Production and secretion of proteolytic enzymes by normal and neoplastic cells.
A possible mechanism for tumor cell invasion of normal tissue might be secretion of proteolytic enzymes. This study compares and contrasts production and secretion of proteinases by cell cultures of normal and chemically transformed mouse epithelial cells. Lysates of normal and neoplastic cells contain similar amounts of neutral proteinase, cathepsin D and plasminogen activator. Neither collagenase nor elastase could be identified in lysates of, or serum-free culture medium bathing, normal or neoplastic cells. Neoplastic cells secrete ten times more plasminogen activator than normal cells. Our data support the hypothesis that plasminogen activator produced by neoplastic cells could fuction to activate latent proteolytic enzymes secreted by connective tissue cells which might result in spread of neoplastic cells into normal tissue.
D000818:Animals; D002403:Cathepsins / Q000096:biosynthesis; D002471:Cell Transformation, Neoplastic; D002478:Cells, Cultured; D004848:Epithelium; D051379:Mice; D010447:Peptide Hydrolases / Q000096:biosynthesis* / Q000378:metabolism; D010960:Plasminogen Activators / Q000096:biosynthesis / Q000378:metabolism
D002403:Cathepsins; D010447:Peptide Hydrolases; D010960:Plasminogen Activators