MODULATION OF DEXAMETHASONE-INDUCED THYMOCYTE APOPTOSIS BY HEAT-SHOCK PROTEIN 90-BINDING AGENTS

• OHTA KAZUMASA

  Department of Biochemistry, Tokyo Dental College

• OKOSHI RINTAROU

  Department of Biochemistry, Tokyo Dental College

• WAKABAYASHI MAIKO

  Department of Biochemistry, Tokyo Dental College

• SATO YUTAKA

  Department of Biochemistry, Tokyo Dental College

• KIZAKI HARUTOSHI

  Department of Biochemistry, Tokyo Dental College

抄録

Heat-shock protein 90 (HSP90) is known to affect a variety of cellular activities. The present study showed that the HSP90-binding agents, geldanamycin, herbimycin A and radicicol, inhibited the murine thymocyte apoptosis induced by dexamethasone and was accompanied by the inhibition of the reduction of the mitochondrial transmembrane potential (ΔΨm). HSP90-binding agents did not inhibit etoposide-induced apoptosis. The inhibition of dexamethasone-induced apoptosis was in part due to the interference of HSP90 with the glucocorticoid receptor, resulting in the inhibition of nuclear translocation of the receptor. The expression of inositol 1, 4, 5-triphosphate receptors, which were shown to be involved in dexamethasone-induced apoptosis, did not participate in the inhibition of apoptosis.

収録刊行物

• The Bulletin of Tokyo Dental College

  The Bulletin of Tokyo Dental College 45 (1), 1-8, 2004

  東京歯科大学

キーワード

• Thymocytes
• Apoptosis
• Glucocorticoid
• HSP90
• Geldanamycin

詳細情報

• CRID: 1390282679563869952
• NII論文ID: 110004690131
• NII書誌ID: AA00592969
• DOI: 10.2209/tdcpublication.45.1
• COI: 1:CAS:528:DC%2BD2cXosVWhu7Y%3D
• ISSN: 00408891
• PubMed: 15346879
• Web Site: https://search.jamas.or.jp/link/ui/2006000206
• 本文言語コード: en
• データソース種別:
  • JaLC
  • Crossref
  • PubMed
  • CiNii Articles
• 抄録ライセンスフラグ: 使用不可