ABSTRACT
Homogeneity in structure and function are broadly assumed to be characteristics of the acinar pancreatic digestive enzyme-secreting tissue. In recent years, physiological studies have shown that the pancreas stores the digestive enzymes in heterogeneously composed pools and releases them from these pools in a cyclic and secretagoguec fashion. The cellular basis for pancreatic heterogeneity is unknown; classical light and electron microscopic preparations appear homogeneous. We applied a panel of biotinylated lectins to pancreatic tissue sections; acinar cell glycoconjugates were localized in situ with peroxidase and fluorescent techniques and lectin-gold complexes. The lectin-binding properties of both fasting rabbit and rat pancreas revealed extensive and specific heterogeneity of the acinar cell population. Light and electron microscopy demonstrated highly heterogeneous labeling of the zymogen granule contents of specific acinar cells with the lectins Ulex europaeus agglutinin (UEA) and Erythrina cristagalli (ECA), which also showed preferential labeling of peri-insular acini. Other lectins also demonstrated heterogeneous binding to specific cellular regions. The striking acinar cell heterogeneity confirms earlier predictions, and may eventually prove to be the cellular basis for the secretion of different enzyme mixtures from heterogeneous sources within the pancreas.
