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20965153

Source:http://linkedlifedata.com/resource/pubmed/id/20965153

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pubmed-article:20965153pubmed:abstractTextA selective phospholipase D (PLD) inhibitor 5-fluoro-2-indolyl des-chlorohalopemide (FIPI) inhibited the O(2)(-) generation and cell migration but not degranulation in formyl-Met-Leu-Phe (fMLP)-stimulated rat neutrophils. A novel benzyl indazole compound 2-benzyl-3-(4-hydroxymethylphenyl)indazole (CHS-111), which inhibited O(2)(-) generation and cell migration, also reduced the fMLP- but not phorbol ester-stimulated PLD activity (IC(50) 3.9±1.2?M). CHS-111 inhibited the interaction of PLD1 with ADP-ribosylation factor (Arf) 6 and Ras homology (Rho) A, and reduced the membrane recruitment of RhoA in fMLP-stimulated cells but not in GTP?S-stimulated cell-free system. CHS-111 reduced the cellular levels of GTP-bound RhoA, membrane recruitment of Rho-associated protein kinase 1 and the downstream myosin light chain 2 phosphorylation, and attenuated the interaction between phosphatidylinositol 4-phosphate 5-kinase (PIP5K) and Arf6, whereas it only slightly inhibited the guanine nucleotide exchange activity of human Dbs (DH/PH) protein and did not affect the arfaptin binding to Arf6. CHS-111 inhibited the interaction of RhoA with Vav, the membrane association and the phosphorylation of Vav. CHS-111 had no effect on the phosphorylation of Src family kinases (SFK) but attenuated the interaction of Vav with Lck, Hck, Fgr and Lyn. CHS-111 also inhibited the interaction of PLD1 with protein kinase C (PKC) ?, ?I and ?II isoenzymes, and the phosphorylation of PLD1. These results indicate that inhibition of fMLP-stimulated PLD activity by CHS-111 is attributable to the blockade of RhoA activation via the interference with SFK-mediated Vav activation, attenuation of the interaction of Arf6 with PLD1 and PIP5K, and the activation of Ca(2+)-dependent PKC in rat neutrophils.lld:pubmed
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pubmed-article:20965153pubmed:authorpubmed-author:WangJih-Pyang...lld:pubmed
pubmed-article:20965153pubmed:authorpubmed-author:ChangLing-Chu...lld:pubmed
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pubmed-article:20965153pubmed:authorpubmed-author:ChangChi-SenC...lld:pubmed
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pubmed-article:20965153pubmed:authorpubmed-author:LinRuey-Hseng...lld:pubmed
pubmed-article:20965153pubmed:authorpubmed-author:HuangTai-Hung...lld:pubmed
pubmed-article:20965153pubmed:authorpubmed-author:TsaiYa-RuYRlld:pubmed
pubmed-article:20965153pubmed:authorpubmed-author:LeePin-WenPWlld:pubmed
pubmed-article:20965153pubmed:copyrightInfo2010 Elsevier Inc. All rights reserved.lld:pubmed
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pubmed-article:20965153pubmed:year2011lld:pubmed
pubmed-article:20965153pubmed:articleTitleSignaling mechanisms of inhibition of phospholipase D activation by CHS-111 in formyl peptide-stimulated neutrophils.lld:pubmed
pubmed-article:20965153pubmed:affiliationInstitute of Medicine, Chung Shan Medical University, Taichung, Taiwan, ROC.lld:pubmed
pubmed-article:20965153pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:20965153pubmed:publicationTypeResearch Support, Non-U.S. Gov'tlld:pubmed
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