Activation of the β2 integrin Mac-1 (CD11b/CD18) by an endogenous lipid mediator of human neutrophils and HL-60 cells

Katja Klugewitz, Klaus Ley, Detlef Schuppan, Rolf Nuck, Peter Gaehtgens, Barbara Walzog

Research output: Contribution to journalArticlepeer-review

9 Scopus citations


β2 integrins (CD11/CD18) play a key role in the adhesion, activation, migration and phagocytosis of human neutrophils. In order to exert their functions, β2 integrins require activation, which results in an enhancement of ligand affinity. This functional up-regulation is probably due to a conformational change of the β2 integrins, but the mechanisms of inside-out signaling that trigger this activation are still under investigation. In the present study, the effect of cellular lipids on the affinity state of β2 integrins was investigated. Lipids were extracted from human neutrophils and HL-60 cells after stimulation with IL-8 or phorbol ester, respectively. The extracts were purified by anion exchange chromatography and/or HPLC fractionation. The lipid extracts induced the adhesion of neutrophils to fibrinogen and, in a cell-free assay system, the binding of C3bi-coated zymosan-particles by purified β2 integrin Mac-1 (CD11b/CD18). The integrin up-regulating activity was resistant to ester hydrolysis, eluted as one particular HPLC-fraction, and showed an absorption maximum at 194 ± 2 nm. Taken together, these data support the concept that activated neutrophils and HL-60 cells can generate an endogenous lipid mediator, which up-regulates ligand binding activity of β2 integrins.

Original languageEnglish (US)
Pages (from-to)985-990
Number of pages6
JournalJournal of Cell Science
Issue number8
StatePublished - 1997
Externally publishedYes


  • Adhesion
  • CD11/CD18
  • Inflammation
  • Integrin
  • Neutrophil

ASJC Scopus subject areas

  • Cell Biology


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