, also stimulated epimastigote motility. It is suggested that an increase of intracellular cyclic GMP levels mediated by nitric oxide may be responsible for the increase in epimastigote motility.
format JOUR
author Pereira, C.
Paveto, C.
Espinosa, J.
Alonso, G.
Flawiá, M.M.
Torres, H.N.
author_facet Pereira, C.
Paveto, C.
Espinosa, J.
Alonso, G.
Flawiá, M.M.
Torres, H.N.
author_sort Pereira, C.
title Control of Trypanosoma cruzi epimastigote motility through the nitric oxide pathway
title_short Control of Trypanosoma cruzi epimastigote motility through the nitric oxide pathway
title_full Control of Trypanosoma cruzi epimastigote motility through the nitric oxide pathway
title_fullStr Control of Trypanosoma cruzi epimastigote motility through the nitric oxide pathway
title_full_unstemmed Control of Trypanosoma cruzi epimastigote motility through the nitric oxide pathway
title_sort control of trypanosoma cruzi epimastigote motility through the nitric oxide pathway
url http://hdl.handle.net/20.500.12110/paper_10665234_v44_n2_p155_Pereira
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