( 報告様式 4) 16cm h0001 平成 29 年 5 月 30 日 平成 28 年度委託研究開発成果報告書 I. 基本情報 事業名 : ( 日本語 ) 次世代がん医療創生研究事業 ( 英語 ) Project for Cancer Research and Therapeutic
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1 ( 報告様式 4) 16cm h0001 平成 29 年 5 月 30 日 平成 28 年度委託研究開発成果報告書 I. 基本情報 事業名 : ( 日本語 ) 次世代がん医療創生研究事業 ( 英語 ) Project for Cancer Research and Therapeutic Evolution 研究 研究開発担当者 ( 日本語 ) 国立大学法人神戸大学大学院医学研究科特命教授高井義美所属役職氏名 : ( 英語 )Kobe University Graduate School of Medicine Project Professor Yoshimi Takai 実施期間 : 平成 28 年 5 月 25 日 ~ 平成 29 年 3 月 31 日 研究開発代表者 ( 日本語 ) 国立大学法人神戸大学大学院医学研究科特命教授高井義美所属役職氏名 : ( 英語 )Kobe University Graduate School of Medicine Project Professor Yoshimi Takai 1
2 研究開発分担者 ( 日本語 ) 国立大学法人神戸大学大学院医学研究科特命講師水谷清人所属役職氏名 : ( 英語 )Kobe University Graduate School of Medicine Project Associate Professor Kiyohito Mizutani 研究開発分担者 ( 日本語 ) 国立大学法人神戸大学大学院医学研究科医学研究員圓岡真宏所属役職氏名 : ( 英語 )Kobe University Graduate School of Medicine Visiting Medical Scientist Masahiro Maruoka 研究開発分担者 ( 日本語 ) 国立大学法人神戸大学大学院医学研究科特命助教慶田城迅所属役職氏名 : ( 英語 )Kobe University Graduate School of Medicine Visiting Assistant Professor Shin Kedashiro 2
3 II. 成果の概要 ( 総括研究報告 ) ( 和文 ) 細胞表面受容体 ( レセプター ) は ホルモン 神経伝達物質 サイトカインなどの特異的なリガンドと相互作用することで活性化される さらに 多くの受容体の活性は リガンドによる活性化以外にも それぞれに特異的な膜貫通タンパク質によって制御され このような分子はコレセプターやアクセサリーレセプターと呼ばれている これらのコレセプターの中には 受容体と同一細胞膜上でシスに相互作用するものがある インテグリンは シスに相互作用する受容体の活性を調節するコレセプターの一つである さらに いくつかの細胞接着分子がコレセプターとして機能し 細胞接着分子と受容体のシスの相互作用は それらの適切な局在化と活性化 およびシグナル伝達に重要である ネクチンやネクチン様分子 (Necls) は 細胞表面受容体やインテグリンとシスに相互作用し それらの活性化とシグナル伝達を制御することが知られている ネクチンは4つのメンバー ( ネクチン-1 ネクチン-2 ネクチン-3 ネクチン-4) から Necls は5つのメンバー (Necl-1 Necl-2 Necl-3 Necl-4 Necl-5) から成るファミリーを形成している それらのうち ネクチン- 1は FGF 受容体やインテグリンαvβ3 と ネクチン-3は PDGF 受容体とインテグリンαvβ3 と ネクチン-4はプロラクチン受容体と そして Necl-5 は PDGF 受容体 VEGF 受容体 インテグリンαvβ3 とそれぞれシスに相互作用する これらのネクチンや Necl-5 は ある種のがんではその発現が亢進していることが知られており これらの受容体やインテグリンに対して促進的な効果を示す 対照的に Necl-2 と Necl-4 は受容体やインテグリンに対して抑制的な効果を示し ある種のがんではその発現が低下していることが知られている 例えば Necl-2 は ErbB3 ErbB4 インテグリンα6β4 と Necl-4 は ErbB3 とインテグリンα6β4 とそれぞれシスに相互作用する このようにネクチンや Necl はコレセプターとして受容体やインテグリンとシスに相互作用することで 細胞接着だけでなく 細胞極性 形態形成 運動 増殖 分化 生存など種々の細胞機能において重要な役割を果たしている これらの知見は ネクチンファミリータンパク質と成長因子受容体 / インテグリンとの間の相互作用を制御することによる 新規抗がん剤の開発のための新しい戦略となりうる 研究開発代表者らは以前に ネクチン-4がその細胞外領域を介してプロラクチン受容体とシスに相互作用し プロラクチン刺激依存的なプロラクチン受容体の活性化とシグナル伝達を制御することを示していた しかし この相互作用による活性化制御機構は不明であった 本年度は ネクチン-4の細胞外領域とプロラクチン受容体とのシス相互作用は このような活性化を誘導するには不十分であり ネクチン-4の細胞内領域も必要であることを見出した ネクチン-4の細胞内領域は SOCS1 と直接的に相互作用し SOCS1 と JAK2 の相互作用を阻害することで 最終的に STAT5a のリン酸化を亢進させた また ネクチン-4の3 番目の Ig 様ドメインおよびプロラクチン受容体の2 番目のフィブロネクチン III 型ドメインが直接結合したが この結合にはネクチン-4 とプロラクチン受容体の膜貫通領域も必要であった これらの結果は JAK2-STAT5a シグナル伝達経路における SOCS1 のフィードバック阻害を制御することによって ネクチン-4がプロラクチン受容体に対するコレセプターとして機能することを示している 3
4 ( 英文 ) Cell surface receptors are activated by interacting with their specific ligands, including hormones, neurotransmitters, and cytokines. In addition to the ligands, activity of many receptors is regulated by their specific transmembrane proteins, which are called co-receptors or accessory receptors. Of these co-receptors, some of them cis-interact with the receptors on the same cell membrane. Integrins are one of the co-receptors modulating the activity of cis-interacting receptors. Moreover, several cell adhesion molecules (CAMs) play multiple roles as cis-interacting co-receptors, and