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A new approach for cellular injury

Research Project

Project/Area Number 11557113
Research Category

Grant-in-Aid for Scientific Research (B).

Allocation TypeSingle-year Grants
Section展開研究
Research Field Anesthesiology/Resuscitation studies
Research InstitutionChiba University

Principal Investigator

AOE Tomohiko  Chiba University, Graduate School of Medicine, Associate Professor, 大学院・医学研究科, 助教授 (90311612)

Co-Investigator(Kenkyū-buntansha) KOSEKI Haruhiko  Chiba University, Graduate School of Medicine, Professor, 大学院・医学研究科, 教授 (40225446)
Project Period (FY) 1999 – 2000
Project Status Completed (Fiscal Year 2000)
Budget Amount *help
¥13,500,000 (Direct Cost: ¥13,500,000)
Fiscal Year 2000: ¥6,700,000 (Direct Cost: ¥6,700,000)
Fiscal Year 1999: ¥6,800,000 (Direct Cost: ¥6,800,000)
Keywordsstress protein / molecular chaperone / HSP27 / VP22 / heat shock protein / 酸化ストレス / 細胞保護 / 分泌
Research Abstract

Extracellular signalling is usually transduced to cells through binding of signalling molecules to the receptors on the cell surface or internalization of them by endocytosis machinery. Recently some proteins have been found to penetrate directly from extracellular space to cytoplasm and nucleus, and function there. VP22, a herpes simplex virus I protein, is such a protein that can penetrate to cytoplasm and nucleus. Interestingly, a chimeric protein with VP22 was also demonstrated to preserve such an ability. In this study, we made chimeric proteins with VP22 and HSP27, a chaperone that has a cytoprotective ability against cellular stresses, to explore a new drug delivery system. One chimeric VP22-HSP27 was an unstable protein that is degraded immediately after synthesis, the other VP22-HSP27 was more stable and we have detected its expression by immunofluorescence and western blot. The cells expressing this protein , unexpectedly, revealed sensitive to cellular stresses, which suggested the chimeric VP22-HSP27 had a dominant-negative character against endogenous HSP27. Further efforts making chimeric proteins with VP22 and HSP27, or other useful proteins will be explored.

Report

(3 results)
  • 2000 Annual Research Report   Final Research Report Summary
  • 1999 Annual Research Report
  • Research Products

    (4 results)

All Other

All Publications (4 results)

  • [Publications] Aoe.T.,: "The KDEL receptor regulates a GTPase-activating protein for ARF1 by interacting with its non-catalytic domain."J Biol Chem.. 274. 20545-20549 (1999)

    • Description
      「研究成果報告書概要(和文)」より
    • Related Report
      2000 Final Research Report Summary
  • [Publications] Aoe, T.: "The KDELreceptor regulates a GTPase-activating protein for ARF1 by interacting with its non-catalytic domain."J Biol Chem. 274. 20545-20549 (1999)

    • Description
      「研究成果報告書概要(欧文)」より
    • Related Report
      2000 Final Research Report Summary
  • [Publications] Aoe.T.,Huber,L.,Vasudevan,C.,Watkins,SC.,Romero.G.,Cassel.D.,HsU.VW: "The KDELreceptor regulates a GTPase-activating protein for ARF1 by interacting with its non-catalytic domain."J Biol Chem.. 274. 20545-20549 (1999)

    • Related Report
      2000 Annual Research Report
  • [Publications] Tomohiko Aoe: "The KDEL receptor regulates a GTPase-activating protein for ARF1 by interacting with its non-catalytic domain"J Biol Chem.. 274. 20545-20549 (1999)

    • Related Report
      1999 Annual Research Report

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Published: 1999-04-01   Modified: 2016-04-21  

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