Regulating phospholipase C activity in human neutrophils

Wan K. Kim-Park, Michelle A. Moore, Michael J. Kowolik

Research output: Contribution to journalArticlepeer-review

Abstract

Bacterial-derived formylated peptide, (FMLP) stimulates the respiratory burst activity of human neutrophils via phospholipase C (PLC) activation followed by increased production of second messengers, IP3 and DG 1. One synthetic bisphosphonate, clodronate was tested to see how it might affect Ca2+-mediated activation of the neutrophil respiratory burst. Clodronate itself did not significantly change the respiratory burst, measured by Luminol-dependent chemiluminescence (CL). However, clodronate inhibited the FMLP-mediated stimulation of CL significantly (p<0.001). A selective inhibitor of PLC, quinacrine, alone inhibited CL significantly (p<0.0001) but with clodronate the inhibition was potentiated. The sensitivity to EGTA-treatment with clodronate indicated that clodronate is a Ca2+ mobilizing agent. Furthermore, clodronate-mediated CL was sensitive (p<0.001) to inhibitors of protein kinase C or tyrosine kinase and potentiated with vanadate treatment. Data suggests possible involvement of bisphosphonate in regulating phospholipase C activity in human neutrophils, probably via Ca2+-mediated phosphorylation of the subunit of PLC.

Original languageEnglish (US)
Pages (from-to)675-679
Number of pages5
JournalPhosphorus, Sulfur and Silicon and Related Elements
Volume144-146
DOIs
StatePublished - Jan 1 1999

Keywords

  • Bisphosphonate
  • Neutrophil
  • Phospholipase c

ASJC Scopus subject areas

  • Biochemistry
  • Organic Chemistry
  • Inorganic Chemistry

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