Radtke et al. showed by in situ hybridization that PCI is expressed in the exocrine part of the pancreas, and by Western blotting that the protein is present in pancreatic fluid. We have shown that PCI mRNA and protein are also present in keratinocytes of the human skin. Its expression is increased in the more differentiated layers of the epidermis. PCI is also present in several body fluids and secretions, e.g. in plasma and seminal fluid. In rodents, PCI is almost exclusively present in the reproductive tract. This makes it difficult to study the effect of PCI outside the reproductive tract in animal models. Because of its wide tissue distribution, PCI may have several functions in humans. So far, very little is known about these functions. PCI might have a protective effect against cancer progression. Since PCI has affinity for glycosaminoglycans and phospholipids, both components of the cell membrane, cell membrane association of PCI is not unlikely. We were therefore interested in Evatanepag analyzing the interaction of PCI with serine proteases also present in or on cell membranes. So far there are only a few indications in the literature, suggesting that PCI interacts with type II transmembrane serine proteases. However, as far as inhibition kinetics or the effect of glycosaminoglycans or phospholipids is concerned, no data is available on these interactions. It was therefore the aim of this study to analyze the interaction of PCI with enteropeptidase. EP is a type II transmembrane serine protease, located mainly at the brush border membrane of the epithelial cells of the duodenum and jejunum. Active EP also occurs in duodenal fluid. In the small intestine, EP activates trypsinogen to trypsin. Active human EP is composed of a light and a heavy chain linked by a disulfide bond. The catalytic center is located on the light chain, whereas the heavy chain is responsible for substrate specificity. Activation of trypsinogen is an obligatory step in the pathogenesis of acute necrotizing pancreatitis. So far, it is not fully understood how trypsinogen is activated prematurely in vivo. This function might be executed intracellularly by cathepsin B. Some VX-661 authors also suggest a role of EP by reflux of duodenal fluid into the pancreatic duct. Howeve
