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Interleukin 3 activates human blood basophils via high-affinity binding sites

Journal Article · · Proceedings of the National Academy of Sciences of the United States of America; (USA)
Pure populations of human basophilic granulocytes were obtained from chronic myeloid leukemia (CML) blood by negative selection using a mixture of monoclonal antibodies and complement. {sup 125}I-radiolabeled recombinant human interleukin 3 (rhIL-3) bound to purified basophils in a specific manner. Quantitative binding studies and Scatchard plot analyses performed on samples from two donors revealed the presence of a single class of high-affinity IL-3 binding sites. Purified CML basophils maintained in suspension in the presence of rhIL-3 incorporated up to 12 times more ({sup 3}H)thymidine than basophils in control cultures. Furthermore, after preincubation in vitro with rhIL-3 for 30 min, normal blood basophils released 2- to 3-fold more histamine than basophils pretreated with control medium when exposed to various concentrations of an anti-IgE antibody. Together, these results show that rhIL-3 binds to a specific receptor on blood basophils and is a regulator of basophil function.
OSTI ID:
5264134
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. 86:14; ISSN PNASA; ISSN 0027-8424
Country of Publication:
United States
Language:
English