Transformed Fibroblasts Anticarcinogenic Bowman-Birk Type Protease Inhibitors in Fluorescent Visualization of Binding and Internalization of the
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چکیده
The Bowman-Birk protease inhibitors from soybeans and chick peas suppress in vitro malignant transformation. This fluorescent microscopy study is designed to visualize the cellular site of action of these protease inhibitors. Binding and internalization of active protease inhibitors occur over a time course of 2 h. The rate and character of fluorescent micro graphs obtained are compared to insulin as a positive control. Internal ization of both molecules is completely blocked at 4°C. Interpretation of the fluorescent micrographs in conjunction with biochemical data (see accompanying paper) suggests the anticarcinogenic action of BowmanBirk type protease inhibitors may involve receptor-mediated endocytosis resulting in the internalization of both the protease inhibitors and a membrane-associated protease.
منابع مشابه
Fluorescent visualization of binding and internalization of the anticarcinogenic Bowman-Birk type protease inhibitors in transformed fibroblasts.
The Bowman-Birk protease inhibitors from soybeans and chick peas suppress in vitro malignant transformation. This fluorescent microscopy study is designed to visualize the cellular site of action of these protease inhibitors. Binding and internalization of active protease inhibitors occur over a time course of 2 h. The rate and character of fluorescent micrographs obtained are compared to insul...
متن کاملFluorescent Visualization of Binding and Internalization of the Anticarcinogenic Bowman-Birk Type Protease Inhibitors in Transformed Fibroblasts1
The Bowman-Birk protease inhibitors from soybeans and chick peas suppress in vitro malignant transformation. This fluorescent microscopy study is designed to visualize the cellular site of action of these protease inhibitors. Binding and internalization of active protease inhibitors occur over a time course of 2 h. The rate and character of fluorescent micro graphs obtained are compared to insu...
متن کاملProteases occurring in the cell membrane: a possible cell receptor for the Bowman-Birk type of protease inhibitors.
The legume-derived Bowman-Birk trypsin and chymotrypsin protease inhibitors (BBI) are effective anticarcinogens in vivo and in vitro. The chymotrypsin-inhibitory domain has been shown to be responsible for this anticarcinogenic action. In this study we identify hydrolytic enzymes by their ability to hydrolyze the relatively specific chymotrypsin substrate succinyl-Ala-Ala-Pro-Phe-aminomethyl co...
متن کاملPotential intracellular target proteins of the anticarcinogenic Bowman Birk protease inhibitor identified by affinity chromatography.
The soybean-derived Bowman Birk inhibitor (BBI) has been shown to inhibit carcinogenesis in both in vitro and in vivo model systems. In the present study, we have utilized a BBI affinity column to determine whether cellular enzymes, present in C3H/10T1/2 cells, specifically interact with this inhibitor. Using this technique, we have identified three proteins with masses of about 70, 60, and 50 ...
متن کاملA growth-regulated protease activity that is inhibited by the anticarcinogenic Bowman-Birk protease inhibitor.
The Bowman-Birk protease inhibitor (BBI) has been shown to be an effective suppressor of carcinogenesis in vivo and in vitro. To elucidate the mechanism(s) by which BBI suppresses carcinogenesis, we believe it will be necessary to identify and characterize the target enzymes that specifically interact with the BBI. We have shown previously that several cellular proteins in C3H/10T1/2 mouse embr...
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