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Secreted form of the human interleukin 2 receptor encoded by an anchor minus cDNA

Journal Article · · J. Immunol.; (United States)
OSTI ID:5389590
The DNA sequence encoding all of the putative intracytoplasmic domain and most of the trans-membrane domain of the huma IL 2 receptor was detected from a full length receptor cDNA. After expression in mouse L cells, the resultant anchor minus cDNA was found to direct the synthesis of a secreted rather than membrane-associated form of the IL 2 receptor. The secreted receptor protein (44,000 to 46,000 M/sub r/) retained the capacity to bind both IL 2 and the monoclonal anti-Tac antibody, as evidenced by (1) retention on IL 2 and anti-Tac affinity columns, (2) inhibition of (/sup 3/H)-antiTac binding to HUT 102B2 cells, and (3) partial inhibition of IL 2-induced CTLL proliferation. Removal of these domains from the IL 2 receptor did not alter the post-translational processing or rate of export of the truncated receptor protein. These data confirm the proposed membrane orientation of the IL 2 receptor (NH/sub 2/ terminus out, COOH terminus in) and underscore the anchoring function of this carboxy terminal receptor segment. The availability of such anchor minus receptor cDNA constructs may facilitate purification of large quantities of receptor protein for further analysis of receptor structure, valency, and localization of the IL 2 binding site(s).
Research Organization:
National Institutes of Health, Bethesda, MD
OSTI ID:
5389590
Journal Information:
J. Immunol.; (United States), Journal Name: J. Immunol.; (United States) Vol. 136:11; ISSN JOIMA
Country of Publication:
United States
Language:
English