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The Journal of Immunology, Vol 141, Issue 2 476-482, Copyright © 1988 by American Association of Immunologists

ARTICLES

Direct identification of the murine IL-2 receptor p55-p75 heterodimer in the absence of IL-2

H Saragovi and TR Malek
Department of Microbiology and Immunology, University of Miami School of Medicine, FL 33101.

The proteins cross-linked to the IL-2R p55 subunit were biochemically compared in distinct cell populations that varied in their capacity to express high affinity IL-2R. We directly cross-linked p75 to p55 in the absence of IL-2 for the cell populations that bear only high affinity IL-2R. Furthermore, although no endogenous IL-2 production was detected, p75 was readily cross-linked to p55 for EL4J-3.4, a p55 transfectant of EL4 that bears high affinity IL-2R. These results strongly suggest that high affinity IL-2R exist as a preformed heterodimer of p55 and p75 which do not require IL-2 for their association. Furthermore, cross-linking of three other proteins of apparent Mr of 100,000, 135,000, and 180,000 to p55 was also seen, raising the possibility of a more complex subunit composition for the IL-2R.


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