Related Experiment Videos
Cloning the interleukin 1 receptor from human T cells
J E Sims1, R B Acres, C E Grubin
1Immunex Corp., Seattle, WA 98101.
Summary
Researchers isolated cDNA clones for the human interleukin 1 (IL-1) receptor, finding high sequence conservation with the mouse receptor. This integral membrane protein functions similarly in T-cells and fibroblasts, binding IL-1 with distinct affinity classes.
Area of Science:
- Immunology
- Molecular Biology
- Cell Biology
Background:
- The interleukin 1 (IL-1) receptor mediates crucial immune responses.
- Understanding human IL-1 receptor structure and function is vital for targeted therapies.
Purpose of the Study:
- To isolate and characterize cDNA clones of the human IL-1 receptor.
- To compare the human IL-1 receptor with its murine counterpart.
- To investigate the functional expression of the human IL-1 receptor.
Main Methods:
- Isolation of human IL-1 receptor cDNA using a murine probe.
- DNA sequencing and comparative analysis.
- Transfection of COS cells with human IL-1 receptor cDNA.
- Characterization of receptor binding affinities.
Main Results:
- High sequence conservation between human and murine IL-1 receptors.
- Human IL-1 receptor is an integral membrane protein with conserved structural domains (cytoplasmic, transmembrane, extracellular).
- Transfected human IL-1 receptor cDNA expressed two IL-1 binding affinity classes in COS cells, matching native T-cell receptors.
- Identical IL-1 receptor sequences were found in human T-cells and dermal fibroblasts.
Conclusions:
- The human IL-1 receptor shares significant structural and functional similarities with the mouse receptor.
- The cloned human IL-1 receptor cDNA accurately reflects native receptor characteristics, including affinity states.
- The IL-1 receptor is expressed identically in different human cell types, suggesting a conserved role in immune signaling.