Effects of S-Nitroso-Cysteine on Proteins That Regulate Exocytosis in PC12 Cells: Inhibitory Effects on Translocation of Synaptophysin and ADP-Ribosylation of GTP-Binding Proteins

DOI Web Site Web Site Web Site Web Site ほか1件をすべて表示 一部だけ表示 被引用文献1件 参考文献68件
  • Naganuma Tomoyoshi
    Department of Pharmacology, Graduate School of Pharmaceutical Sciences, Hokkaido University, Sapporo 060-0812, Japan
  • Maekawa Mutsuko
    Department of Pharmacology, Graduate School of Pharmaceutical Sciences, Hokkaido University, Sapporo 060-0812, Japan
  • Murayama Toshihiko
    Department of Pharmacology, Graduate School of Pharmaceutical Sciences, Hokkaido University, Sapporo 060-0812, Japan Laboratory of Chemical Pharmacology, Faculty of Pharmaceutical Sciences, Chiba University, Chiba 263-8522, Japan
  • Nomura Yasuyuki
    Department of Pharmacology, Graduate School of Pharmaceutical Sciences, Hokkaido University, Sapporo 060-0812, Japan

この論文をさがす

抄録

S-Nitroso-cysteine (SNC) inhibits Ca2+-induced noradrenaline (NA) release from PC12 cells. Since SNC stimulated Ca2+ mobilization from intracellular Ca2+ pools and SNC-induced inhibition of NA release was not washed-out, SNC may modify exocytosis-related proteins that overcome Ca2+ mobilization. In the present study, we investigated the effects of SNC on exocytosis-related proteins in PC12 cells. Ionomycin stimulated NA release and increased the immunoreactivity of synaptophysin in the cytosol fraction. A 25-kDa synaptosome-associated protein (SNAP-25), which localizes to plasma membranes and vesicles, increased in the cytosol fraction after stimulation. The increases in these proteins by ionomycin were inhibited in PC12 cells treated with 0.6 mM SNC. Synaptobrevin and synapsin-1 in the cytosol fraction, and syntaxin and 43 kDa growth-associated protein in the membrane fraction were not affected by ionomycin or SNC. Incubation of each protein with SNC did not affect antibody immunoreactivity. [32P] ADP-ribosylation of GTP-binding proteins (Gi/Go) by pertussis toxin, but not Gs by cholera toxin, was inhibited in SNC-treated PC12 cells and by co-addition of SNC to the assay mixture. These findings suggest that 1) SNC inhibits translocation of vesicles containing synaptophysin and SNAP-25, and 2) SNC reacts with cysteine residues in Gi/Go, causing inhibition of ADP-ribosylation by pertussis toxin.

収録刊行物

  • Jpn.J.Pharmacol.

    Jpn.J.Pharmacol. 84 (4), 391-398, 2000

    公益社団法人 日本薬理学会

被引用文献 (1)*注記

もっと見る

参考文献 (68)*注記

もっと見る

キーワード

詳細情報 詳細情報について

問題の指摘

ページトップへ