Disproportional immunostaining patterns of two secretory proteins in guinea pig and rat exocrine pancreatic cells. An immunoferritin and fluorescence study.
Amylase (Am) and chymotrypsinogen (Chtg) were demonstrated in rat and guinea pig exocrine pancreatic cells by immunofluorescence and immunoferritin cytochemistry on thin and ultrathin frozen sections. We describe two observations indicating that Am and Chtg may behave differently in the pre-Golgi phase of their intracellular transport. Firstly, aggregates of material within the RER cisternae of the guinea pig (so-called intracisternal granules) reacted strongly with anti-Chtg, but showed no affinity for anti-Am. Secondly, in both rat and guinea pig, the increase in labeling intensity from cytoplasm (RER) to secretory granules was larger for Chtg than for Am. We hypothesize that the two proteins do not travel in-parallel towards the Golgi complex. Compared with Chtg, Am would lag behind in the RER cisternae.
D000681:Amylases / Q000378:metabolism*; D000818:Animals; D002919:Chymotrypsinogen / Q000378:metabolism*; D004721:Endoplasmic Reticulum / Q000378:metabolism; D005293:Ferritins; D005455:Fluorescent Antibody Technique; D006056:Golgi Apparatus / Q000378:metabolism; D006168:Guinea Pigs; D007158:Immunologic Techniques; D007425:Intracellular Membranes / Q000378:metabolism; D010179:Pancreas / Q000378:metabolism* / Q000648:ultrastructure; D051381:Rats
D005293:Ferritins; D002919:Chymotrypsinogen; D000681:Amylases