title: Tissue distribution of avian pancreatic polypeptide-degrading activity.
abstract: Degradation of avian pancreatic polypeptide (APP) by subcellular fractions from homogenates of chicken kidney, liver, and brain was characterized in this study. Chicken kidney cytosol exhibited the highest degrading activity of all kidney subcellular fractions studied including nuclear, mitochondrial, and microsomal. The cytosolic kidney APP-degrading activity was inhibited in a dose-dependent manner by bacitracin, serine protease inhibitors, and dithiothreitol, and eluted in the void volume of a Sephadex G-100 column, indicating that it is a soluble, serine protease-like activity with a Mr greater than 100,000 kDa and with some dependence on disulfide bonds. Soluble cytosol fractions from chicken liver, kidney, and brain all exhibited greater APP-degrading activity than that of corresponding membrane fractions and, furthermore, were similar in activity between one another. It is concluded that APP degradation by tissue homogenates occurs via a soluble, cytosolic protease which is inhibited by selected serine protease inhibitors; the activity does not differ among liver, kidney, and brain, three tissues which show different receptivity for APP.
authors.affiliation: Department of Biology-Program in Physiology, University of Houston, Texas 77204-5513.
authors.forename: M L
authors.initials: ML
authors.lastname: Adamo
authors.forename: R L
authors.initials: RL
authors.lastname: Hazelwood
mesh_terms: D000818:Animals; D001921:Brain / Q000201:enzymology; D002645:Chickens; D003600:Cytosol / Q000201:enzymology; D007668:