The released interleukin 2 receptor binds interleukin 2 efficiently

The released interleukin 2 receptor (IL 2R) molecule was characterized in order to clarify its biochemical structure and to determine its functional capacity. Enzymatic digestions demonstrated that the released IL 2R, like the cell surface IL 2R, is a complex glycoprotein, modified by the addition o...

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Bibliographic Details
Published in:The Journal of immunology (1950) Vol. 137; no. 12; pp. 3841 - 3844
Main Authors: Rubin, LA, Jay, G, Nelson, DL
Format: Journal Article
Language:English
Published: Bethesda, MD Am Assoc Immnol 15-12-1986
American Association of Immunologists
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Summary:The released interleukin 2 receptor (IL 2R) molecule was characterized in order to clarify its biochemical structure and to determine its functional capacity. Enzymatic digestions demonstrated that the released IL 2R, like the cell surface IL 2R, is a complex glycoprotein, modified by the addition of both N- and O-linked carbohydrates and sialic acid residues. It has a peptide backbone that is approximately 10 Kd smaller than that of its membrane-associated counterpart. Affinity chromatography demonstrated that released IL 2R from either an HTLV-I-positive T cell line (HUT-102) or PHA-activated normal peripheral lymphocytes binds efficiently to purified recombinant IL 2. Furthermore, the interaction between the growth factor and the released receptor does not appear to require any accessory molecules. These observations suggest a potentially significant role for the released IL 2R in the regulation of IL 2-dependent lymphocyte functions.
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ISSN:0022-1767
1550-6606
DOI:10.4049/jimmunol.137.12.3841