Kinetic study of interleukin-2 binding on the reconstituted interleukin-2 receptor complexes including the human gamma chain.

To gain an insight into roles of the interleukin-2 (IL-2) receptor gamma chain in IL-2 binding mechanisms, we examined association and dissociation rate constants for IL-2 binding with a series of fibroblastoid L929 cell lines expressing IL-2 receptor complexes reconstituted by transfection with the alpha, beta and gamma genes. The association rate constant (k) with the alpha beta gamma complex on L cells was fourfold larger than that with the alpha beta complex on L cells, and the dissociation rate constant (k') was one fifth of that with the alpha beta complex. These results indicate that the gamma chain is involved in both mechanisms by which IL-2 associates with and dissociates from receptors, resulting in the generation of the high-affinity IL-2 receptor along with the alpha and beta chains. During the course of this study, we found that the IL-2 dissociation from alpha beta gamma complex on lymphoid cells was a lot slower than that from the alpha beta gamma complex on fibroblast cells. A similar difference was observed with the beta gamma complex. These observations may indicate functional and constitutional differences of the high- and intermediate-affinity IL-2 receptor complexes between lymphoid and fibroblastoid cells.