carboxypeptidase-b and Colonic-Neoplasms

carboxypeptidase-b has been researched along with Colonic-Neoplasms* in 2 studies

Other Studies

2 other study(ies) available for carboxypeptidase-b and Colonic-Neoplasms

Article	Year
Amyloid endostatin induces endothelial cell detachment by stimulation of the plasminogen activation system. Molecular cancer research : MCR, 2003, Volume: 1, Issue:8 Endostatin is a fragment of collagen XVIII that acts as an inhibitor of tumor angiogenesis and tumor growth. Anti-tumor effects have been described using both soluble and insoluble recombinant endostatin. However, differences in endostatin structure are likely to cause differences in bioactivity. In the present study, we have investigated the cellular effects of insoluble endostatin. We previously found that insoluble endostatin shows all the hallmarks of amyloid aggregates and potently stimulates tissue plasminogen activator-mediated formation of the serine protease plasmin. We here show that amyloid endostatin induces plasminogen activation by endothelial cells, resulting in vitronectin degradation and plasmin-dependent endothelial cell detachment. Endostatin-mediated stimulation of plasminogen activation, vitronectin degradation, and endothelial cell detachment is inhibited by carboxypeptidase B, indicating an essential role for carboxyl-terminal lysines. Our results suggest that amyloid endostatin may inhibit angiogenesis and tumor growth by stimulating the fibrinolytic system. Topics: Angiogenesis Inhibitors; Animals; Carboxypeptidase B; Cattle; Cells, Cultured; Colonic Neoplasms; Endostatins; Endothelium, Vascular; Extracellular Matrix; Fibrinolysin; Male; Mice; Mice, Inbred BALB C; Neoplasm Transplantation; Plasminogen; Pulmonary Artery; Tissue Plasminogen Activator	2003
Limited proteolysis of tumor cells increases their plasmin-binding ability. FEBS letters, 1989, Mar-13, Volume: 245, Issue:1-2 Mild proteolytic treatment of SW1116 tumor cells with trypsin or plasmin increases their plasmin-binding ability considerably by increasing the number of binding sites without altering their affinity. This mechanism may be operative for increasing the concentration of active plasmin at the surface of tumor cells. C-terminal lysine residues are involved in plasmin binding to cells, since treatment of cells with carboxypeptidase B decreases this binding by 50%. Topics: Aprotinin; Carboxypeptidase B; Carboxypeptidases; Colonic Neoplasms; Electrophoresis, Polyacrylamide Gel; Fibrinogen; Fibrinolysin; Humans; Peptide Hydrolases; Trypsin; Tumor Cells, Cultured	1989

Article

Year

Amyloid endostatin induces endothelial cell detachment by stimulation of the plasminogen activation system.

Molecular cancer research : MCR, 2003, Volume: 1, Issue:8

Endostatin is a fragment of collagen XVIII that acts as an inhibitor of tumor angiogenesis and tumor growth. Anti-tumor effects have been described using both soluble and insoluble recombinant endostatin. However, differences in endostatin structure are likely to cause differences in bioactivity. In the present study, we have investigated the cellular effects of insoluble endostatin. We previously found that insoluble endostatin shows all the hallmarks of amyloid aggregates and potently stimulates tissue plasminogen activator-mediated formation of the serine protease plasmin. We here show that amyloid endostatin induces plasminogen activation by endothelial cells, resulting in vitronectin degradation and plasmin-dependent endothelial cell detachment. Endostatin-mediated stimulation of plasminogen activation, vitronectin degradation, and endothelial cell detachment is inhibited by carboxypeptidase B, indicating an essential role for carboxyl-terminal lysines. Our results suggest that amyloid endostatin may inhibit angiogenesis and tumor growth by stimulating the fibrinolytic system.

Topics: Angiogenesis Inhibitors; Animals; Carboxypeptidase B; Cattle; Cells, Cultured; Colonic Neoplasms; Endostatins; Endothelium, Vascular; Extracellular Matrix; Fibrinolysin; Male; Mice; Mice, Inbred BALB C; Neoplasm Transplantation; Plasminogen; Pulmonary Artery; Tissue Plasminogen Activator

2003

Limited proteolysis of tumor cells increases their plasmin-binding ability.

FEBS letters, 1989, Mar-13, Volume: 245, Issue:1-2

Mild proteolytic treatment of SW1116 tumor cells with trypsin or plasmin increases their plasmin-binding ability considerably by increasing the number of binding sites without altering their affinity. This mechanism may be operative for increasing the concentration of active plasmin at the surface of tumor cells. C-terminal lysine residues are involved in plasmin binding to cells, since treatment of cells with carboxypeptidase B decreases this binding by 50%.

Topics: Aprotinin; Carboxypeptidase B; Carboxypeptidases; Colonic Neoplasms; Electrophoresis, Polyacrylamide Gel; Fibrinogen; Fibrinolysin; Humans; Peptide Hydrolases; Trypsin; Tumor Cells, Cultured

1989