Collagenase activity in cultures of rat prostate carcinoma.
A specific collagenase (EC 3.4.24.3) has been found and purified from serum-free culture medium of 11095 epidermoid carcinoma of rat prostate. The molecular weight of this collagenase was estimated at 71 000 and the pH optimum was approx. 7. At 26 degrees C, the collagenase cleaved collagen at a site 3/4 the length from the N-terminus. At 37 degrees C, this collagenase degraded collagen to smaller peptides. The enzyme activity was inhibited by serum, cysteine and EDTA, but not by protease inhibitors. The presence of collagenase in rat tumor tissue suggests that this enzyme might play a significant role in tissue invasion by cancer cells.
D000818:Animals; D001769:Blood; D003545:Cysteine / Q000494:pharmacology; D004492:Edetic Acid / Q000494:pharmacology; D006863:Hydrogen-Ion Concentration; D008297:Male; D003012:Microbial Collagenase / Q000037:antagonists & inhibitors / Q000302:isolation & purification / Q000378:metabolism*; D008970:Molecular Weight; D011471:Prostatic Neoplasms / Q000201:enzymology*; D011480:Protease Inhibitors / Q000494:pharmacology; D051381:Rats
D011480:Protease Inhibitors; D004492:Edetic Acid; D003012:Microbial Collagenase; D003545:Cysteine