{"created":"2023-07-27T06:59:59.364731+00:00","id":59758,"links":{},"metadata":{"_buckets":{"deposit":"bb6dcd76-7316-495a-8e19-7dd773284fb3"},"_deposit":{"created_by":18,"id":"59758","owners":[18],"pid":{"revision_id":0,"type":"depid","value":"59758"},"status":"published"},"_oai":{"id":"oai:kanazawa-u.repo.nii.ac.jp:00059758","sets":["2812:2813:2835"]},"author_link":["32079","77197"],"item_9_biblio_info_8":{"attribute_name":"書誌情報","attribute_value_mlt":[{"bibliographicIssueDates":{"bibliographicIssueDate":"1999-12-07","bibliographicIssueDateType":"Issued"},"bibliographicPageStart":"3p.","bibliographicVolumeNumber":"1997 – 1998","bibliographic_titles":[{"bibliographic_title":"平成10(1998)年度 科学研究費補助金 基盤研究(C) 研究成果報告書概要"},{"bibliographic_title":"1998 Fiscal Year Final Research Report Summary","bibliographic_titleLang":"en"}]}]},"item_9_creator_33":{"attribute_name":"著者別表示","attribute_type":"creator","attribute_value_mlt":[{"creatorNames":[{}],"nameIdentifiers":[{},{}]}]},"item_9_description_21":{"attribute_name":"抄録","attribute_value_mlt":[{"subitem_description":"免疫抑制療法を受けた多数の再生不良性貧血症例について,末梢血リンパ球におけるheat shock protein(hsp72)の発現をフローサイトメトリーで検討した.その結果,シクロスポリン療法に反応して改善した再生不良性貧血患者のリンパ球では,熱ショック後のhsp72の発現が亢進していることが明らかになった.この現象は,再生不良性貧血以外の血液疾患患者ではみられなかった.hsp72の発現はTリンパ球においてとくに顕著であった.したがって,治療前に末梢血リンパ球のhsp72の誘導性を調べることは,シクロスポリンのような免疫抑制剤に対する反応性を予測する上で有用と考えられた.一方,全国の症例について調査を行ったところ,再生不良性貧血全体の約40%の症例で,末梢血単核細胞中のhsp72陽性細胞の割合が高値(>30%)を示した.しかし,抗胸腺細胞グロブリン+シクロスポリン療法の効果との関係をみたところ,シクロスポリン療法でみられたような明らかな相関は認められなかった.一部の再生不良性貧血患者では,リンパ球だけでなく,赤血球の表面にもhsp72が検出された.そこで,赤血球表面のhsp72について詳細に検討したところ,hsp72は,再生不良性貧血患者だけでなく,約30%の健常人で20〜90%の赤血球表面に発現していた.血液型との関係を調べたところ,hsp72はA型とAB型の赤血球にのみ検出された.hsp72の発現は熱ストレスとは無関係であった.hsp72陽性の健常人の骨髄をin vitroで培養し,赤血球前駆細胞を分化させたところ,得られた赤芽球の表面にはhsp72は検出されなかった.このためhsp72は,A型およびAB型の赤芽球が脱核したのちに赤血球表面に発現すると思われた.赤血球表面にはhsp72だけでなく,hsp90の発現も認められた.A型物質との関係を調べるため,O型赤血球をNアセチルガラクトサミン(GalNAc)トランスフェラーゼとUDP-GalNAcで処理することによりA血球に変換したところ,抗hsp72抗体との反応はみられなかった.したがって,赤血球表面のhsp72の発現は,遺伝的に決定されたものであり,A型物質の発現と密接な関係にあることが示唆された.","subitem_description_type":"Abstract"},{"subitem_description":"To characterize immune pathophysiology of aplastic anemia (AA), we studied expression of heat shock piotein (-hsp) 72 in peripheral blood mononuclear cells (PBMCs) of untreated AA patients using flow cytometry. AA patients whose PBMCs exhibited high percentages (>30%) of hsp72+ cells after heat treatment were likely to respond to cyclosporine therapy. The high inducibility of hsp72 in PBMCs was not detected in other hematologic diseases, such as myelodysplastic syndrome and hemolytic anemia. Among PBMCs of AA patients responsive to cyclosporine, hsp72 expression was primarily detected in T cells. Thus, detection of hsp72^+ cell in PBMCs before treatments appeared to be useful for predicting a favorable response to cyclosporine therapy. Next, we collected PBMCs of AA patients who later received combined immunosuppressive therapy consisting of antithymocyte globulin and cyclosporine from the other hospitals in Japan, and determined the inducibility of hsp72. Although approximately 40% of patients showed high percentages of hsp72^+ cell among PBMCs, there was no correlation between a good response to the combined immunosuppressive therapy and a high inducibility of hsp72 in PBMCs.\nIn some AA patients, hsp72 was detectable not only in the cytoplasm of PBMCs but also on the surface of red blood cells (RB Cs). Detailed analysis of hsp72 on RBCs revealed that in additi9n to AA patients, hsp72^+ cells could be detected on 20-90% of RBCs of about 30% of normal individuals and that its expression was restricted to individuals bearing blood type A and AB.Heat treatments did not influence the expression of hsp72 on RB Cs. Since hsp72 could not be detected on normocytic erythroblasts that were generated from erythroid progenitor cells of a normal individual with blood type A, hsp72 appeared to emerge on RBCs after terminal differentiation of erythroid progenitor cells. Beside hsp72, RBCs of individuals with blood type A and AB expressed hsp90. Binding of anti-hsp72 monoclonal antibodies was not seen