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Interleukin 1. cap alpha. and interleukin 1. beta. bind to the same receptor on T cells

Journal Article · · J. Immunol.; (United States)
OSTI ID:5783789
Pure, E. coli-derived recombinant murine interleukin 1..cap alpha.. (IL 1..cap alpha..) was labeled with /sup 125/I and used for receptor binding studies. The /sup 125/I-IL 1 binds to murine EL-4 thymoma cells in a specific and saturable manner. Scatchard plot analysis for binding studies carried out at 4/sup 0/C reveals a single type of high affinity binding site with an apparent dissociation constant of approximately 2.6 X 10/sup -10/ M and the presence of approximately 1200 binding sites per cell. Unlabeled recombinant murine IL 1 competes for /sup 125/I-IL 1 binding in a dose-dependent manner, whereas interferon-..cap alpha..A, interleukin 2 (IL 2), epidermal growth factor, and nerve growth factor have no effect. The /sup 125/I-IL 1 binding site is sensitive to trypsin, suggesting that it is localized on the cell surface. The authors have also examined the ability of purified recombinant human IL 1..cap alpha.. and IL 1..beta.. to compete for binding of the radiolabeled murine IL 1 to its receptor and to stimulate IL 2 production by EL-4 cells. They report here that both human IL 1 proteins are able to recognize the same binding site on mouse IL 1. In addition, murine as well as both human IL 1 proteins stimulate IL 2 production by EL-4 cells.
Research Organization:
Hoffmann-La Roche, Inc., Nutley, NJ
OSTI ID:
5783789
Journal Information:
J. Immunol.; (United States), Journal Name: J. Immunol.; (United States) Vol. 136; ISSN JOIMA
Country of Publication:
United States
Language:
English