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Self‐association of interleukin 2 bound to its receptor 1
Author(s) -
Kaplan David,
Smith Dawn,
Huang Robert,
Yildirim Zafer
Publication year - 1995
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.9.11.7649410
Subject(s) - association (psychology) , interleukin 2 , interleukin 12 receptor, beta 1 subunit , interleukin 4 receptor , receptor , chemistry , interleukin 21 receptor , psychology , biochemistry , psychotherapist
Although radioiodinated interleukin 2 (IL‐2) has been used to define the binding characteristics of the cytokine to the α chain of the receptor complex, we have found that unsubstituted IL‐2 behaves differently. Whereas previous investigations with radioiodinated IL‐2 have shown binding to the a chain with a Kd of 10 nM, we show that unsubstituted IL‐2 binds to the a chain but does not reach saturation between 100 and 1000 nM. The explanation for the discrepancy between the analysis of radioiodinated and unsubstituted cytokine involves the propensity of unsubstituted IL‐2 for self‐association, a property that is abrogated by radioiodination. The functional relevance of our findings is indicated by the different capacities of unsubstituted and iodinated cytokine to induce prolonged proliferation of human T lymphocytes.—Kaplan, D., Smith, D., Huang, R., Yildirim, Z. Self‐association of interleukin 2 bound to its receptor. FASEBJ. 9, 1096‐1102 (1995)