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Glutathione-S-transferase as a selective inhibitor of oncogenic ras-p21-induced mitogenic signaling through blockade of activation of jun by jun-N-terminal kinase

  1. Author:
    Villafania, A.
    Anwar, K.
    Amar, S.
    Chie, L.
    Way, D.
    Chung, D. L.
    Adler, V.
    Ronai, Z.
    Brandt-Rauf, P. W.
    Yamaizumii, Z.
    Kung, H. F.
    Pincus, M. R.

  2. Author Address

    Pincus MR VA Med Ctr, Dept Pathol & Lab Med 800 Poly Pl Brooklyn, NY 11209 USA VA Med Ctr, Dept Pathol & Lab Med Brooklyn, NY 11209 USA Long Isl Univ, Dept Chem Brooklyn, NY USA Long Isl Univ, Dept Biol Brooklyn, NY USA Mt Sinai Med Ctr, Ruttenberg Canc Ctr New York, NY 10029 USA Columbia Univ, Coll Phys & Surg, Div Environm Sci New York, NY USA Natl Canc Inst Tokyo Japan NCI, Lab Biochem Physiol Frederick, MD 21701 USA SUNY Hlth Sci Ctr, Dept Pathol Brooklyn, NY 11203 USA
    1. Year: 2000
  2. Journal: Annals of Clinical and Laboratory Science
    1. 30
    2. 1
    3. Pages: 57-64
  4. Type of Article: Article
  1. Abstract:

    We have identified the intracellular detoxification enzyme, glutathione-S-transferase (GST), as a potent inhibitor of the activation of jun by its kinase, jun-N-terminal kinase (JNK), in vitro. All three major isozymes (alpha, mu, and pi) bind to JNK-jun complexes and inhibit activation of jun by JNK. We now find that GST inhibits JNK-induced oocyte maturation in vivo and strongly inhibits oocyte maturation induced by oncogenic ras-p21 protein, but not by insulin-activated normal cellular p21 protein. These results correlate with the finding that oncogenic, but not insulin-activated normal, p21 induces high levels of activated JNK. GST also strongly blocks induction of oocyte maturation by protein kinase C (PKC) which is a critical downstream target of oncogenic but not normal ras-p21. Thus, we have established a new function for GST as a potent physiological inhibitor of the ras-JNK-jun pathway. [References: 23]

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