title: Effect of duct obstruction on histology and on activities of gamma-glutamyl transferase, adenosine triphosphatase, alkaline phosphatase, and amylase in rat pancreas.
abstract: The effect of pancreatic duct obstruction on the activities of amylase and three nonexocrine pancreatic enzymes was studied in the rat. gamma-Glutamyl transferase (GGTase) activity, which is localized primarily in the plasma membrane of acinar cells, disappeared from the acinar basolateral plasma membrane and declined in specific activity by 80% over a seven-day experimental period. Mg-ATPase, localized primarily in the apical plasma membrane of acinar cells, simultaneously declined in activity in acinar cells but increased in activity in connective tissue. Mg-ATPase specific activity rose 3.5-fold. The histochemical results showed that the ductlike cells resulting from obstruction were derived primarily from acinar cells. Alkaline phosphatase (APase) activity, which is localized in vascular endothelium and the stroma of interlobular ducts, exhibited a dramatic increase in the periacinar, periductal, and interlobular stroma, and specific activity rose 11-fold. Amylase-specific activity declined as did the protein to DNA ratio. Gel electrophoresis showed that the amount of zymogen granule polypeptides declined after duct obstruction, whereas a few other polypeptides increased in amount.
mesh_terms: D000469:Alkaline Phosphatase / Q000378:metabolism*; D000681:Amylases / Q000378:metabolism*; D000818:Animals; D017301:Ca(2+) Mg(2+)-ATPase / Q000378:metabolism*; D008026:Ligation; D008297:Male; D010179:Pancreas / Q000201:enzymology*; D010183:Pancreatic Ducts / Q000502:physiology*; D010195:Pancreatitis / Q000201:enzymology / Q000209:etiology*; D051381:Rats; D011919:Rats, Inbred Strains; D005723:gamma-Glutamyltransferase / Q000378:metabolism*
chemical_list: D005723:gamma-Glutamyltransferase; D000469:Alkaline Phosphatase; D000681:Amylases; D017301:Ca(2+) Mg(2+)-ATPase