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イタノ ナオキ
ITANO NAOKI
板野 直樹 所属 京都産業大学 生命科学部 先端生命科学科 職種 教授 |
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| 言語種別 | 英語 |
| 発行・発表の年月 | 2009 |
| 形態種別 | 研究論文 |
| 査読 | 査読あり |
| 標題 | A Splice Variant of ASC Regulates IL-1 beta Release and Aggregates Differently from Intact ASC |
| 執筆形態 | その他 |
| 掲載誌名 | MEDIATORS OF INFLAMMATION |
| 出版社・発行元 | HINDAWI PUBLISHING CORPORATION |
| 巻・号・頁 | 2009,pp.287387 |
| 著者・共著者 | Kazuhiko Matsushita,Michiko Takeoka,Junji Sagara,Naoki Itano,Yuka Kurose,Akihiro Nakamura,Shun'ichiro Taniguchi |
| 概要 | The apoptosis-associated speck-like protein containing a caspase recruit domain (ASC) is involved in apoptosis and innate immunity and is a major adaptor molecule responsible for procaspase-1 activation. ASC mRNA is encoded by three exons: exons 1 and 3 encode a pyrin domain (PYD) and caspase recruit domain (CARD), respectively, and exon 2 encodes a proline and glycine-rich (PGR) domain. Here, we identified a variant ASC protein (vASC) lacking the PGR domain that was smaller than full length ASC (fASC) derived from fully transcribed mRNA and searched for differences in biochemical and biological nature. Both fASC and vASC were found to activate procaspase-1 to a similar degree, but the efficiency of IL-1 beta excretion was significantly higher for vASC. There was also a marked structural difference observed in the fibrous aggregates formed by fASC and vASC. These results suggest that although the PGR domain is dispensable for procaspase-1 activation, it plays an important role in the regulation of the molecular structure and activity of ASC. Copyright (C) 2009 Kazuhiko Matsushita et al. |
| DOI | 10.1155/2009/287387 |
| ISSN | 0962-9351 |