Immunocytochemical localization of exocrine enzymes in rat pancreatic acinar carcinoma.
Ten pancreatic secretory proteins have been demonstrated in differentiated pancreatic acinar carcinoma cells by the protein A-gold immunocytochemical approach. The high resolution of the technique has allowed for the localization of the different proteins in the cellular compartments involved in protein secretion: RER, Golgi and secretory granules. The quantitative evaluation of the labeling for amylase has demonstrated the presence of an increasing gradient in the intensity from the RER to the Golgi and to the secretory granules which may reflect the process of protein concentration along the secretory pathway. These results, together with those obtained using the pulse-labeling autoradiographic approach, demonstrate that differentiated acinar carcinoma cells are capable of processing secretory proteins. When intensities of labeling obtained for different proteins on acinar carcinoma cells were compared to those obtained on normal pancreatic acinar cells, major differences were observed for some proteins. In addition, studies performed on the pancreatic tissue of the tumor-bearing animals have shown the presence of morphological alterations in the acinar cells.
D000818:Animals; D002277:Carcinoma / Q000201:enzymology* / Q000648:ultrastructure; D003851:Deoxyribonucleases / Q000378:metabolism; D006651:Histocytochemistry; D006867:Hydrolases / Q000378:metabolism*; D008049:Lipase / Q000378:metabolism; D008297:Male; D008854:Microscopy, Electron; D010179:Pancreas / Q000201:enzymology*; D010190:Pancreatic Neoplasms / Q000201:enzymology* / Q000648:ultrastructure; D010447:Peptide Hydrolases / Q000378:metabolism*; D051381:Rats; D011916:Rats, Inbred F344; D012260:Ribonucleases / Q000378:metabolism; D000516:alpha-Amylases / Q000378:metabolism
D006867:Hydrolases; D003851:Deoxyribonucleases; D012260:Ribonucleases; D008049:Lipase; D000516:alpha-Amylases; D010447:Peptide Hydrolases