the cis-interactions of CAMs with cell surface receptors are generally important for their proper localization, activation, and signaling. It has previously been shown that nectins and nectin-like molecules (Necls) cis-interact with cell surface membrane receptors and integrins and regulate their activation and signaling. Nectins comprise a family with four members (nectin-1, nectin-2, nectin-3, and nectin-4), whereas Necls comprise a family with five members (Necl-1, Necl-2, Necl-3, Necl-4, and Necl-5). Among them, nectin-1 cis-interacts with the FGF receptor and integrin αvβ3; nectin-3 cis-interacts with the PDGF receptor and integrin αvβ3; nectin-4 interacts with the prolactin receptor; and Necl-5 cis-interacts with the PDGF receptor, the VEGF receptor, and integrin αvβ3. These nectins and Necl-5, which are known to be up-regulated in several types of cancers, show a stimulatory effect on these receptors and the integrin. In contrast, Necl-2 and Necl-4, which are known to be down-regulated in several types of cancers, show an inhibitory effect on some receptors and integrins. For instance, Necl-2 cis-interacts with ErbB3, ErbB4, and integrin α6β4, and Necl-4 cis-interacts with ErbB3 and integrin α6β4. By cis-interacting with these membrane receptors and integrins, nectins and Necls play important roles not only in cell adhesion, but also in many other cell functions, such as cell polarization, morphogenesis, movement, proliferation, differentiation, and survival. These findings have provided us with a new strategy for the development of novel therapeutic agents to treat cancer by controlling the interactions between the nectin. We previously showed that nectin-4 cis-interacts with the prolactin receptor through the extracellular region and stimulates the prolactin-induced prolactin receptor activation and signaling. However, it remained unknown how this interaction regulates these stimulatory effects. In this physical year, we found that the cis-interaction of the extracellular region of nectin-4 with the prolactin receptor was not sufficient for eliciting these effects and that the cytoplasmic region of nectin-4 was also required for this interaction. The cytoplasmic region of nectin-4 directly interacted with suppressor of cytokine signaling 1 (SOCS1) and inhibited the interaction of SOCS1 with JAK2, eventually resulting in the increased phosphorylation of STAT5a. The third Ig-like domain of nectin-4 and the second fibronectin type III domain of the prolactin receptor were involved in this cis-interaction, and both the extracellular and transmembrane regions of nectin-4 and the prolactin receptor were required for this direct interaction. These results indicate that nectin-4 serves as a stimulatory co-receptor for the prolactin receptor by regulating the feedback inhibition of SOCS1 in the JAK2-STAT5a signaling pathway. 4
5 III. 成果の外部への発表 (1) 学会誌 雑誌等における論文一覧 ( 国内誌 0 件 国際誌 1 件 ) 1. Maruoka, M., Kedashiro, S., Ueda, Y., Mizutani, K., and Takai, Y. Nectin-4 co-stimulates the prolactin receptor by interacting with SOCS1 and inhibiting its activity on the JAK2-STAT5a signaling pathway. J. Biol. Chem. 2017, 292, (2) 学会 シンポジウム等における口頭 ポスター発表 該当なし (3) 国民との科学 技術対話社会 に対する取り組み 該当なし (4) 特許出願 日本 : 特願 号 5
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