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A soluble interleukin 2 receptor produced by a normal alloreactive human T cell clone binds interleukin 2 with low
Y Jacques1, B Le Mauff, F Boeffard
1Institut National de la Santé et de la Recherche Médicale (INSERM U211), Nantes, France.
Journal of Immunology (Baltimore, Md. : 1950)
|October 1, 1987
Summary
Researchers studied soluble interleukin 2 receptors (IL-2R) produced by human T cells. They found this soluble IL-2R binds IL-2 similarly to low-affinity cell-surface receptors and lacks high-affinity binding sites.
Area of Science:
- Immunology
- Molecular Biology
Background:
- Alloreactive T cells from kidney grafts produce soluble interleukin 2 receptors (IL-2R).
- Soluble IL-2R plays a role in immune responses and T cell activation.
Purpose of the Study:
- To characterize the soluble IL-2R produced by a specific human T cell clone (2B11).
- To compare the binding properties of soluble IL-2R with cell-surface IL-2R for IL-2 and anti-IL-2R monoclonal antibodies (mAb).
Main Methods:
- Purification of soluble IL-2R from T cell culture supernatants using affinity chromatography.
- Analysis of soluble IL-2R structure and molecular weight via SDS-PAGE.
- Characterization of binding kinetics using immunoradiometric assays (IRMA) with anti-IL-2R mAb and IL-2.
Main Results:
- Purified soluble IL-2R is a single chain of 35-45 kDa.
- Soluble IL-2R exhibits identical mAb binding affinities and stoichiometry to cell-surface IL-2R (Tac antigen).
- Soluble IL-2R binds IL-2 with low affinity (KD = 30 nM) and lacks high-affinity binding sites, unlike cell-surface IL-2R.
Conclusions:
- The soluble IL-2R produced is likely an extracellular fragment of the Tac antigen.
- The characterized soluble IL-2R does not significantly impact IL-2-induced T cell proliferation.
- Findings provide insights into the function and implications of soluble IL-2R in immune regulation.