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REGULATION OF ZINC PROTEINS AND CELLULAR ZINC HOMEOSTASIS

Research Project

Project/Area Number 07457541
Research Category

Grant-in-Aid for Scientific Research (B)

Allocation TypeSingle-year Grants
Section一般
Research Field Biological pharmacy
Research InstitutionFACULTY OF PHARMACEUTICAL SCIENCES,KYUSHU UNIVERSITY

Principal Investigator

OGURI Kazuta  KYUSHU UNIV., FAC.PHARM.SCI., PROFESSOR, 薬学部, 教授 (70037589)

Co-Investigator(Kenkyū-buntansha) ISHII Yuji  KYUSHU UNIV., FAC.PHARM.SCI., INSTRUCTOR, 薬学部, 助手 (90253468)
Project Period (FY) 1995 – 1996
Project Status Completed (Fiscal Year 1996)
Budget Amount *help
¥1,500,000 (Direct Cost: ¥1,500,000)
Fiscal Year 1996: ¥1,500,000 (Direct Cost: ¥1,500,000)
Keywordscytosol / aldolase / rat / alcohol dehydrogenase / triose phosphate / tyrosine phosphatase / carbonic anhydrase / polychlorinated biphenyl / ホメオスタシス / 亜鉛フィンガー / 転写調節因子
Research Abstract

Toxic manifestation of coplanar PCB is thought to be mediated by aromatic hydrocarbon (Ah)-receptor. However, the suppression of protein expression by coplanar PCBs is scarcely clarified. We report here the suppression of cytosolic proteins by a coplanar PCB-treatment and propose new aspects of the toxicity. Male Wistar rats were treated with PenCB (single 25 mg/kg, i. p.). Free- and pair-fed control groups were treated with vehicle. At the day 5, the liver cytosol was prepared. The cytosolic proteins were compared among three groups by SDS-PAGE and two-dimensional RAGE (2D-PAGE). Expression level of cytosolic 40-kDa and 27-kDa proteins in rat liver were markedly suppressed by PenCB-treatment. The 40-kDa proteins were identified as aldolase B (Ald B) and alcohol dehydrogenase (ADH) class I by amino acid sequencing of the internal peptides. The 27-kDa protein was also identified as carbonic anhydrase III (CA II). The liver cytosolic Ald and ADH activities were significantly reduced to about 50% and 60% of both control groups by PenCB-treatment. Immunoblotting after sD-PAGE demonstrated that Ald B was markedly suppressed by PenCB-treatment, while change in Ald A was slight. The reduction of ADH by PenCB-treatment was also verified by immunoblotting. The significant suppression of CA III by PenCB-treatment in rat liver was demonstrated by immunoblotting using CA III-selective antibody. Ald plays an important role in glycolytic and gluconeogenetic pathways. In addition, ADH catalyzes biotransformation of triose phosphate to glycerol-3-phosphate. Sippression of Ald B and ADH may be a key biochemical lesion for disordered intermediary metabolism occurring by PenCB-treatment and should be taken into an account as a cause of the wasting syndrom which is a severe toxic effect of toxic coplanar PCBs. CA III possesses tyrosine phosphatase activity, therefore, its suppression could account for the effects on signal transduction by toxic coplanar PCBs.

Report

(3 results)
  • 1996 Annual Research Report   Final Research Report Summary
  • 1995 Annual Research Report
  • Research Products

    (3 results)

All Other

All Publications (3 results)

  • [Publications] Yuji Ishii et al.: "Significant suppression of rat liver aldolase B by a toxic coplanar polychlorinated biphenyl,3,3′,4,4′,5-pentachlorobiohenyl" Toxicology. 116. 193-199 (1997)

    • Description
      「研究成果報告書概要(和文)」より
    • Related Report
      1996 Final Research Report Summary
  • [Publications] Ishii, Y., Kato, H., Hatsumura, M., Ishida, T.Ariyoshi, N., Oguri, K.: "Significant suppression of rat liver aldolase B by a toxic coplanar polychlorinated biphenyl, 3,3', 4,4', 5-pentachlorobiphenyl" Toxicology. 116. 193-199 (1997)

    • Description
      「研究成果報告書概要(欧文)」より
    • Related Report
      1996 Final Research Report Summary
  • [Publications] Yuji Ishii et al.: "Significant suppression of rat liver aldolase B by a toxic coplanar polychlorinated biphenyl,3,3',4,4',5-pentachlorobiphenyl" Toxicology. 116. 193-199 (1997)

    • Related Report
      1996 Annual Research Report

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Published: 1996-04-01   Modified: 2016-04-21  

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