chymostatin and Cell-Transformation--Viral

chymostatin has been researched along with Cell-Transformation--Viral* in 1 studies

Other Studies

1 other study(ies) available for chymostatin and Cell-Transformation--Viral

Article	Year
Inhibition of plasminogen activator release from transformed chicken fibroblasts by a protease inhibitor. Cell, 1981, Volume: 27, Issue:1 Pt 2 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. Topics: 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	1981

Article

Year

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

Cell, 1981, Volume: 27, Issue:1 Pt 2

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.

Topics: 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

1981