Abstract
Human pancreatic acinar cells synthesize and store numerous proteins whose intracellular processing has been extensively studied in its homologous guinea-pig cell [1]. Digestive enzymes which constitute most of the pancreatic proteins and lysosomal hydrolases are both synthesized by ribosomes attached to the rough endoplasmic reticulum. The nascent polypetide chains elongate within the cisternae of the reticulum, migrate through this compartment, and are transported to the Golgi complex where the pathways of the two classes of enzymes diverge. Secretory digestive proteins are accumulated into granules and when necessary are discharged into the acinar lumen by fusion-fission of the zymogen granule limiting membrane and the luminal plasmalemma whereas lysosomal hydrolases are usually targeted for inclusion into lysosomes.
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© 1990 Springer-Verlag Berlin Heidelberg
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Figarella, C., Basso, D., Guy-Crotte, O. (1990). Lysosomal Enzyme Activation of Digestive Enzymes During Chronic Pancreatitis?. In: Beger, H.G., Büchler, M., Ditschuneit, H., Malfertheiner, P. (eds) Chronic Pancreatitis. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-75319-0_15
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DOI: https://doi.org/10.1007/978-3-642-75319-0_15
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