Inactivation of Trypanosoma cruzi dihydrolipoamide dehydrogenase by leukocyte myeloperoxidase systems: role of hypochloride and nitrite related radicals.
Rev. argent. microbiol
; 32(3): 136-43, 2000 Jul-Sep.
Artigo
em Inglês
| BINACIS
| ID: bin-39792
Biblioteca responsável:
AR32.1
ABSTRACT
Dihydrolipoamide dehydrogenase (LADH) from Trypanosoma cruzi, the causative agent of Chagas disease, was inactivated by treatment with myeloperoxidase (MPO)-dependent systems. LADH lipoamide reductase and diaphorase activities decreased as a function of incubation time and composition of the MPO/H2O2/halide system, a transient increase preceding the loss of diaphorase activity. Iodide, bromide, thiocyanide and chloride were effective components of MPO/H2O2 or MPO/NADH systems. Catalase prevented LADH inactivation by the MPO/NADH/halide systems in agreement with H2O2 production by NADH-supplemented LADH. Thiol compounds (L-cysteine, N-acetylcysteine, penicillamine, N-(2-mercaptopropionylglycine) and Captopril prevented LADH inactivation by the MPO/H2O2/NaCl system and by NaOCl, thus supporting HOCl as agent of the MPO/H2O2/NaCl system. MPO/H2O2/NaNO2 and MPO/NADH/NaNO2 inactivated LADH, the reaction being prevented by MPO inhibitors and thiol compounds. T. cruzi LADH was affected by MPO-dependent systems like myocardial LADH, allowance being made for the variation of the diaphorase activity and the greater sensitivity of the T. cruzi enzyme to MPO/H2O2/halide systems.
Buscar no Google
Coleções:
Bases de dados nacionais
/
Argentina
Contexto em Saúde:
Doenças Negligenciadas
Problema de saúde:
Doença de Chagas
/
Doenças Negligenciadas
Base de dados:
BINACIS
Idioma:
Inglês
Revista:
Rev. argent. microbiol
Ano de publicação:
2000
Tipo de documento:
Artigo