Immunohistochemical localization of pancreatic exocrine enzymes in normal and neoplastic pancreatic acinar epithelium of rat.
The transplantable pancreatic acinar carcinomas of rat established recently provide useful model systems to examine the composition of secretory proteins as well as the secretory process in transformed pancreatic exocrine epithelium. The neoplastic acinar cells exhibit considerable variation in the extent of cytodifferentiation. In the present study the enzymatic profile of this heterogeneous tumor cell population has been investigated by the indirect immunofluorescent technique using antibodies against six pancreatic enzymes. By immunofluorescence, all neoplastic cells stained positively for the six enzymes tested: amylase, lipase, carboxypeptidase A, chymotrypsinogen, trypsinogen, and ribonuclease. Some variability in the intensity of immunofluorescence was noted, suggesting possible quantitative differences in the content of a given enzyme among tumor cells. These observations suggest that neoplastic acinar cells with or without secretory granules contain secretory proteins, but to a variable extent.
D000681:Amylases / Q000378:metabolism*; D000818:Animals; D002268:Carboxypeptidases / Q000378:metabolism*; D043422:Carboxypeptidases A; D002919:Chymotrypsinogen / Q000378:metabolism*; D004848:Epithelium / Q000201:enzymology; D005455:Fluorescent Antibody Technique; D005779:Immunodiffusion; D008049:Lipase / Q000378:metabolism*; D010179:Pancreas / Q000201:enzymology*; D010190:Pancreatic Neoplasms / Q000201:enzymology* / Q000473:pathology; D051381:Rats; D012260:Ribonucleases / Q000378:metabolism*; D014362:Trypsinogen / Q000378:metabolism*
D014362:Trypsinogen; D002919:Chymotrypsinogen; D012260:Ribonucleases; D008049:Lipase; D000681:Amylases; D002268:Carboxypeptidases; D043422:Carboxypeptidases A