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Characterization of factor H binding to human polymorphonuclear leukocytes

V M Avery1, D L Gordon

  • 1Department of Microbiology and Infectious Diseases, Flinders Medical Centre, Bedford Park, Australia.

Journal of Immunology (Baltimore, Md. : 1950)
|November 15, 1993
PubMed
Summary

Factor H (fH) specifically binds to polymorphonuclear leukocytes (PMN), suggesting a novel receptor (fHR) on these cells. This interaction may influence immune responses and cell protection.

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Area of Science:

  • Immunology
  • Cell Biology

Background:

  • Factor H (fH) is known to interact with various cell types, with functions beyond complement regulation.
  • The specific binding mechanisms and cellular receptors for fH on immune cells are not fully elucidated.

Purpose of the Study:

  • To investigate the binding of factor H (fH) to polymorphonuclear leukocytes (PMN).
  • To characterize the nature of fH binding to PMN and identify potential receptors.

Main Methods:

  • Flow cytometry and radiolabeled binding assays were employed to quantify fH binding to PMN.
  • Binding assays were performed under varying ionic strengths and in the presence of divalent cations.
  • PMN stimulation and fragment inhibition studies were conducted to understand binding characteristics.

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Main Results:

  • Specific and saturable binding of fH to PMN was observed, with approximately 6 x 10^4 binding sites/PMN and a Ka of 3.3 x 10^8 L/M.
  • fH binding to PMN was dependent on ionic strength, required divalent cations, and was enhanced by PMN stimulation.
  • A 38-kDa N-terminal fragment of fH bound to PMN, and blocking studies indicated the fifth SCR domain of fH is involved in receptor interaction.
  • Binding was independent of surface-bound C3 or CR3, and fH also bound to U937 and Raji cells, but not T cells.

Conclusions:

  • These findings provide presumptive evidence for a novel factor H receptor (fHR) on PMN.
  • fH binding to PMN via fHR may play roles in enhancing target recognition, initiating intracellular signaling, or protecting cells from complement-mediated damage.