A trypsin-like neutral protease on Ehrlich ascites cell surfaces: its role in the activation of tumour-cell zymogen of collagenase.
Ehrlich ascites cells in mice have been shown to have a cell-surface trypsin-like neutral protease (TLNP) with proteolytic and beta-naphthylamidase activity. This activity is inhibited by low-mol.-wt inhibitors of trypsin but not by 11 high-mol.-wt inhibitors of trypsin in free solution. We believe that lack of inhibition is due to protection given to the enzyme by the chemical environment of the cell surface. These cells were demonstrated to export a collagenase zymogen which has been shown to be activated by the cell-surface TLNP. When this protease was completely inhibited by low-mol.-wt inhibitors of trypsin, chymotrypsin was used to activate the collagenase zymogen exported by Ehrlich ascites cells. Examination of the products of collagenolysis at 15 degrees C demonstrated the expected 3/4- and 1/4-length alpha-chain fragments derived from monomeric collagen, confirming that collagenase was one of the enzymes responsible for lysis of the collagen fibrils in the test system.
D000818:Animals; D002286:Carcinoma, Ehrlich Tumor / Q000201:enzymology*; D002462:Cell Membrane / Q000201:enzymology; D002478:Cells, Cultured; D003094:Collagen; D004789:Enzyme Activation; D004792:Enzyme Precursors / Q000378:metabolism*; D005782:Gels; D007700:Kinetics; D051379:Mice; D003012:Microbial Collagenase / Q000378:metabolism*; D010447:Peptide Hydrolases / Q000378:metabolism*; D011480:Protease Inhibitors / Q000494:pharmacology; D014361:Trypsin Inhibitors / Q000494:pharmacology
D004792:Enzyme Precursors; D005782:Gels; D011480:Protease Inhibitors; D014361:Trypsin Inhibitors; D003094:Collagen; D010447:Peptide Hydrolases; D003012:Microbial Collagenase