Protein kinase C-independent pathway for NADPH oxidase activation in guinea pig peritoneal polymorphonuclear leukocytes by cytochalasin D

Cytochalasin D (CD) induced production of the superoxide radical ( O 2 − ) in guinea pig polymorphonuclear leukocytes (PMNs). The protein kinase C (PKC) inhibitor GF109203X (GFX) was rarely without effect on CD-induced O 2 − production. CD as well as PMA induced the translocation of p47 phox to the...

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Veröffentlicht in:Archives of biochemistry and biophysics 2005-06, Vol.438 (2), p.119-124
Hauptverfasser: Imagawa, Naoki, Nagasawa, Kazuki, Nagai, Katsuhito, Kawakami-Honda, Naoko, Fujimoto, Sadaki
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Sprache:eng
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Zusammenfassung:Cytochalasin D (CD) induced production of the superoxide radical ( O 2 − ) in guinea pig polymorphonuclear leukocytes (PMNs). The protein kinase C (PKC) inhibitor GF109203X (GFX) was rarely without effect on CD-induced O 2 − production. CD as well as PMA induced the translocation of p47 phox to the membrane fraction, and this translocation was slightly decreased by GFX. Moreover, the inhibitory effect of a PKCζ antagonist with sequences based on the endogenous PKCζ pseudosubstrate region was weaker than the inhibitory effect on N-formyl-methionyl-leucyl-phenylalanine (fMLP)-induced O 2 − production. On the other hand, the production of O 2 − induced by CD was more strongly suppressed by the PLD inhibitor ethanol and phosphatidylinositol 3-kinase (PI3-K) inhibitor wortmannin than that induced by fMLP, and the activation of phospholipase D (PLD) by CD was restrained by wortmannin. These findings suggest that NADPH oxidase is activated by CD through a PKC-independent signaling pathway in PMNs, and this pathway involves the activation of PLD through PI3-K.
ISSN:0003-9861
1096-0384
DOI:10.1016/j.abb.2005.04.003