alpha-chymotrypsin and Digestive-System-Neoplasms

Pancreatic digestive enzymes have rarely been reported in human nonpancreatic organs. We examined their expression in the epithelial cells of the nonpancreatic gastrointestinal organs, looking for pancreatic alpha-amylase, trypsin, chymotrypsin and pancreatic lipase. Western blotting, enzyme assay and pancreatic alpha-amylase mRNA were also used in selected specimens. In normal tissues, immunoreactivity of one or more of these enzymes was frequently noted in cells of the salivary glands, stomach, duodenum, large pancreatic ducts, extrahepatic bile ducts and gall bladder. The epithelium of the normal oesophagus, small intestine and colon were consistently negative for these enzymes. In pathologic tissues, immunoreactivity for one or more enzymes was present in epithelial cells of pleomorphic adenomas of the salivary glands, oesophageal squamous cell carcinoma, gastric adenoma and adenocarcinoma, pancreatic adenocarcinoma, cholecystitis, adenocarcinoma of the gall bladder and extrahepatic bile duct, and colon adenoma and adenocarcinoma. Western blotting showed a specific band of each enzyme in some specimens of normal stomach. In situ hybridization for pancreatic alpha-amylase mRNA showed specific signals in the normal stomach, but not in the normal colon. Reverse transcriptase polymerase chain reaction analysis for pancreatic alpha-amylase mRNA revealed specific signals in the normal stomach. Enzyme assay revealed that the stomach and gall bladder showed these activities. The data suggest that pancreatic digestive enzymes are produced by several epithelial cell types of the nonpancreatic gastrointestinal organs, that the organs positive for pancreatic enzyme have a common cell lineage, and that neoplasms continue to express or neoexpress these enzymes after neoplastic transformation.

Topics: Adult; Aged; alpha-Amylases; Blotting, Western; Chymotrypsin; Digestive System; Digestive System Diseases; Digestive System Neoplasms; Epithelium; Female; Humans; Hydrolases; Immunohistochemistry; In Situ Hybridization; Lipase; Male; Middle Aged; Salivary Gland Neoplasms; Salivary Glands; Trypsin

Myofibrillar protease activity and activity of inhibitors toward trypsin, chymotrypsin, elastase, and the myofibrillar protease were determined in human skeletal muscle. The protease activity was found to increase in patients with acute and chronic inflammation as well as in patients with metastatic and nonmetastatic tumors. The inhibitory activity directed against trypsin and chymotrypsin was not affected by acute inflammation, while the inhibition of elastase and the myofibrillar protease was increased. Chronic inflammation did not affect the ability of the muscle cytosol to inhibit trypsin and elastase, but increased the inhibition of chymotrypsin and the myofibrillar protease. Nonmetastatic tumors produced an increase in the activity of inhibitors toward trypsin, chymotrypsin, and elastase, while patients bearing metastatic tumors had a high level of cytosolic inhibitors of all the tested proteolytic activities. These results indicate that the myofibrillar protease and the cytosolic protease inhibitors in human skeletal muscle are differentially affected by catabolic conditions.

Topics: Abdominal Muscles; Chymotrypsin; Digestive System Diseases; Digestive System Neoplasms; Humans; Inflammation; Muscles; Pancreatic Elastase; Peptide Hydrolases; Protease Inhibitors; Trypsin