title: Expression of pancreatic digestive enzymes in normal and pathologic epithelial cells of the human gastrointestinal system.
abstract: 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.
authors.affiliation: Second Department of Pathology, Tottori University Faculty of Medicine, Yonago, Japan.
authors.forename: T
authors.initials: T
authors.lastname: Terada
authors.forename: Y
authors.initials: Y
authors.lastname: Kitamura
authors.forename: K
authors.initials: K
authors.lastname: Ashida
authors.forename: Y
authors.initials: Y
authors.lastname: Matsunaga
authors.forename: M
authors.initials: M
authors.lastname: Kato
authors.forename: K
authors.initials: K
authors.lastname: Harada
authors.forename: T
authors.initials: T
authors.lastname: Morita
authors.forename: T
authors.initials: T
authors.lastname: Ohta
authors.forename: Y
authors.initials: Y
authors.lastname: Nakanuma
mesh_terms: D000328:Adult; D000368:Aged; D015153:Blotting, Western; D002918:Chymotrypsin / Q000378:metabolism; D004064:Digestive System / Q000201:enzymology*; D004066:Digestive System Diseases / Q000201:enzymology*; D004067:Digestive System Neoplasms / Q000201:enzymology*; D004848:Epithelium / Q000201:enzymology; D005260:Female; D006801:Humans; D006867:Hydrolases / Q000378:metabolism*; D007150:Immunohistochemistry; D017403:In Situ Hybridization; D008049:Lipase / Q000378:metabolism; D008297:Male; D008875:Middle Aged; D012468:Salivary Gland Neoplasms / Q000201:enzymology*; D012469:Salivary Glands / Q000201:enzymology*; D014357:Trypsin / Q000378:metabolism; D000516:alpha-Amylases / Q000378:metabolism
chemical_list: D006867:Hydrolases; D008049:Lipase; D000516:alpha-Amylases; D002918:Chymotrypsin; D014357:Trypsin