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Related Experiment Videos

Cloning of complementary DNA encoding a functional human interleukin-8 receptor.

P M Murphy1, H L Tiffany

  • 1Laboratory of Host Defenses, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, MD 20892.

Science (New York, N.Y.)
|September 13, 1991
PubMed
Summary

Researchers identified a novel human Interleukin-8 (IL-8) receptor (p2) from HL-60 neutrophils. This receptor binds IL-8 and triggers calcium mobilization in Xenopus oocytes.

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Calcium flux assay in Xenopus oocytes.

Current protocols in neuroscience·2008

Area of Science:

  • Immunology
  • Cell Biology
  • Molecular Biology

Background:

  • Interleukin-8 (IL-8) is a key inflammatory cytokine.
  • IL-8 mediates neutrophil functions like chemotaxis and respiratory burst.
  • Neutrophil IL-8 receptors are G protein-coupled and trigger intracellular calcium release.

Purpose of the Study:

  • To isolate and characterize a cDNA clone encoding a human IL-8 receptor.
  • To confirm the functional expression of the identified IL-8 receptor.

Main Methods:

  • cDNA cloning from HL-60 neutrophils.
  • Expression of the clone (p2) in Xenopus laevis oocytes.
  • Binding assays with 125I-labeled IL-8.
  • Measurement of calcium mobilization in response to IL-8.

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Main Results:

  • A cDNA clone, p2, encoding a human IL-8 receptor was isolated.
  • Xenopus oocytes expressing p2 specifically bound 125I-IL-8.
  • IL-8 induced calcium store mobilization in expressing oocytes with an EC50 of 20 nM.
  • The p2 receptor showed 77% amino acid identity to another human IL-8 receptor isotype and 69% to a rabbit N-formyl peptide receptor.

Conclusions:

  • The p2 clone represents a functional human IL-8 receptor.
  • This receptor plays a role in neutrophil inflammatory responses.
  • The findings provide insights into G protein-coupled receptor diversity and function.