IL-1β primes IL-8-activated human neutrophils for elastase release, phospholipase D activity, and calcium flux

Laura Brandolini, Riccardo Bertini, Cinzia Bizzarri, Rita Sergi, Gianfranco Caselli, Dan Zhou, Massimo Locati, Silvano Sozzani

Research output: Contribution to journalArticlepeer-review


Interleukin-8 (IL-8), the prototype of the a (i.e., C-X-C branch) chemokine family, induced elastase release in a concentration-dependent manner (50-1000 ng/mL) in cytochalasin B-treated human polymorphonuclear leukocytes (PMNs). This response was potentiated about twofold if PMNs were preexposed to interleukin-1β (IL-1β) at concentrations that were by themselves inactive. The effect of IL-1β was clearly observed after 5 min and was maximal after a 30-min preincubation of the cells. The effect was present over the whole active concentration range of IL-8 and was completely blocked by the presence of IL-1 receptor antagonist. Priming of elastase release by IL-1β was not associated with a change in receptor number or affinity for IL-8. On the contrary, it was correlated with priming of phospholipase D activity and calcium flux activated by IL-8. Preincubation of the cells with ethanol and/or La3+ inhibited IL-8-induced degranulation, suggesting that activation of phospholipase D and increase of [Ca2+]i were important for this response. In contrast, ethanol and La3+ did not decrease the priming effect of IL-1β. IL-8 and IL-1β have been shown to be released by the same cell types and may be concomitantly present at sites of inflammation, giving rise to an amplification of the inflammatory response.

Original languageEnglish
Pages (from-to)427-434
Number of pages8
JournalJournal of Leukocyte Biology
Issue number3
Publication statusPublished - Mar 1996


  • Calcium flux
  • Cytochalasin B
  • Elastase
  • Ethanol
  • Interleukin-1β
  • La
  • Neutrophils
  • Phospholipase D

ASJC Scopus subject areas

  • Cell Biology


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