Scientific article

Demonstration of two distinct forms of released low affinity-type rat IL-2 receptors

Published inImmunology, vol. 66, no. 3, p. 384-387
Publication date1989

The release of IL-2 binding proteins, derived from the 55,000 MW low affinity IL-2R (L chain), has been observed for virtually all L chain-bearing cells in either humans, the mouse or the rat. Based on the characterization of the released human L chain as a molecule 10,000 MW smaller than the cell surface receptor, either proteolytic cleavage or differential splicing of the L chain encoding mRNA have been suggested as mechanisms underlying the receptor release. Combining affinity labelling of the L chain with [125I]IL-2 and immunoprecipitation with L chain-specific monoclonal antibody (mAb) applied for the detection of soluble rat IL-2R revealed the existence of two classes of soluble receptors, one being of the same size as cell surface-expressed L chain, the other of 40,000 apparent molecular mass. These findings raise the possibility of other mechanisms of receptor release than those discussed for human L chain.

  • Affinity labels
  • Animals
  • Cultured cells
  • Molecular weight
  • Rats
  • Interleukin-2 receptors/isolation & purification
  • Solubility
  • T-lymphocytes/analysis
Affiliation Not a UNIGE publication
Citation (ISO format)
HERRMANN, Thomas et al. Demonstration of two distinct forms of released low affinity-type rat IL-2 receptors. In: Immunology, 1989, vol. 66, n° 3, p. 384–387.
Main files (1)
Article (Published version)
ISSN of the journal0019-2805

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