chymostatin and Cell-Transformation--Neoplastic

chymostatin has been researched along with Cell-Transformation--Neoplastic* in 2 studies

Other Studies

2 other study(ies) available for chymostatin and Cell-Transformation--Neoplastic

Article	Year
The conditions for the modification of radiation transformation in vitro by a tumor promoter and protease inhibitors. Carcinogenesis, 1985, Volume: 6, Issue:10 These experiments were designed to define the conditions necessary for the modification of radiation-induced transformation in C3H/10T1/2 cells by TPA and protease inhibitors. The results show that: (i) the lowest effective dose of various protease inhibitors to suppress transformation in vitro varies over several orders of magnitude; on a molar basis, the inhibitors of chymotrypsin appear to be the most effective protease inhibitors at suppression of radiation-induced transformation in vitro, (ii) the protease inhibitors antipain and the Bowman-Birk (soybean) protease inhibitor have no effect on radiation transformation when present only during irradiation, (iii) the protease inhibitor antipain can suppress radiation transformation in vitro when applied to proliferating "initiated' cells as late as 10 days and 13 cell divisions post-irradiation, and (iv) TPA treatment following a 10-day protease inhibitor (anti-pain) exposure of X-irradiated "initiated' cells does not lead to promotion in vitro. These results suggest that protease inhibitor treatment of the initiated cells has irreversibly reverted cells to their original or "uninitiated' condition which existed before irradiation. Topics: Animals; Antipain; Cell Division; Cell Line; Cell Transformation, Neoplastic; Cocarcinogenesis; Mice; Oligopeptides; Phorbols; Protease Inhibitors; Tetradecanoylphorbol Acetate; Time Factors; X-Rays	1985
Detection and partial characterization of a chymostatin-sensitive endopeptidase in transformed fibroblasts. Proceedings of the National Academy of Sciences of the United States of America, 1983, Volume: 80, Issue:2 A chymostatin-sensitive step in the release of plasminogen activator from transformed fibroblasts has been described recently. By using synthetic peptidyl substrates, we have detected and characterized a chymostatin-sensitive peptidase activity in chicken embryo fibroblasts transformed by Rous sarcoma virus. The activity represents a neutral endopeptidase that exhibits phenylalanine specificity and is inhibited by diisopropyl fluorophosphate. A detailed inhibitor profile of the enzyme activity shows that it is distinct from other chymotrypsin-like phenylalanine-preferring peptidases. The endopeptidase activity in transformed fibroblasts is increased over that of parallel cultures of normal fibroblasts. The mechanism of enzyme inhibition by chymostatin is indicated by these studies, and the possible role of the enzyme in modulating plasminogen activator secretion is discussed. Topics: Amino Acid Sequence; Animals; Avian Sarcoma Viruses; Cell Transformation, Neoplastic; Chick Embryo; Endopeptidases; Fibroblasts; Kinetics; Oligopeptides; Protease Inhibitors; Substrate Specificity	1983

Article

Year

The conditions for the modification of radiation transformation in vitro by a tumor promoter and protease inhibitors.

Carcinogenesis, 1985, Volume: 6, Issue:10

These experiments were designed to define the conditions necessary for the modification of radiation-induced transformation in C3H/10T1/2 cells by TPA and protease inhibitors. The results show that: (i) the lowest effective dose of various protease inhibitors to suppress transformation in vitro varies over several orders of magnitude; on a molar basis, the inhibitors of chymotrypsin appear to be the most effective protease inhibitors at suppression of radiation-induced transformation in vitro, (ii) the protease inhibitors antipain and the Bowman-Birk (soybean) protease inhibitor have no effect on radiation transformation when present only during irradiation, (iii) the protease inhibitor antipain can suppress radiation transformation in vitro when applied to proliferating "initiated' cells as late as 10 days and 13 cell divisions post-irradiation, and (iv) TPA treatment following a 10-day protease inhibitor (anti-pain) exposure of X-irradiated "initiated' cells does not lead to promotion in vitro. These results suggest that protease inhibitor treatment of the initiated cells has irreversibly reverted cells to their original or "uninitiated' condition which existed before irradiation.

Topics: Animals; Antipain; Cell Division; Cell Line; Cell Transformation, Neoplastic; Cocarcinogenesis; Mice; Oligopeptides; Phorbols; Protease Inhibitors; Tetradecanoylphorbol Acetate; Time Factors; X-Rays

1985

Detection and partial characterization of a chymostatin-sensitive endopeptidase in transformed fibroblasts.

Proceedings of the National Academy of Sciences of the United States of America, 1983, Volume: 80, Issue:2

A chymostatin-sensitive step in the release of plasminogen activator from transformed fibroblasts has been described recently. By using synthetic peptidyl substrates, we have detected and characterized a chymostatin-sensitive peptidase activity in chicken embryo fibroblasts transformed by Rous sarcoma virus. The activity represents a neutral endopeptidase that exhibits phenylalanine specificity and is inhibited by diisopropyl fluorophosphate. A detailed inhibitor profile of the enzyme activity shows that it is distinct from other chymotrypsin-like phenylalanine-preferring peptidases. The endopeptidase activity in transformed fibroblasts is increased over that of parallel cultures of normal fibroblasts. The mechanism of enzyme inhibition by chymostatin is indicated by these studies, and the possible role of the enzyme in modulating plasminogen activator secretion is discussed.

Topics: Amino Acid Sequence; Animals; Avian Sarcoma Viruses; Cell Transformation, Neoplastic; Chick Embryo; Endopeptidases; Fibroblasts; Kinetics; Oligopeptides; Protease Inhibitors; Substrate Specificity

1983