Characterization of the human IL-5 receptors on eosinophils.
Interleukin 5 (IL-5) receptors on the cell surface of human eosinophils and other hematopoietic cells were characterized using radiolabeled recombinant IL-5. The binding of 35S-labeled murine IL-5 to eosinophils from normal human peripheral blood was rapid and saturable within a 30-min incubation at both 4 and 37 degrees C. The binding of 35S-labeled murine IL-5 to eosinophils was inhibited by an excess of unlabeled murine and human IL-5 or by an anti-murine IL-5 monoclonal antibody (NC17) but not by other human cytokines. Scatchard plot analysis revealed that human eosinophils have a single class of high affinity receptor (Kd 170-330 pM; number of binding sites: 260-380/cell). IL-5 receptors on eosinophils from four patients with eosinophilia displayed similar characteristics. Affinity cross-linking experiments resulted in the identification of human IL-5 receptor on eosinophils with a molecular mass of 55-60 kDa. Among the various cells besides eosinophils and cell lines that we could test, a subline of HL-60 (YY-1 cells) was found to display a significant number of IL-5 receptor. These results suggest that IL-5 may act on limited types of cells in the human system.
Migita
M
M
Department of Biology, Kumamoto University Medical School, Japan.
Yamaguchi
N
N
Mita
S
S
Higuchi
S
S
Hitoshi
Y
Y
Yoshida
Y
Y
Tomonaga
M
M
Matsuda
I
I
Tominaga
A
A
Takatsu
K
K
D000368:Aged; D000818:Animals; D004802:Eosinophilia / Q000209:etiology / Q000378:metabolism; D004804:Eosinophils / Q000737:chemistry* / Q000187:drug effects; D006801:Humans; D007223:Infant; D015848:Interleukin-5 / Q000378:metabolism* / Q000494:pharmacology; D008297:Male; D051379:Mice; D008970:Molecular Weight; D011971:Receptors, Immunologic / Q000032:analysis* / Q000378:metabolism; D018123:Receptors, Interleukin; D053649:Receptors, Interleukin-5
D015848:Interleukin-5; D011971:Receptors, Immunologic; D018123:Receptors, Interleukin; D053649:Receptors, Interleukin-5