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| Content Provider | PubMed Central |
|---|---|
| Author | Robb, R. J. |
| Abstract | The cellular receptors for interleukin 2 (IL-2) exist in at least two forms, one with a particularly high affinity and a second, more numerous class, with a much lower affinity for IL-2. Indirect evidence suggests that both classes of receptors use the same p55 glycoprotein as their ligand-binding component. L cells transfected with cDNA encoding this protein, however, displayed only low-affinity IL-2 binding. To determine if such receptors could be converted to a high-affinity state, L-cell membranes containing the murine p55 protein were fused with membranes from human T cells displaying high-affinity receptors. The anti-Tac antibody was used to block ligand binding to human p55 on the fusion product. The results showed that a fraction of the murine p55 chains were converted to a dramatically higher affinity following fusion. Fusion of the L-cell membranes with themselves or with membrane preparations from human T-cell lines lacking the IL-2 receptor resulted in little or no affinity modulation. One explanation of the results is that cofactors present in receptor-positive T-cell lines crossed species lines and combined with the murine p55 chain to create "high-affinity" binding sites. Thus, depending upon its environment, the same p55 molecule can apparently form either a low- or high-affinity IL-2 receptor. |
| Starting Page | 3992 |
| File Format | |
| ISSN | 10916490 |
| e-ISSN | 10916490 |
| Journal | Proceedings of the National Academy of Sciences of the United States of America |
| Issue Number | 11 |
| Volume Number | 83 |
| Language | English |
| Publisher Date | 1986-06-01 |
| Access Restriction | Open |
| Subject Keyword | Research in Higher Education |
| Content Type | Text |
| Resource Type | Article |
| Subject | Multidisciplinary |
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