Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
9882189 | Archives of Biochemistry and Biophysics | 2005 | 6 Pages |
Abstract
Cytochalasin D (CD) induced production of the superoxide radical (O2â) in guinea pig polymorphonuclear leukocytes (PMNs). The protein kinase C (PKC) inhibitor GF109203X (GFX) was rarely without effect on CD-induced O2â production. CD as well as PMA induced the translocation of p47phox 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 O2â production. On the other hand, the production of O2â 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.
Keywords
Related Topics
Life Sciences
Biochemistry, Genetics and Molecular Biology
Biochemistry
Authors
Naoki Imagawa, Kazuki Nagasawa, Katsuhito Nagai, Naoko Kawakami-Honda, Sadaki Fujimoto,