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Characterization of the high-affinity cell-surface receptor for murine B-cell-stimulating factor 1

Journal Article · · Proc. Natl. Acad. Sci. U.S.A.; (United States)
Radiolabeled recombinant murine B-cell-stimulatory factory 1 (BSF-1) was used to characterize receptors specific for this lymphokine on the surface of primary B and T cells and in vitro cell lines representing the B-cell, T-cell, mast cell, macrophage, and myelomonocytic lineages. BSF-1 binding was rapid and saturable at 4/sup 0/C and 37/sup 0/C with a slow dissociation rate. On all cell types examined, BSF-1 bound to a single class of high-affinity receptor (<20000 receptors per cell) with a K/sub a/ of 10/sup 10/-10/sup 11/ M/sup -1/. Receptor expression on resting primary B and T cells was low (<100 receptors per cell), whereas activation with lipopolysaccharide or Con A produced a 5- to 10-fold increase in receptor numbers. Among a panel of lymphokines and growth hormones, only unlabeled BSF-1 was able to compete for the binding of /sup 125/I-labeled BSF-1. Affinity crosslinking experiments resulted in the identification on all cells tested on a receptor protein with an average M/sub r/ of 75,000.
Research Organization:
Immunex Corp., Seattle, WA
OSTI ID:
5903526
Journal Information:
Proc. Natl. Acad. Sci. U.S.A.; (United States), Journal Name: Proc. Natl. Acad. Sci. U.S.A.; (United States) Vol. 84:6; ISSN PNASA
Country of Publication:
United States
Language:
English