Calyculin A modulates activation of the NADPH-oxidase in Me2SO-differentiated HL-60 cells
Experimental & Molecular Medicine
;
: 214-220, 1998.
Artigo
em Inglês
| WPRIM
| ID: wpr-159767
ABSTRACT
Human promyelocytic leukemia cells (HL-60) have been used as a model system in which to study the effects of protein phosphatase inhibitors on NADPH-oxidase activation. Since O2- is generated by NADPH-oxidase, we examined the effect of calyculin A pretreatment on oxidase activation in response to various agonists. When Me2SO-differentiated HL-60 cells were treated with calyculin A prior to the addition of phorbol 12-myristate 13-acetate (PMA), O2- production was inhibited; however, calyculin A enhanced O2- production by N-formyl-methionyl-leucyl-phenylalanine (FMLP). The decreased O2- production seen with calyculin A pretreatment followed by PMA may be due to diminished translocation of the p47-phox and p67-phox, cytosolic components of the oxidase, and inhibition of arachidonic acid release. Interestingly calyculin A pretreatment followed by either agonist significantly enhanced mitogen-activated-protein kinase (MAPK) activity. The differential effects of pretreatment with calyculin A on subsequent oxidase stimulation elicited by FMLP or PMA provide further evidence for substantial heterogeneity in the activation of the respiratory burst.
Texto completo:
DisponíveL
Índice:
WPRIM (Pacífico Ocidental)
Assunto principal:
Oxazóis
/
Oxigênio
/
Fosfoproteínas
/
Fatores de Tempo
/
Acetato de Tetradecanoilforbol
/
Transdução de Sinais
/
Diferenciação Celular
/
Dimetil Sulfóxido
/
Ácido Araquidônico
/
Proteínas Quinases Dependentes de Cálcio-Calmodulina
Tipo de estudo:
Estudo prognóstico
Limite:
Humanos
Idioma:
Inglês
Revista:
Experimental & Molecular Medicine
Ano de publicação:
1998
Tipo de documento:
Artigo
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