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Introduction to Cancer
Published in Anjana Pandey, Saumya Srivastava, Recent Advances in Cancer Diagnostics and Therapy, 2022
Anjana Pandey, Saumya Srivastava
Another important factor involved in metastasis is extracellular proteases (Martin et al., 2013). Due to the upregulation of particular proteases, it is converted from its inactive zymogen form to active zymogen form. By binding to specific protease receptor matrix-degrading proteases can associate with the cell surface, which can be considered as a reason for cancer cells to invade the epithelial surface and blood vessel crossing (Sevenich and Joyce, 2014).
Analysis of hydrolytic differences of free and “polyacrylic acid (PAAc)-conjugated trypsin and chymotrypsin” by using fluorescence lifetime distributions
Published in Preparative Biochemistry & Biotechnology, 2020
Ümmügülsüm Polat, İbrahim Ethem Özyiğit, Emine Karakuş
Trypsin and chymotrypsin in the proteolytic enzyme group are synthesized as inactive zymogen enzymes (trypsinogen and chymotrypsinogen) to avert undesirable breaking down of cellular proteins, and to regulate when and where enzyme activity occurs. These inactive zymogens are released into the duodenum, which is the peristaltic movement of the small and large intestines before being thrown away. Moreover, zymogens enter the bloodstream, where they can be found in serum prior to excretion in urine. Zymogens are turned into an active enzyme by proteolysis to split off a pro-peptide, either in a subcellular division or in an extracellular division where they are required for digestion. Although trypsin and chymotrypsin are structurally very similar, they bind different substrates. While trypsin has an effect on lysine and arginine residues, chymotrypsin acts on large hydrophobic residues such as tryptophan, tyrosine, and phenylalanine.[4]