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Interaction of apohtosis inhibitor PI-9 with cellular factors

Research Project

Project/Area Number 13670314
Research Category

Grant-in-Aid for Scientific Research (C)

Allocation TypeSingle-year Grants
Section一般
Research Field Immunology
Research InstitutionThe University of Tokyo

Principal Investigator

KANAMORI Hiroshi  The University of Tokyo, Faculty of Medicine, Research Associate, 医学部附属病院, 助手 (60211851)

Co-Investigator(Kenkyū-buntansha) OHNISHI Shin  The University of Tokyo, Faculty of Medicine, Lecturer, 医学部附属病院, 講師 (00183236)
Project Period (FY) 2001 – 2003
Project Status Completed (Fiscal Year 2003)
Budget Amount *help
¥1,800,000 (Direct Cost: ¥1,800,000)
Fiscal Year 2003: ¥900,000 (Direct Cost: ¥900,000)
Fiscal Year 2002: ¥900,000 (Direct Cost: ¥900,000)
KeywordsProteinase inhibitor-9 / Phage display / アポトーシス / 肝細胞 / セリン・プロテネース / PI-9
Research Abstract

Granzyme B (GraB) is secreted from cytotoxic T cells (CTL) and ntural killer (NK) cells and plays a key role in the apoptotic reaction of the target cells. Proteinase-9 (PI-9) is known to interact with GrB and prevent cells from apoptotic attack from CTL and NK cells. Recent investigation by others has revealed the interaction of PI-9 with other cellular molecules such as caspase. I and elastase. It has been suggested that this serine proteinase has the potential of binding to several sets of intracellular molecules and has other unknown physiological roles.
We have introduced a system by which PI-9 expression levels were regulated in the presence of tetracycline using HepG2 liver cells. We observed that the upregulation of PI-9 prevent the apoptotic reaction caused by GrB. Induction of PI-9 also prevented the apoptosis by the attack of human NK cell line YT. These observations enable us to utilize this system to observe the effect of the interaction of other molecule with PI-9 on cellular physiology.
We have established a system by which we can produce biotinated recombinant PI-9 by using E. Coli. We have developed a phage display system to obtain oligopeptides with high affinity binding to PI-9 protein. From a library of 12-mer random oligonucleotides, we have obtained a consensus sequence (LLADTTHHRPWT). By employing a data base search (BLAST), we have obtained several known and unknown proteins in which contain homologous amino acid sequence with the consensus sequence.
These results encourage us to further investigate weatherthe interaction of the individual protein with PI-9 may have significant physiological effect.

Report

(4 results)
  • 2003 Annual Research Report   Final Research Report Summary
  • 2002 Annual Research Report
  • 2001 Annual Research Report

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Published: 2002-04-01   Modified: 2016-04-21  

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