Fulltext

Molecular characterization of the β chain of the murine interleukin 5 receptor

Mita, Seiji ; Takaki, Satoshi ; Hitoshi, Yasumichi ; Rolink, Antonius G. ; Tominaga, Akira ; Yamaguchi, Naoto ; Takatsu, Kiyoshi

In: International Immunology, 1991, vol. 3, no. 7, p. 665-672

Aggiungi alla tua lista
    Titre
    • Molecular characterization of the β chain of the murine interleukin 5 receptor
    Auteur
    • Mita, Seiji
    • Takaki, Satoshi
    • Hitoshi, Yasumichi
    • Rolink, Antonius G.. Basel Institute for Immunology Grenzacherstrasse, Basel, Switzerland
    • Tominaga, Akira
    • Yamaguchi, Naoto
    • Takatsu, Kiyoshi. Department of Biology, Institute for Medical Immunology, Kumomoto University Medical School, 2-2-1 Honjo, Kumamoto 860, Japan, Grenzacherstrasse, Basel, Switzerland
    Type de document
    • Postprint
    Langue
    • Inglese
    Publié dans
    • International Immunology, 1991, vol. 3, no. 7, p. 665-672. Oxford University Press
    Autre version électronique
    Identifiant OAI-PMH
    • oai:doc.rero.ch:304837
    Summary
    Interleukin 5 (IL-5) is a multifunctional cytokine that regulates the proliferation and differentiation of hematopoietlc cells Including B cells and eosinophlls. The murine IL-5 acts on target cells via an IL-5 specific high-affinity receptor (Kd ≃ 150 pM) that has been proposed to be composed of at least two membrane polypeptide chains. The p60 component recognized by anti-murine IL-5 receptor mAbs H7 and T21 binds IL-5 with low affinity (Kd ≃ 10 nM). The other component is p130, detectable by following cross-linking experiments with IL-5. Using H7, T21, and R52.120 mAbs specific to murine IL-5 receptor, we characterized the molecular nature of the p130 of the high affinity receptor for murine IL-5. R52.120 mAb did not recognize the IL-5 binding recombinant p60 expressed on COS7 cells, but reacted with p130/140 on IL-5-dependent cell lines. R52.120 mAb showed partial inhibition of the IL-5-induced proliferation of the IL-5-dependent early B cell line Y16 at high IL-5 concentrations. Addition of R52.120 mAb together with H7 or T21 mAb caused more striking inhibition of the IL-5-dependent proliferation than that caused by either of them alone. R52.120 mAb down-regulated the number and dissociation constant of IL-5 binding sites with high affinity without affecting the levels of these with low-affinity. It also preferentially inhibited the formation of the cross-linked complex of p130 with radlolabeledIL-5. These results Indicate that p130/p140, recognized by R52.120 mAb, Is indispensable, together with p60, for the formation of high affinity IL-5 receptor. We propose to designate p60 and p130/p140 as the α and β chain of IL-5 receptor, respectively