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Protease inhibitor anti-pain suppresses 12-o-tetradecanoyl-phorbol-13-acetate induction of plasminogen-activator in transformable mouse embryo fibroblasts

Academic Article
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Overview

authors

  • Long, S. D.
  • Quigley, James
  • Troll, W.
  • Kennedy, A. R.

publication date

  • 1981

journal

  • Carcinogenesis  Journal

abstract

  • Plasminogen activator (PA) activity was analyzed in normal and transformed 10T1/2 mouse fibroblasts treated with the tumor promoter 12-O-tetradecanoylphorbol-13-acetate (TPA) and the protease inhibitors antipain, leupeptin, and soybean trypsin inhibitor (SBTI). TPA induced PA activity in normal 10T1/2 cells was inhibited by antipain. Transformed 10T1/2 cells maintained high levels of PA activity which were not further stimulated by the addition of TPA. Similarly, antipain inhibited the PA activity of the transformed cultures. Leupeptin and SBTI had no effect. These findings, in light of the fact that antipain has been shown to suppress the promotional effect of TPA in X-ray induced malignant transformation, may suggest a definite role for proteases in the transformational event or maintenance of the transformed state.

subject areas

  • Animals
  • Antipain
  • Cell Transformation, Neoplastic
  • Cells, Cultured
  • Enzyme Induction
  • Female
  • Fibroblasts
  • Leupeptins
  • Mice
  • Oligopeptides
  • Phorbols
  • Plasminogen Activators
  • Plasminogen Inactivators
  • Pregnancy
  • Tetradecanoylphorbol Acetate
  • Time Factors
  • Trypsin Inhibitor, Bowman-Birk Soybean
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Identity

International Standard Serial Number (ISSN)

  • 0143-3334

Digital Object Identifier (DOI)

  • 10.1093/carcin/2.9.933

PubMed ID

  • 6794928
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Additional Document Info

start page

  • 933

end page

  • 936

volume

  • 2

issue

  • 9

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