Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: UMLS:C0596263 (carcinogenesis)
 64,820 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

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.
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PMID:Intestinal epithelial cells contain a high molecular weight protease subject to inhibition by anticarcinogenic protease inhibitors. 156 90

Epidemiological studies suggest that human populations consuming diets rich in protease inhibitors have a reduced incidence of cancer at several sites including the breast. Protease inhibitors, such as the Bowman-Birk inhibitor (BBI) have been shown to be highly effective at suppressing carcinogenesis in a variety of experimental model systems. In this study, we have identified a protease activity in human breast epithelial cells which is inhibited by BBI. This enzyme has a molecular mass of 43 kDa, cleaves gelatin and is primarily localized in the cytosol. Protease activity is maximal at pH 8 and is inhibited by DFP, but unaffected by EDTA, indicating that this enzyme is a serine protease. The protease identified in MCF7 cells has characteristics which are similar to a protease present in human fibroblasts. Hence, our results suggest that BBI targets a common enzyme in human epithelial cells and fibroblasts.
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PMID:A proteolytic activity in a human breast cancer cell line which is inhibited by the anticarcinogenic Bowman-Birk protease inhibitor. 795 38