Inhibition of formyl peptide-stimulated phospholipase D activation by Fal-002-2 via blockade of the Arf6, RhoA and protein kinase C signaling pathways in rat neutrophils
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- 作者：Ya-Ru Tsai (1)
Li-Jiau Huang (2)
Hui-Yi Lin (2)
Yun-Jie Hung (1)
Miau-Rong Lee (3)
Sheng-Chu Kuo (2)
Mei-Feng Hsu (3)
Jih-Pyang Wang (1) - 关键词：Fal ; 002 ; 2 ; Phospholipase D ; RhoA ; Arf6 ; Protein kinase C ; Neutrophils ; Superoxide anion
- 刊名：Naunyn-Schmiedeberg's Archives of Pharmacology
- 出版年：2013
- 出版时间：June 2013
- 年：2013
- 卷：386
- 期：6
- 页码：507-519
- 全文大小：730KB
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Li-Jiau Huang (2)
Hui-Yi Lin (2)
Yun-Jie Hung (1)
Miau-Rong Lee (3)
Sheng-Chu Kuo (2)
Mei-Feng Hsu (3)
Jih-Pyang Wang (1)
1. Department of Medical Research, Taichung Veterans General Hospital, 160, Section 3, Chung Kang Road, Taichung, 407, Taiwan
2. Graduate Institute of Pharmaceutical Chemistry, China Medical University, Taichung, 404, Taiwan
3. Department of Biochemistry, China Medical University, Taichung, 404, Taiwan - ISSN：1432-1912
文摘
Three recently developed selective phospholipase D (PLD) inhibitors N-(2-(4-(2-oxo-2,3-dihydro-1H-benzo[d]imidazol-1-yl)piperidin-1-yl)ethyl)-2-naphthamide (VU0155056), (S)-N-(1-(4-(5-chloro-2-oxo-2,3-dihydro-1H-benzo[d]imidazol-1-yl)piperidin-1-yl)propan-2-yl)-2-naphthamide (VU0155069), and N-(2-(4-oxo-1-phenyl-1,3,8-triazaspiro[4,5]decan-8-yl)ethyl)quinoline-3-carboxamide (VU0285655-1) inhibited O2 ?? generation in formyl-Met-Leu-Phe (fMLP)-stimulated rat neutrophils. A novel 2-phenyl-4-quinolone compound 6-chloro-2-(2-chlorophenyl)-4-oxo-1,4-dihydroquinoline-3-carboxylate (Fal-002-2), which inhibited O2 ?? generation, also reduced the fMLP- but not phorbol ester-stimulated PLD activity (IC50 16.0?±-.0?μM). Fal-002-2 attenuated the interaction of PLD1 with ADP-ribosylation factor (Arf) 6, Ras homology (Rho) A and protein kinase C (PKC) isoforms (α, βI, and βII), and also inhibited the membrane recruitment of Arf6 and RhoA in fMLP-stimulated neutrophils, but not in GTPγS-stimulated cell-free system. The cellular levels of GTP-bound Arf6 and GTP-bound RhoA were reduced by Fal-002-2. Fal-002-2 also attenuated the membrane recruitment of Rho-associated protein kinase 1, phosphorylation of myosin light chain 2 at Thr18/Ser19 and PLD1 at Thr147, and the interaction of Arf6 with both arfaptin 1 and phosphatidylinositol 4-phosphate 5-kinase 1A. The association between RhoA and Vav, the interaction of Vav with both Lyn and Lck, the membrane recruitment of Vav, and the phosphorylation of Vav at Tyr174, but not Src family at Tyr416, were all attenuated by Fal-002-2 in fMLP-stimulated neutrophils. These results indicate that Fal-002-2 is not a direct PLD inhibitor, but the inhibition of fMLP-stimulated PLD activity by Fal-002-2, which partly accounts for its suppression of O2 ?? generation, is attributable to the blockade of both Arf6 and RhoA activation and attenuation of the interaction of Arf6, RhoA and PKC isoforms with PLD1 in rat neutrophils.