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Inhibition of plasminogen-activator release from transformed chicken fibroblasts by a protease inhibitor

Academic Article
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Overview

authors

  • Odonnelltormey, J.
  • Quigley, James

publication date

  • 1981

journal

  • Cell  Journal

abstract

  • Chicken embryo fibroblasts (CEF) transformed by Rous sarcoma virus (RSV) exhibit increases in both a cell-associated and a secreted form of plasminogen activator (PA). The mechanism whereby the membrane-bound, cell-associated form of PA is processed to an extracellular, soluble form has been examined in cultures of chicken fibroblasts transformed by a temperature-sensitive mutant of RSV. We report that chymostatin, a protease inhibitor of limited specificity, inhibits the release of PA from tsRSVCEF while causing accumulation of cell-associated PA. Chymostatin's effect on PA release is specific, reversible and appears to be due to its anti-proteolytic capacity. Chymostatin does not inhibit cellular protein synthesis or interfere in the assay used to measure PA. A chymostatin-sensitive protease activity has been found in a membrane fraction isolated from tsRSVCEF.

subject areas

  • Animals
  • Avian Sarcoma Viruses
  • Cell Adhesion
  • Cell Membrane
  • Cell Transformation, Viral
  • Cells, Cultured
  • Chick Embryo
  • Chymotrypsin
  • Oligopeptides
  • Plasminogen Activators
  • Protein Biosynthesis
  • Proteins
  • Secretory Rate
  • Solubility
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Identity

International Standard Serial Number (ISSN)

  • 0092-8674

Digital Object Identifier (DOI)

  • 10.1016/0092-8674(81)90363-9

PubMed ID

  • 6276025
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Additional Document Info

start page

  • 85

end page

  • 95

volume

  • 27

issue

  • 1

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