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High affinity binding of human interleukin 4 to cell lines
H Cabrillat1, J P Galizzi, O Djossou
1UNICET, Laboratory for Immunological Research, Dardilly, France.
Biochemical and Biophysical Research Communications
|December 31, 1987
Summary
Radioiodinated interleukin 4 (IL-4) specifically binds to Burkitt lymphoma cells, revealing approximately 1200-1400 receptors per cell. This binding affinity correlates with IL-4
Area of Science:
- Immunology
- Cell Biology
- Biochemistry
Background:
- Interleukin 4 (IL-4) is a key cytokine in immune responses.
- Understanding IL-4 receptor interactions is crucial for immune modulation.
Purpose of the Study:
- To characterize the binding of purified human recombinant IL-4 to specific cell surface receptors.
- To determine the affinity and number of IL-4 receptors on Jijoye cells.
Main Methods:
- Radioiodination of purified human recombinant IL-4 to create 125I-IL-4.
- Binding assays using 125I-IL-4 on Jijoye cells and other cell lines.
- Competition assays with other lymphokines to assess binding specificity.
Main Results:
- 125I-IL-4 demonstrated specific binding to Burkitt lymphoma Jijoye cells.
- Jijoye cells possess high-affinity IL-4 receptors (Kd ≈ 7 x 10^-11 M) with 1200-1400 sites/cell.
- IL-4 receptor binding affinity correlates with Fc epsilon RL/CD23 expression.
- Only IL-4 competed for its own receptor binding, indicating high specificity.
Conclusions:
- Human recombinant IL-4 binds with high affinity to specific receptors on Jijoye cells.
- The number and affinity of these receptors are quantified.
- These findings provide a basis for understanding IL-4's role in cellular signaling and immune regulation.