The nitric oxide transduction pathway in Trypanosoma cruzi
A nitric oxide synthase was partially purified from soluble extracts of Trypanosoma cruzi epimastigote forms. The conversion of L-arginine to citrulline by this enzyme activity required NADPH and was blocked by EGT(A). The reaction was activated by Ca2+, calmodulin, tetrahydrobiopterin, and FAD, and...
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1995
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Acceso en línea: | https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00219258_v270_n28_p16576_Paveto http://hdl.handle.net/20.500.12110/paper_00219258_v270_n28_p16576_Paveto |
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paper:paper_00219258_v270_n28_p16576_Paveto2023-06-08T14:43:17Z The nitric oxide transduction pathway in Trypanosoma cruzi 2 amino 5 phosphonovaleric acid amino acid derivative arginine calcium calmodulin citrulline cyclic gmp dizocilpine egtazic acid flavine adenine nucleotide glutamic acid glycine guanylate cyclase ketamine n methyl dextro aspartic acid n(g) methylarginine nitric oxide nitric oxide synthase nitroprusside sodium reduced nicotinamide adenine dinucleotide phosphate serine tetrahydrobiopterin article cell free system controlled study enzyme activity epimastigote nonhuman priority journal receptor binding signal transduction trypanosoma cruzi Amino Acid Oxidoreductases Animal Arginine Citrulline Cyclic GMP Dizocilpine Maleate Guanylate Cyclase Nitric Oxide Nitric-Oxide Synthase Receptors, N-Methyl-D-Aspartate Support, Non-U.S. Gov't Trypanosoma cruzi A nitric oxide synthase was partially purified from soluble extracts of Trypanosoma cruzi epimastigote forms. The conversion of L-arginine to citrulline by this enzyme activity required NADPH and was blocked by EGT(A). The reaction was activated by Ca2+, calmodulin, tetrahydrobiopterin, and FAD, and inhibited by N(ω)-methyl-L-arginine. L-Glutamate and N-methyl-D- aspartate stimulated in vivo conversion of L-arginine to citrulline by epimastigote cells. These stimulations could be blocked by EGTA, MK-801, and ketamine and enhanced by glycine. A sodium nitroprusside-activated guanylyl cyclase activity was detected in cell-free, soluble preparations of T. cruzi epimastigotes. L-Glutamate, N-methyl-D-aspartate, and sodium nitroprusside increased epimastigote cyclic GMP levels. MK-801 bound specifically to T. cruzi epimastigote cells. This binding was competed by ketamine and enhanced by glycine or L-serine. Evidence thus indicates that in T. cruzi epimastigotes, L-glutamate controls cyclic GMP levels through a pathway mediated by nitric oxide. 1995 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00219258_v270_n28_p16576_Paveto http://hdl.handle.net/20.500.12110/paper_00219258_v270_n28_p16576_Paveto |
institution |
Universidad de Buenos Aires |
institution_str |
I-28 |
repository_str |
R-134 |
collection |
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) |
topic |
2 amino 5 phosphonovaleric acid amino acid derivative arginine calcium calmodulin citrulline cyclic gmp dizocilpine egtazic acid flavine adenine nucleotide glutamic acid glycine guanylate cyclase ketamine n methyl dextro aspartic acid n(g) methylarginine nitric oxide nitric oxide synthase nitroprusside sodium reduced nicotinamide adenine dinucleotide phosphate serine tetrahydrobiopterin article cell free system controlled study enzyme activity epimastigote nonhuman priority journal receptor binding signal transduction trypanosoma cruzi Amino Acid Oxidoreductases Animal Arginine Citrulline Cyclic GMP Dizocilpine Maleate Guanylate Cyclase Nitric Oxide Nitric-Oxide Synthase Receptors, N-Methyl-D-Aspartate Support, Non-U.S. Gov't Trypanosoma cruzi |
spellingShingle |
2 amino 5 phosphonovaleric acid amino acid derivative arginine calcium calmodulin citrulline cyclic gmp dizocilpine egtazic acid flavine adenine nucleotide glutamic acid glycine guanylate cyclase ketamine n methyl dextro aspartic acid n(g) methylarginine nitric oxide nitric oxide synthase nitroprusside sodium reduced nicotinamide adenine dinucleotide phosphate serine tetrahydrobiopterin article cell free system controlled study enzyme activity epimastigote nonhuman priority journal receptor binding signal transduction trypanosoma cruzi Amino Acid Oxidoreductases Animal Arginine Citrulline Cyclic GMP Dizocilpine Maleate Guanylate Cyclase Nitric Oxide Nitric-Oxide Synthase Receptors, N-Methyl-D-Aspartate Support, Non-U.S. Gov't Trypanosoma cruzi The nitric oxide transduction pathway in Trypanosoma cruzi |
topic_facet |
2 amino 5 phosphonovaleric acid amino acid derivative arginine calcium calmodulin citrulline cyclic gmp dizocilpine egtazic acid flavine adenine nucleotide glutamic acid glycine guanylate cyclase ketamine n methyl dextro aspartic acid n(g) methylarginine nitric oxide nitric oxide synthase nitroprusside sodium reduced nicotinamide adenine dinucleotide phosphate serine tetrahydrobiopterin article cell free system controlled study enzyme activity epimastigote nonhuman priority journal receptor binding signal transduction trypanosoma cruzi Amino Acid Oxidoreductases Animal Arginine Citrulline Cyclic GMP Dizocilpine Maleate Guanylate Cyclase Nitric Oxide Nitric-Oxide Synthase Receptors, N-Methyl-D-Aspartate Support, Non-U.S. Gov't Trypanosoma cruzi |
description |
A nitric oxide synthase was partially purified from soluble extracts of Trypanosoma cruzi epimastigote forms. The conversion of L-arginine to citrulline by this enzyme activity required NADPH and was blocked by EGT(A). The reaction was activated by Ca2+, calmodulin, tetrahydrobiopterin, and FAD, and inhibited by N(ω)-methyl-L-arginine. L-Glutamate and N-methyl-D- aspartate stimulated in vivo conversion of L-arginine to citrulline by epimastigote cells. These stimulations could be blocked by EGTA, MK-801, and ketamine and enhanced by glycine. A sodium nitroprusside-activated guanylyl cyclase activity was detected in cell-free, soluble preparations of T. cruzi epimastigotes. L-Glutamate, N-methyl-D-aspartate, and sodium nitroprusside increased epimastigote cyclic GMP levels. MK-801 bound specifically to T. cruzi epimastigote cells. This binding was competed by ketamine and enhanced by glycine or L-serine. Evidence thus indicates that in T. cruzi epimastigotes, L-glutamate controls cyclic GMP levels through a pathway mediated by nitric oxide. |
title |
The nitric oxide transduction pathway in Trypanosoma cruzi |
title_short |
The nitric oxide transduction pathway in Trypanosoma cruzi |
title_full |
The nitric oxide transduction pathway in Trypanosoma cruzi |
title_fullStr |
The nitric oxide transduction pathway in Trypanosoma cruzi |
title_full_unstemmed |
The nitric oxide transduction pathway in Trypanosoma cruzi |
title_sort |
nitric oxide transduction pathway in trypanosoma cruzi |
publishDate |
1995 |
url |
https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00219258_v270_n28_p16576_Paveto http://hdl.handle.net/20.500.12110/paper_00219258_v270_n28_p16576_Paveto |
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1768545493788393472 |