{"_buckets": {"deposit": "4fee4277-5199-4b4f-8f56-614ccec64d59"}, "_deposit": {"created_by": 1, "id": "1087", "owners": [1], "pid": {"revision_id": 0, "type": "depid", "value": "1087"}, "status": "published"}, "_oai": {"id": "oai:ir.soken.ac.jp:00001087", "sets": ["22"]}, "author_link": ["9281", "9280", "9279"], "item_1_biblio_info_21": {"attribute_name": "書誌情報（ソート用）", "attribute_value_mlt": [{"bibliographicIssueDates": {"bibliographicIssueDate": "1997-03-24", "bibliographicIssueDateType": "Issued"}, "bibliographic_titles": [{}]}]}, "item_1_creator_2": {"attribute_name": "著者名", "attribute_type": "creator", "attribute_value_mlt": [{"creatorNames": [{"creatorName": "石原, 悟"}], "nameIdentifiers": [{"nameIdentifier": "9279", "nameIdentifierScheme": "WEKO"}]}]}, "item_1_creator_3": {"attribute_name": "フリガナ", "attribute_type": "creator", "attribute_value_mlt": [{"creatorNames": [{"creatorName": "イシハラ, サトル"}], "nameIdentifiers": [{"nameIdentifier": "9280", "nameIdentifierScheme": "WEKO"}]}]}, "item_1_date_granted_11": {"attribute_name": "学位授与年月日", "attribute_value_mlt": [{"subitem_dategranted": "1997-03-24"}]}, "item_1_degree_grantor_5": {"attribute_name": "学位授与機関", "attribute_value_mlt": [{"subitem_degreegrantor": [{"subitem_degreegrantor_name": "総合研究大学院大学"}]}]}, "item_1_degree_name_6": {"attribute_name": "学位名", "attribute_value_mlt": [{"subitem_degreename": "博士（学術）"}]}, "item_1_description_1": {"attribute_name": "ID", "attribute_value_mlt": [{"subitem_description": "1997044", "subitem_description_type": "Other"}]}, "item_1_description_12": {"attribute_name": "要旨", "attribute_value_mlt": [{"subitem_description": "　　　β catenin is involved not only in the cadherin-based cell adhesion system but also in the Wnt signaling pathway. In this pathway, it is supposed that β catenin is phosphorylated by glycogen synthase kinase-3β(GSK-3β) to become susceptible to degradation, that the Wnt signaling suppresses GSK-3β to increase the amount of non-phosphorylated, stable β catenin, and that the stable β catenin affects the transcription of various genes in the nucleus. To separate the role of β catenin in intracellular signaling from its role in the cadherin-based cell adhesion, they constructed a mutant β catenin(mbH) with amino acid substitutions at its putative GSK-3β phosphorylation site (GSKP sequence), and introduced it into L fibroblasts that lack the cadherin expression. In stable transfectants (LmbH), not only mbH but also endogenous wild type β catenin was stabilized. Green fluorescence protein (GFP) carrying the mutated GSKP sequence also stabilized the endogenous β catenin in L cells, indicating that the mutated GSKP sequence suppresses the degradation machinery for β catenin. Furthermore, by adding the nuclear localization signal to mbH, they obtained L transfectants (LmbHN) expressing the stabilized β catenin predominantly in the nucleus. Under the long-term aggregation conditions, LmbHN formed compact cell aggregates consisting mainly of 2-5 cells. LmbH also showed a similar aggregation activity but to a lesser extent, and parent L cells mostly remained to be dissociated. Close analyses by immunofluorescence microscopy and the cell adhesion inhibition assay with RGD peptides revealed that aggregation activity is attributed to the integrin-based cell adhesion. Considering that the amount of stabilized β catenin in the nucleus is significantly larger in LmbHN than in LmbH, they speculate that the accumulation of β catenin in the nucleus resulted in the activation of integrin-based cell adhesion. The transfectants established in this study, thus, will provide an advantageous system to selectively analyze the role of β catenin in the nucleus and in the regulation of integrin activity. 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