in type O RBCs that were forced to express A antigens by the treatment with N-acetyl galactosaminyltransferase and UDP-N-acefyl galactosamine. Thus, the expression of hsp72 seemed to be genetically determined although it is closely associated with A antigen expression. The function and biological significance of hsp72 on RBCs remain to be determined.","subitem_description_type":"Abstract"}]},"item_9_description_22":{"attribute_name":"内容記述","attribute_value_mlt":[{"subitem_description":"研究課題/領域番号:09671103, 研究期間(年度):1997 – 1998","subitem_description_type":"Other"},{"subitem_description":"出典：研究課題「再生不良性貧血の病因としての heat shock protein 70 の解析 」課題番号09671103\n（KAKEN：科学研究費助成事業データベース（国立情報学研究所）） \n（https://kaken.nii.ac.jp/ja/report/KAKENHI-PROJECT-09671103/096711031998kenkyu_seika_hokoku_gaiyo/）を加工して作成","subitem_description_type":"Other"}]},"item_9_description_5":{"attribute_name":"提供者所属","attribute_value_mlt":[{"subitem_description":"金沢大学医学部附属病院","subitem_description_type":"Other"}]},"item_9_identifier_registration":{"attribute_name":"ID登録","attribute_value_mlt":[{"subitem_identifier_reg_text":"10.24517/00066013","subitem_identifier_reg_type":"JaLC"}]},"item_9_relation_28":{"attribute_name":"関連URI","attribute_value_mlt":[{"subitem_relation_name":[{"subitem_relation_name_text":"https://kaken.nii.ac.jp/search/?qm=70217660"}],"subitem_relation_type_id":{"subitem_relation_type_id_text":"https://kaken.nii.ac.jp/search/?qm=70217660","subitem_relation_type_select":"URI"}},{"subitem_relation_name":[{"subitem_relation_name_text":"https://kaken.nii.ac.jp/grant/KAKENHI-PROJECT-09671103/"}],"subitem_relation_type_id":{"subitem_relation_type_id_text":"https://kaken.nii.ac.jp/grant/KAKENHI-PROJECT-09671103/","subitem_relation_type_select":"URI"}},{"subitem_relation_name":[{"subitem_relation_name_text":"https://kaken.nii.ac.jp/ja/report/KAKENHI-PROJECT-09671103/096711031998kenkyu_seika_hokoku_gaiyo/"}],"subitem_relation_type_id":{"subitem_relation_type_id_text":"https://kaken.nii.ac.jp/ja/report/KAKENHI-PROJECT-09671103/096711031998kenkyu_seika_hokoku_gaiyo/","subitem_relation_type_select":"URI"}}]},"item_9_version_type_25":{"attribute_name":"著者版フラグ","attribute_value_mlt":[{"subitem_version_resource":"http://purl.org/coar/version/c_ab4af688f83e57aa","subitem_version_type":"AM"}]},"item_creator":{"attribute_name":"著者","attribute_type":"creator","attribute_value_mlt":[{"creatorNames":[{"creatorName":"中尾, 真二"}],"nameIdentifiers":[{"nameIdentifier":"32079","nameIdentifierScheme":"WEKO"},{"nameIdentifier":"70217660","nameIdentifierScheme":"e-Rad","nameIdentifierURI":"https://kaken.nii.ac.jp/ja/search/?qm=70217660"}]}]},"item_files":{"attribute_name":"ファイル情報","attribute_type":"file","attribute_value_mlt":[{"accessrole":"open_date","date":[{"dateType":"Available","dateValue":"2022-05-27"}],"displaytype":"detail","filename":"HO-PR-NAKAO-S-kaken 1999-3p.pdf","filesize":[{"value":"150.7 kB"}],"format":"application/pdf","licensetype":"license_11","mimetype":"application/pdf","url":{"label":"HO-PR-NAKAO-S-kaken 1999-3p.pdf","url":"https://kanazawa-u.repo.nii.ac.jp/record/59758/files/HO-PR-NAKAO-S-kaken 1999-3p.pdf"},"version_id":"45102577-39ed-40a7-b57d-abe93580824b"}]},"item_language":{"attribute_name":"言語","attribute_value_mlt":[{"subitem_language":"jpn"}]},"item_resource_type":{"attribute_name":"資源タイプ","attribute_value_mlt":[{"resourcetype":"research report","resourceuri":"http://purl.org/coar/resource_type/c_18ws"}]},"item_title":"再生不良性貧血の病因としての heat shock protein 70 の解析","item_titles":{"attribute_name":"タイトル","attribute_value_mlt":[{"subitem_title":"再生不良性貧血の病因としての heat shock protein 70 の解析"},{"subitem_title":"Analysis of heat shock protein 70 as a causal molecule of aplastic anemia","subitem_title_language":"en"}]},"item_type_id":"9","owner":"18","path":["2835"],"pubdate":{"attribute_name":"公開日","attribute_value":"2022-05-27"},"publish_date":"2022-05-27","publish_status":"0","recid":"59758","relation_version_is_last":true,"title":["再生不良性貧血の病因としての heat shock protein 70 の解析"],"weko_creator_id":"18","weko_shared_id":-1},"updated":"2024-07-01T06:34:32.382116+00:00"}