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- Material Type
- 文書・図像類
- Author/Editor
- 上田, 雅博岸田, 昭世飯島, 幹雄岸田, 想子
- Publication, Distribution, etc.
- Alternative Title
- Identification and characterization of desacyl-ghrelin
- Text Language Code
- jpn
- Subject Heading
- Target Audience
- 一般
- Note (General)
- 2011-2012年度科学研究費助成事業(科学研究費補助金(挑戦的萌芽研究)研究成果報告書 課題番号：23659124 研究代表者：上田雅博(鹿児島大学自然科学教育研究支援センター技術職員)非修飾型グレリンを固定化したカラムを作成し、アフィニティ精製の手法によりブタ脳抽出液からグレリン結合たんぱく質を濃縮し、高塩濃度での溶出を行った後、SDSポリアクリルアミド電気泳動と質量分析を行って、グレリンに結合する蛋白質の同定を試みたが、有意なバンドを検出するには至らなかった。次に、マウス脳cDNAライブラリーを培養細胞に発現させ、標識グレリンを作用させ、グレリンを検出することにより、グレリンと結合するクローンのスクリーニングを行い、いくつかの陽性クローンを含む細胞集団があることを検出できたので、現在受容体のクローニングをさらに進めようとしている。Ghrelin is a peptide hormone to regulate appetite and is known to have two forms (acyl ghrelin and des-acyl ghrelin). Ghrelin receptor (GHSR), which recognizes the post-translational acyl-modification, expressed in various tissues. However, ghrelin without lipid-modification does not bind to GHSR and functions antagonistic to acyl ghrelin. These findings suggested the presence of unknown receptor specific for des-acyl ghrelin. We performed affinity-purification of des-acyl ghrelin-binding protein using pig brain extract. We tried to elute des-acyl ghrelin-associated protein by high salt condition (1M NaCl) but detected no significant condensation of candidate molecules. Next, we performed conventional receptor panning assay using COS7 cells transfected with sub-pooled mouse brain cDNA libraries. We detected several pools as “positive pools” and further selection of procedures for cloning is in process.