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Characterization of high-affinity receptors for interleukin 5 on interleukin 5-dependent cell lines

Journal Article · · Proceedings of the National Academy of Sciences of the United States of America; (USA)
Interleukin 5 (IL-5) is a glycosylated polypeptide that acts as a key factor for B-cell growth and differentiation. The authors demonstrated previously that there are two classes (high and low affinity) of IL-5 receptors on murine chronic B-cell leukemic cells (BCL{sub 1}-B20). Treatment of surface-bound radiolabeled IL-5 with bivalent crosslinkers identified a polypeptide of M{sub r} 92,500. In this study, the authors analyzed characteristics of high-affinity IL-5 receptors on IL-5-dependent early B-cell lines (T-88 and T88-M), mouse myeloma cells (MOPC-104E), and BCL{sub 1}-B20 cells. All cell lines had two classes of IL-5 binding sites, but T88-M cells bore the highest number of high-affinity receptors. Disuccinimidyl tartarate crosslinking of {sup 35}S-labeled IL-5 to the receptors on the T88-M and lipopolysaccharide-stimulated BCL{sub 1}-B20 cells revealed two major {sup 35}S-labeled components of M{sub r} 92,500 and M{sub r} 160,000, even when the binding of {sup 35}S-labeled IL-5 was carried out under high-affinity conditions. The M{sub r} 92,500 component, but not the M{sub r} 160,000 component, was detected in the lysates of MOPC-104E and T-88 cells, both of which bore a large number of low-affinity receptors and a limited number of high-affinity receptors. The results suggest that the M{sub r} 92,500 component represents the complex of IL-5 with the low-affinity M{sub r} 46,500 receptor, whereas the high-affinity receptor consists of the M{sub r} 46,500 peptide and an additional peptide.
OSTI ID:
5353193
Journal Information:
Proceedings of the National Academy of Sciences of the United States of America; (USA), Journal Name: Proceedings of the National Academy of Sciences of the United States of America; (USA) Vol. 86:7; ISSN 0027-8424; ISSN PNASA
Country of Publication:
United States
Language:
English