Project/Area Number |
06454637
|
Research Category |
Grant-in-Aid for General Scientific Research (B)
|
Allocation Type | Single-year Grants |
Research Field |
環境影響評価(含放射線生物学)
|
Research Institution | Kanazawa University |
Principal Investigator |
NIKAIDO Osamu Kanazawa Univ., Dept. of Pharm. Sci., Professor, 薬学部, 教授 (60019669)
|
Co-Investigator(Kenkyū-buntansha) |
ISHIGAKI Yasuhito Kanazawa Univ., Dept.of Pharm. Sci., Research Associate, 薬学部, 教務職員 (20232275)
SUZUKI Fumio Kanazawa Univ., Dept.of Pharm. Sci., Associate Professor, 薬学部, 助教授 (10019672)
|
Project Period (FY) |
1994 – 1995
|
Project Status |
Completed (Fiscal Year 1995)
|
Budget Amount *help |
¥6,300,000 (Direct Cost: ¥6,300,000)
Fiscal Year 1995: ¥2,000,000 (Direct Cost: ¥2,000,000)
Fiscal Year 1994: ¥4,300,000 (Direct Cost: ¥4,300,000)
|
Keywords | Nulceotide excision Repair / Xeroderma pigmentosum / GAPD / Damage recognition / (6-4) photoproducts / Monoclonal antibody / XPA protein / UV-DNA binding factor |
Research Abstract |
UV-damage-specific binding proteins are considered to play important roles in the early steps of DNA repair in human cells irradiated with UV.We have survayd the nuclear and cytoplasmic proteins binding selectively to UV-irradiated DNA.We purifiied one of the binding factors from nuclear extracts to humogeneity, which was designated NF-10. Its molecular weight is - 40kDa. The experimets using photolyases specific for cyclobutane pyrimidine dimer and (6-4) photoproduct revealed that the NF-10 protein binds to UV-DNA though (6-4) photoproducts. By using a monoclonal antibody raised against the NF-10 protein, we could show the existence of the NF-10 protein in all xeroderma pigmentosum complementation group cell lines. This result suggests us that NF-10 is a novel protein different from XPA protein and UV-DNA binding factor previously reported. The immunodepletion of NF-10 protein from cell extract by the antibody decreased the in vitro repair activity, whereas the additon of the protein recovered it. The partial peptide sequences of the protein are almost identical to human glyceraldehyde-3-phosphate dehydrogenase (GAPD). The purified NF-10 protein exerted the GAPD activuty in glycolysis. These results suggest that the GAPD may play a function in nucleotide excision repair as well as in glycolysis, probably in the damage recognition process.
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