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

Research output: Contribution to journalArticlepeer-review

6 Citations (Scopus)

Abstract

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.

Original languageEnglish
Pages (from-to)191-198
Number of pages8
JournalBiochimica et Biophysica Acta - General Subjects
Volume1620
Issue number1-3
DOIs
Publication statusPublished - Mar 17 2003

Keywords

  • ADP-ribosylation factor
  • Neutrophil
  • Phospholipase D1a
  • Phospholipase D2
  • Protein tyrosine phosphorylation
  • Rho A

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

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