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Intestinal epithelial cells contain a high molecular weight protease subject to inhibition by anticarcinogenic protease inhibitors.

Abstract：

:Protease inhibitors have been shown to be highly effective suppressors of carcinogenesis in both in vivo and in vitro model systems. For example, the soybean derived Bowman Birk inhibitor (BBI) has been shown to inhibit colon carcinogenesis. Although the precise mechanisms by which protease inhibitors suppress carcinogenesis are not known, it is believed that these compounds exert their anticarcinogenic effects by inhibiting specific cellular protease activities involved in the induction and/or expression of the transformed phenotype. In the current report, we describe a BBI-inhibitable proteolytic activity present in intestinal epithelial cells. The protease has a mass of approximately 125 kDa, cleaves gelatin and will bind to a BBI-affinity resin. Subcellular fractionation experiments indicate that this protease is located in the 10,000 x g pellet (lysosomal/golgi fraction) of IEC17 cell homogenates. Further studies have revealed that this proteolytic activity is inhibited by BBI and DFP, but unaffected by EDTA, indicating that this enzyme is a serine protease. Our results suggest that the 125-kDa protease is a 'target enzyme' of the BBI in these cells.

journal_name

Cancer Lett

journal_title

Cancer letters

authors

Habres JM,Billings PC

doi

10.1016/0304-3835(92)90063-2

keywords:

subject

Has Abstract

pub_date

1992-04-15 00:00:00

pages

135-42

issue

2

eissn

0304-3835

issn

1872-7980

pii

0304-3835(92)90063-2

journal_volume

63

pub_type

杂志文章

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