Endocytosis of β2 integrins by stimulated human neutrophils analyzed by flow cytometry

J. D. Chambers, S. I. Simon, E. M. Berger, L. A. Sklar, K. E. Arfors

Research output: Contribution to journalArticlepeer-review

39 Scopus citations

Abstract

Flow cytometry and fluorescently labeled monoclonal antibodies were used to investigate endocytosis of human neutrophil β2 integrins following cellular activation. CD18 initially present on the cell surface cycled in two phases after exposure to formyl peptide or platelet-activating factor. The first phase lasted 3 min at 37°C; after a lag, CD18 was specifically internalized at approximately 20%/min. Subsequently a second phase was detectable consisting of exponential reduction of internal fluorescence with a half-time of approximately 2 min, representing probe reexpression. At peak endocytosis approximately 40% of CD18 was internalized. All of the internalized CD18 was associated with α(M) (CR3); no endocytosis of α(L) (LFA-1) was observed. When neutrophils were stimulated with phorbol esters or calcium ionophore, CD18 was internalized much more slowly(t( 1/2 ) 5 min) and probe was not reexpressed. Endocytosis of CD18 may participate in regulating neutrophil adhesiveness, removing activated receptors, or permitting receptor recycling.

Original languageEnglish (US)
Pages (from-to)462-469
Number of pages8
JournalJournal of Leukocyte Biology
Volume53
Issue number4
StatePublished - 1993

Keywords

  • CD18
  • fluorescent probe
  • internalization
  • monoclonal antibody
  • receptor cycling

ASJC Scopus subject areas

  • Cell Biology

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