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Proteolytic activities of mouse sarcoma 180 cells that are inhibited by Bowman‐Birk and Kunitz protease inhibitors
Author(s) -
Chu ShuChen,
Chou FenPi,
Liu JerYuh,
Lin LiJen,
Hsieh YihShou
Publication year - 1997
Publication title -
iubmb life
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.132
H-Index - 113
eISSN - 1521-6551
pISSN - 1521-6543
DOI - 10.1080/15216549700203411
Subject(s) - proteases , trypsin , protease , serine protease , enzyme , zymography , proteolytic enzymes , serine , cytosol , biochemistry , matrix metalloproteinase , protease inhibitor (pharmacology) , microbiology and biotechnology , chemistry , biology , virus , immunology , antiretroviral therapy , viral load
In this study, using zymogram analysis two proteolytic activities were identified in the mouse sarcoma 180 (S‐180) cells that were activated by trypsin treatment and inhibited by both BBI and ACTI. These enzymes, with molecular weights of 46 kDa (dominant band) and 62 kDa (minor band), were mainly localized in the cytosol, and had optimal activity at pH 7 and 8 respectively. Their inhibition by DFP, BBI and ACTI but not EDTA and TPCK indicated they were trypsin‐like serine proteases and may be the intracellular target‐enzymes of protease inhibitors. The level of the precursor of the 62 kDa protease was significantly increased in the S‐180 solid and soft tumors, whereas the level of the 46 kDa precursor was almost undetectable, implying that a physiological role may be played by these serine proteases during tumor invasion.