Calyculin A modulates activation of the NADPH-oxidase in Me2SO-differentiated HL-60 cells
Experimental & Molecular Medicine
;
: 214-220, 1998.
Article
Dans Anglais
| 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.
Texte intégral:
Disponible
Indice:
WPRIM (Pacifique occidental)
Sujet Principal:
Oxazoles
/
Oxygène
/
Phosphoprotéines
/
Facteurs temps
/
12-Myristate-13-acétate de phorbol
/
Transduction du signal
/
Différenciation cellulaire
/
Diméthylsulfoxyde
/
Acide arachidonique
/
Calcium-Calmodulin-Dependent Protein Kinases
Type d'étude:
Étude pronostique
Limites du sujet:
Humains
langue:
Anglais
Texte intégral:
Experimental & Molecular Medicine
Année:
1998
Type:
Article
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