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The Journal of Immunology, Vol 145, Issue 8 2494-2499, Copyright © 1990 by American Association of Immunologists

ARTICLES

Functional and biochemical characterization of mouse P40/IL-9 receptors

C Druez, P Coulie, C Uyttenhove and J Van Snick
Unit of Experimental Medicine, University of Louvain, Brussels, Belgium.

The existence of saturable and specific binding sites for mouse P40/IL- 9 was demonstrated on a variety of factor-dependent T cell lines derived from Th clones by long term culture in the presence of P40- containing T cell supernatants. Scatchard transformation of the data obtained with one such line was consistent with the existence of a single class of receptors with a Kd of approximately 100 pM and a density of 3000/cell. P40 binding to these cells was followed by rapid internalization of the ligand. P40-receptors (P40-R)3 were also found on certain Th clones maintained in conventional cultures, especially after stimulation with Ag and APC. Only T cell clones that proliferated in response to P40 showed significant levels of binding, suggesting that the regulation of P40-R expression is an important element in the control of P40-responsiveness. In accord with this idea, fresh T cells, cytolytic T cell clones and a wide variety of other cells including B cells and fibroblasts, which do not proliferate in response to P40, showed no significant binding. However, P40-R were not restricted to a few unusual Th clones. They were also detected on several T cell tumors, on macrophages and on mast cell lines. The latter point is of particular interest in view of the mast cell growth factor activity recently ascribed to P40. Cross-linking studies with T-cell lines and mast cells indicated that the P40-R consists of a 64-kDa glycoprotein, the molecular mass of which is reduced to 54 kDa on treatment with N- glycosidase F.


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