Inhibition of formyl-methionyl-leucyl-phenylalanine-stimulated phospholipase D activation in rat neutrophils by the synthetic isoquinoline DMDI

Ling Chu Chang, Chi Ming Chen, Jih Pyang Wang

研究成果: 雜誌貢獻文章同行評審

6 引文 斯高帕斯(Scopus)

摘要

The expression of phospholipase D (PLD) isoenzymes in neutrophils was investigated using reverse transcription-polymerase chain reaction analysis. Amplification products of predicted size were obtained from rat neutrophils with nucleotide sequences corresponding to PLD1a and PLD2. 1-(3′,4′-Dimethoxybenzyl)-6,7-dichloroisoquinoline (DMDI) inhibited the formyl-methionyl-leucyl-phenylalanine (fMLP)-stimulated PLD activation in rat neutrophils. The underlying cellular signaling mechanism of DMDI inhibition was investigated. The fMLP-induced protein tyrosine phosphorylation and the membrane translocation of ADP-ribosylation factor (ARF) and Rho A in neutrophils was attenuated by DMDI in a concentration-dependent manner. However, neither the membrane association of protein kinase C-α and -β isoenzymes in fMLP-stimulated cells nor the GTPγS- and phorbol 12-myristate 13-acetate-stimulated membrane translocation of ARF and Rho A in a cell-free system was affected significantly by DMDI. These results indicate that the expression of PLD1a and PLD2 mRNA in neutrophils. Attenuation of protein tyrosine phosphorylation and the membrane association of ARF and Rho A probably play a concerted role in the inhibition of PLD by DMDI in rat neutrophils in response to fMLP.
原文英語
頁(從 - 到)191-198
頁數8
期刊Biochimica et Biophysica Acta - General Subjects
1620
發行號1-3
DOIs
出版狀態已發佈 - 三月 17 2003

ASJC Scopus subject areas

  • 生物化學
  • 生物物理學
  • 分子生物學

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