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Title: Properties of an EBV-B cell line derived interleukin 1 (IL 1) receptor

Conference · · Fed. Proc., Fed. Am. Soc. Exp. Biol.; (United States)
OSTI ID:5392937

The properties of an human IL 1 receptor on a human EBV-B line were studied. Purified human IL 1-..beta.. produced by a myelomonocytic cell line (THP-1) was labeled with /sup 125/I by the Bolton-Hunter method without loss of biological activity. Among four EBV-B cell lines tested, a pre-B cell type (VDS-O) specifically bound the most /sup 125/I IL-..beta... Maximal binding was reached within 20 min at 4/sup 0/C. Scatchard analysis of the binding of /sup 125/I-IL 1-..beta.. to VDS-O cells yielded a Kd of 2.4-5.9 x 10/sup -00/ M with 110 to 220 binding (receptor) sites/cell. The binding of /sup 125/I-IL 1-..beta.. to VDS-O cells was inhibited by anti-human IL 1 antibody, natural and recombinant human IL 1-..cap alpha.. as well as IL 1-..beta.., but not by IFN-..cap alpha.., TNF, or LT, suggesting that IL 1-..cap alpha.. and IL 1-..beta.. specifically bind to the same receptor. The mw of the IL 1 receptor on human EBV-B cells was estimated to be 60 Kd both by a chemical crosslinking method and by HPLC gel filtration analysis of solubilized receptor extracted from membranes by a nonionic detergent (CHAPS). The pI of solubilized human IL 1 receptor was 7.3 by HPLC chromatofocusing. Data showing that VDS-O cells proliferate in response to exogenously added IL 1, express IL 1 receptors and also produce IL 1 all support the hypothesis that IL 1 may function as an autocrine signal for B lymphocytes.

Research Organization:
Lab. of Molecular Immunoregulation, Frederick, MD
OSTI ID:
5392937
Report Number(s):
CONF-8604222-
Journal Information:
Fed. Proc., Fed. Am. Soc. Exp. Biol.; (United States), Vol. 45:3; Conference: 70. annual meeting of the Federation of American Society for Experimental Biology, St. Louis, MO, USA, 13 Apr 1986
Country of Publication:
United States
Language:
English

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