Effects of antimalarial drugs on several rat-liver lysosomal enzymes involved in phosphatidylethanolamine catabolism.
Biochim Biophys Acta
; 713(1): 112-7, 1982 Oct 14.
Article
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| MEDLINE
| ID: mdl-7138892
ABSTRACT
The effects of three cationic amphiphilic antimalarial drugs (chloroquine, mepacrine and primaquine) on the intralysosomal catabolism of phosphatidylethanolamine and several of its metabolites were studied with rat-liver lysosomes which had been isolated from animals previously treated with Triton WR-1339. The activities of each of the various enzymes involved in the main pathways of intralysosomal phosphatidylethanolamine degradation (Kunze, H., Hesse, B. and Bohn, E. (1982) Biochim. Biophys. Acta 711, 10-18) exhibited almost identical inhibitory sensitivities towards mepacrine and primaquine. In contrast, chloroquine inhibited the activities of the various enzymes to different extents, lysophospholipid acylhydrolase (EC 3.1.1.5) being the most sensitive enzyme, followed by phospholipase A1 (EC 3.1.1.32) and monoacylglycerol lipase, and eventually lysophospholipid monoacylglycerol hydrolase as the least sensitive enzyme. The relative inhibitory potencies towards phospholipase A1 activity of chloroquine were increased with increasing pH, and the mode of inhibition was competitive. In contrast, the inhibitory potencies towards monoacylglycerol lipase activity of chloroquine increased only up to pH 5 but decreased above this value, and the mode of inhibition was noncompetitive.
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Bases de datos:
MEDLINE
Asunto principal:
Fosfatidiletanolaminas
/
Fosfolipasas
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Fosfolipasas A
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Hidrolasas de Éster Carboxílico
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Hígado
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Lisofosfolipasa
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Monoacilglicerol Lipasas
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Antimaláricos
Límite:
Animals
Idioma:
En
Revista:
Biochim Biophys Acta
Año:
1982
Tipo del documento:
Article