An associated molecule, p64, with high-affinity interleukin 2 receptor.
1990
: TU11 mAb specific for the human interleukin-2 receptor (IL-2R) beta-chain, p75, co-precipitated two molecules, p64 and p55, with the beta-chain in the lysates of cells bearing the high-affinity IL-2R. The co-precipitation was detected in the presence of IL-2 even in the absence of a chemical cross-linker. H-48 mAb specific for the IL-2R alpha-chain completely pre-absorbed p64 as well as p55 and partially pre-absorbed the beta-chain from the lysates. The co-precipitation was also detected in phytohemagglutinin-stimulated normal peripheral blood lymphocytes, which express the high-affinity IL-2R, but not in the cell line cells bearing only the low-affinity IL-2R. The peptide maps indicate that p64 is a molecule distinct from both the alpha- and beta-chains, and that p55 is identical to the alpha-chain. These findings suggest that p64, along with the alpha- and beta-chains, is a component of the high affinity IL-2R complex, and we have tentatively named it the gamma-chain of IL-2R.
Keywords:
- Interleukin 1 receptor, type I
- Interleukin 12 receptor, beta 1 subunit
- Interleukin 8 receptor, alpha
- Interleukin 26
- Interleukin-6 receptor
- Molecular biology
- High Affinity Interleukin-2 Receptor
- Interleukin 1 receptor, type II
- Biology
- Interleukin
- Interleukin 10 receptor, alpha subunit
- Interleukin 10
- Interleukin 5 receptor alpha subunit
- Receptor
- Interleukin-4 receptor
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