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Shigetomi, Hiroshi*; Oka, Kiyoshi; Oi, Hidekazu*; Furukawa, Naoto*; Yoshida, Shozo*; Kawaguchi, Ryuji*; Nagai, Akira*; Haruta, Shoji*; Yanase, Yasuhito*; Akasaka, Julia*; et al.
Nihon Reza Igakkai-Shi, 33(2), p.131 - 135, 2012/08
no abstracts in English
Ito, Takachika*; Suzuki, Shoichi*; Kanaji, Sachiko*; Shiraishi, Hiroshi*; Ota, Shoichiro*; Arima, Kazuhiko*; Tanaka, Go*; Tamada, Taro; Honjo, Eijiro*; Garcia, K. C.*; et al.
Journal of Biological Chemistry, 284(36), p.24289 - 24296, 2009/09
Times Cited Count：24 Percentile：45.24(Biochemistry & Molecular Biology)Both IL-4 and IL-13 can bind to the shared receptor composed of the IL-4 receptor 
chain and the IL-13 receptor -1 chain (IL-13R1); however, the assembly mechanisms of these ligands to the receptor is different, enabling the principal functions of these ligands to be different. We have previously shown that the N-terminal Ig-like domain in IL-13R1, called the D1 domain, is the specific and critical binding unit for IL-13. However, it has still remained obscure which the amino acid has specific binding capacity to IL-13 and why the D1 domain acts as the binding site for IL-13, but not IL-4. To address these questions, in this study, we performed the mutational analyses for the D1 domain, combining the structural data to identify the amino acids critical for binding to IL-13. Mutations of Lys76, Lys77, or Ile78 in c' strand in which the crystal structure showed interact with IL-13 and those of Trp65 and Ala79 adjacent to the interacting site, resulted in significant impairment of IL-13 binding, demonstrating that these amino acids generate the binding site. Furthermore, mutations of Val35, Leu38, or Val42 at N-terminal 
-strand also resulted in loss of IL-13 binding, probably from decrease structural stability. None of the mutations employed here affected IL-4 binding. These results demonstrate that the hydrophobic patch composed of Lys76, Lys77, and Ile78 is the IL-13 recognition site and solidify our understanding that the differential requirements of the D1 domain in IL-13R1 allows the shared receptor to respond differentially to IL-4 and IL-13.
Matsukado, Koji*; Esirkepov, T. Z.; Kinoshita, Kenichi*; Daido, Hiroyuki; Utsumi, Takayuki*; Li, Z.*; Fukumi, Atsushi*; Hayashi, Yukio; Orimo, Satoshi; Nishiuchi, Mamiko; et al.
Physical Review Letters, 91(21), p.215001_1 - 215001_4, 2003/11
Times Cited Count：136 Percentile：95.24(Physics, Multidisciplinary)no abstracts in English
Hoshiya, Taiji; *; Ando, Hiroei
Nihon Kinzoku Gakkai-Shi, 56(7), p.741 - 746, 1992/00
no abstracts in English
Hoshiya, Taiji; *; Katsuta, Hiroji; Ando, Hiroei
Nihon Kinzoku Gakkai-Shi, 56(7), p.747 - 756, 1992/00
no abstracts in English
Hoshiya, Taiji; *; ; Takamura, Saburo;
Nihon Kinzoku Gakkai-Shi, 55(10), p.1054 - 1062, 1991/10
no abstracts in English
Hoshiya, Taiji; ; Kizaki, Minoru; *; Sudo, Kenji; ;
JAERI-M 89-205, 68 Pages, 1989/12
no abstracts in English
Hoshiya, Taiji; *;
Proc. of MRS Int. Meeting on Advanced Materials, Vol. 9, p.225 - 230, 1989/00
no abstracts in English
; *; ; ;
Proceedings of International Conference on Martensitic Transformations, p.685 - 690, 1986/00
no abstracts in English
Aoyama, Yoshio; Miyamoto, Yasuaki; Yamaguchi, Hiromi; Izumi, Mikio*; Naito, Susumu*; Yamamoto, Shuji*; Sano, Akira*; Nambu, Kenichi*; Takahashi, Hiroyuki*; Oda, Akinori*
no journal, ,
no abstracts in English
2 chain (IL-13R2)Matsumoto, Fumiko; Tamada, Taro; Honjo, Eijiro*; Ota, Shoichiro*; Izuhara, Kenji*; Kuroki, Ryota
no journal, ,
The allergic disease has dramatically increased in recent years. Interleukin-13 (IL-13) is a key cytokine critical to the development of T-cell-mediated humoral immune responses which are associated with allergy and asthma. IL-13 possesses two types of receptor: the heterodimer, composed of IL-13R1 and IL-4R, transducing the IL-13 signals; and the IL-13R2, acting as a nonsignaling "decoy" receptor. Although the extracellular region of IL-13R1 and IL-13R2 are composed of a common structure of the class 1 cytokine receptor superfamily and they have similar amino acid sequence, the affinity of IL-13R2 with IL-13 is more than ten-fold higher than that of IL-13R1. In order to investigate the reason for this higher ligand affinity to IL-13R2, extra cellular region of IL-13R2 was expressed by silkworm-baculovirus expression system after fusing the DNA cording the extracellular region of human IL-13R2 with the Fc derived from mouse IgG2a. The expressed fusion protein IL-13R2-Fc was purified by a protein G column, and the affinity to IL-13 was confirmed by gel filtration followed by light scattering analysis. After Fc region was removed by thrombin digestion, the resulting extra cellular region of IL-13R2 receptor was confirmed to retain strong affinity to IL-13 with 1:1 ratio.
2 chainMatsumoto, Fumiko; Hatanaka, Takaaki*; Tamada, Taro; Honjo, Eijiro*; Ota, Shoichiro*; Ito, Yuji*; Izuhara, Kenji*; Kuroki, Ryota
no journal, ,
Interleukin-13 (IL-13) is a key cytokine critical to the development of T-cell-mediated humoral immune responses which are associated with allergy and asthma. IL-13 possesses two types of receptor: the heterodimer, composed of IL-13R1 and IL-4R, transducing the IL-13 signals; and the IL-13R2, it has high affinity rather than IL-13R1 against IL-13, acting as a nonsignaling "decoy" receptor. In order to investigate the inhibition mechanism of IL-13 signal by IL-13R2, extra cellular region of IL-13R2 was expressed by silkworm-baculovirus expression system after fusing the DNA cording the extracellular region of human IL-13R2 with the Fc derived from mouse IgG2a. The expressed fusion protein (IL-13R2)2-Fc was purified by a protein A column followed by an ion exchange column. The affinities of the ligand complexes, IL-13/IL-13R1 and IL-13/IL-13R2 to (IL-4R)2-Fc were investigated to explore the inactivation mechanism of the IL-13R1 signal with IL-13R2 by surface plasmon resonance analysis. IL-13/IL-13R1 complex has an affinity (KD=1.20
10
M) with (IL-4Ra)2-Fc, whereas the IL-13/IL-13R2 complex had no affinity with (IL-4R)2-Fc. This observation suggests that IL-13R2 does not inactivate the IL-13R1 through formation of a ternary complex with IL-13 and IL-4R, but removes the IL-13 with its higher affinity to IL-13 without forming a ternary complex.
