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Trypsin inhibitors secreted by human colorectal adenocarcinoma cell lines were analyzed by reverse zymography. Among eleven cell lines analyzed, the major inhibitor secreted was protease nexin-II (PN-II), a secreted form of amyloid Β protein precursor (APP) containing a Kunitz-type serine proteinase inhibitor domain. Expression of the APP gene was also confirmed in the cell lines and the main APP mRNA species were PN-II types. The APP gene expression was constant during cell growth  in vitro . On the other hand, the rate of extracellular PN-II accumulation markedly increased after long-term serum-free maintenance of the confluent culture. The extracellular accumulation of PN-II was also strongly stimulated either by interleukin-1β (IL-1β) treatment or to a lesser extent by basic fibroblast growth factor, tumor necrosis factor-α, hepatocyte growth factor or epidermal growth factor. Neither serum depletion-nor IL-1β-induced stimulation of extracellular PN-II accumulation were accompanied by obvious alteration of the levels of APP mRNA and cellular APP holoprotein, suggesting that the enhanced extracellular accumulation of PN-II might result from up-regulation of the secretory pathway of APP. The IL-1β-induced PN-II secretion was significantly inhibited by relatively high concentrations (50–200μg/ml) of aprotinin, a serine proteinase inhibitor, in a dose-dependent manner without obvious cell-toxic effects.

biological chemistry

Secretion of Protease Nexin-II/Amyloid β Protein     Precursor by Human Colorectal Carcinoma Cells and Its Modulation by     Cytokines/Growth Factors and Proteinase Inhibitors