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International Immunology, Vol. 2, No. 2, pp. 143-150,February 1990
© 1990 Japanese Society for Immunology

Identification of a cell surface 105 kd protein (Aic-2 antigen) which binds interleukin-3

Shin Yonehara, Ai Ishii, Minako Yonehara, Shigeo Koyasu, Atsushi Miyajima1, Jolanda Schreurs1, Ken-ichi Arai1 and Iciro Yahara

Department of Cell Biology, Tokyo Metropolitan Institute of Medical Science 3-18-22 Honkomagome, Bunkyo-ku, Tokyo 113, Japan
1 DNAX Research Institute of Molecular and Cellular Biology 901 California Avenue, Palo Alto, CA 94304-1104, USA

Correspondence to: Correspondence to: Shin Yonehara, as above

A mouse Interleukin-3 (IL-3)-binding molecule that is an essential constituent of the mouse IL-3 receptor complex was identified as a cell surface protein of M, 105 kd. A rat monoclonal antibody, anti-Aic-2 lgM, recognized and immunoprecipitated a cell surface 105 kd protein (Aic-2 antigen). The antigen (Aic-2) and IL-3 receptor were co-down-regulated upon incubation of IL-3-dependent mouse IC2 cells with either anti-Aic-2 lgM or IL-3 at 37°C, whereas anti-Aic-2 did not inhibit the binding of IL-3 to IC2 cells at 15°C. The Aic-2 antigen and IL-3 receptor were co-distributed on various cell lines and cell types. IL-3 was shown to bind specificaily to the Aic-2 antigen (Mr 105 kd) in the immunoprecipitated complex with anti-Aic-2. Chemically cross-linking of IL-3 to surface molecules of IC2 cells produced three types of complexes with Mr 95, 140, and 200–340 kd in SDS-PAGE, and pre-incubation with anti-Aic-2 lgM at 37°C reduced the intensity of the three bands to the same degree. Moreover, anti-Aic-2 immunoprecipitated these three IL-3-cross-linked complexes, whereas the same monoclonal antibody recognized a single 105 kd molecule. Anti-Aic-2 lgM enhanced IL-3-dependent growth of IC2 cells though it did not promote proliferation of IC2 cells.

Keywords: IL-3, monoclonal antibody, receptor, signal transduction

Received 1 September 1989, accepted 28 October 1989.


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