Evidence for a Low-Affinity Interleukin-3 Receptor

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Abstract
Interleukin-3 (IL-3) regulates the proliferation of myeloid, erythroid, and lymphoid cells. Previous reports showed IL-3 binding restricted to a single high-affinity (Kd = 50-200 pM) site. Here, we demonstrate by equilibrium studies an additional binding site for IL-3 with lower apparent affinity (Kd = 5-20 nM). Furthermore, kinetic analysis shows that two binding sites for IL-3 exist: IL-3 dissociates slowly from the first site (T1/2 = 4 hr; k-1 = 2.7 x 10(-3) min-1), whereas it dissociates rapidly (T1/2 = 4.0 min; k-1 = 0.116 min-1) from the second site. Cross-linking showed that [125I]IL-3 binding to the 115- and 140-kD proteins was not saturable at concentrations commensurate with high-affinity binding and IL-3 dissociated rapidly from these same molecules. Thus, the low affinity IL-3 receptor is a molecule(s) of 115- to 140-kD.