Purification of Liver Serine Protease Which Activates Microsomal Glutathione S-Transferase: Possible Involvement of Hepsin

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  • Kunii Daisuke
    Laboratory of Functional and Molecular Pharmacology, Graduate School of Medicine, University of the Ryukyus
  • Shimoji Miyuki
    Laboratory of Functional and Molecular Pharmacology, Graduate School of Medicine, University of the Ryukyus
  • Nakama Shinji
    Laboratory of Functional and Molecular Pharmacology, Graduate School of Medicine, University of the Ryukyus
  • Ikebe Masashi
    Laboratory of Functional and Molecular Pharmacology, Graduate School of Medicine, University of the Ryukyus
  • Hachiman Teruyuki
    Laboratory of Functional and Molecular Pharmacology, Graduate School of Medicine, University of the Ryukyus
  • Sato Izumi
    Laboratory of Functional and Molecular Pharmacology, Graduate School of Medicine, University of the Ryukyus
  • Tamaki Atsuko
    Laboratory of Functional and Molecular Pharmacology, Graduate School of Medicine, University of the Ryukyus
  • Yamazaki Kazuko
    Laboratory of Functional and Molecular Pharmacology, Graduate School of Medicine, University of the Ryukyus
  • Aniya Yoko
    Laboratory of Functional and Molecular Pharmacology, Graduate School of Medicine, University of the Ryukyus

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Rat liver microsomal glutathione S-transferase (MGST1) is known to be activated by trypsin, however, it has not been clarified whether MGST1 is activated by a protease present in liver. In the present study we purified the MGST1 activating protease from liver microsomes and finally identified that the protease is hepsin, a type II transmembrane serine protease. When the protease was incubated with the purified MGST1 or liposomal MGST1 at 4 °C, MGST1 activity was increased 3—4.5 fold after 3—6 d. In electrophoretic and immunoblot analyses after the incubation of MGST1 with the protease MGST1 dimer and its degraded fragment were detected. These results suggest that the rat liver microsomal hepsin functions as MGST1 activating/degrading enzyme.

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