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Large intestine malignancy is the second most common malignancy and second leading cause of cancer mortality in Poland. This is related to late detection of these lesions, e.g. due to lack of effective screening tests. Lesions found by a surgeon are clinically advanced, making the treatment often ineffective and sometimes even completely impossible. Discovery of a substance that would be able to stop key processes for the development of malignancy could change such situation. Activity of certain enzymes was found to increase in malignant cells and invasion of malignancy could be triggered by inadequate amount of endogenous inhibitors of these enzymes in the surrounding healthy tissues. Inhibitors identical with that produced in human cells were found in egg whites.The aim of the study was to determine ability of cystatin isolated from egg whites to inhibit activity of cathepsin B and L.Material and methods. Immunohistochemistry and histology of tissue specimen collected from malignant lesions resected from 60 patients diagnosed with large intestine adenocarcinoma, who underwent surgical treatment in 2nd Department of General and Oncological Surgery, Medical University of Wrocław between 2007 and 2009.Results. Differences were fund between health tissues, margins and center of the malignant lesions with regard to amount and distribution of stained cathepsin B - cystatin complexes. The above mentioned inhibitors were able to inhibit 90% of primary activity of cathepsin B and L in malignant tissues.Conclusions. Cystatins obtained from egg whites could be used as substances supporting anti-cancer therapy in the future.
Proteolytic enzymes are molecular scissors that are responsible for the amide bond breakdown in peptide and protein substrates. Over the years, the view on proteases has been considerably changed from non-specific digestive enzymes to sophisticated biocatalysts, which by performing limited proteolysis control virtually all biological processes. In order to better understand how proteases work and what are their biologically relevant target substrates, it is indispensable to determine their catalytic preferences. This knowledge can be further utilized to develop selective substrates, inhibitors and activity-based probes (ABPs) enabling the monitoring of proteases activity in various settings, from in vitro analysis on recombinant enzymes or cell lysates to ex vivo and in vivo imaging at the single cell level. Among many chemical-based approaches that have been developed and applied over the years, the Hybrid Combinatorial Substrate Library (HyCoSuL) technology has emerged as one of the most powerful one. HyCoSuL is a combinatorial peptide-based library of fluorogenic substrates, that comprise natural and unnatural amino acids, that can deeply explore the chemical space in proteases active site, providing a structural framework for the development of highly-selective chemical tools. In this review we present the most prominent examples of proteolytic enzymes that have been profiled with HyCoSuL approach yielding selective substrates, potent inhibitors, and very sensitive activity-based probes.
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