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Nature 324, 73 - 76 (06 November 1986); doi:10.1038/324073a0

Complementary DNA for a novel human interleukin (BSF-2) that induces B lymphocytes to produce immunoglobulin

Toshio Hirano, Kiyoshi Yasukawa, Hisashi Harada*, Tetsuya Taga, Yasuo Watanabe, Tadashi Matsuda, Shin-ichiro Kashiwamura, Koichi Nakajima, Koichi Koyama, Akihiro Iwamatsu, Susumu Tsunasawa, Fumio Sakiyama, Hiroshi Matsui, Yoshiyuki Takahara, Tadatsugu Taniguchi* & Tadamitsu Kishimoto

Division of Immunology, Osaka University, 1–3, Yamada-Oka, Suita, Osaka 565, Japan
*Division of Molecular Biology, Institute for Molecular and Cellular Biology, Osaka University, 1–3, Yamada-Oka, Suita, Osaka 565, Japan
Division of Protein Chemistry, Institute for Protein Research, Osaka University, 1–3, Yamada-Oka, Suita, Osaka 565, Japan
Central Research Laboratories, Ajinomoto Co. Inc., Totsuka-ku, Yokohama 244, Japan

When stimulated with antigen, B cells are influenced by T cells to proliferate and differentiate into antibody-forming cells. Since it was reported1,2 that soluble factors could replace certain functions of helper T cells in the antibody response, several different kinds of lymphokines and monokines have been reported in B-cell growth and differentiation3,4. Among these, human B-cell differentiation factor (BCDF or BSF-2) has been shown to induce the final maturation of B cells into immunoglobulin-secreting cells5–8. BSF-2 was purified to homogeneity9 and its partial NH2-terminal amino-acid sequence was determined10. These studies indicated that BSF-2 is functionally and structurally unlike other known proteins. Here, we report the molecular cloning, structural analysis and functional expression of the cDNA encoding human BSF-2. The primary sequence of BSF-2 deduced from the cDNA reveals that BSF-2 is a novel interleukin consisting of 184 amino acids.

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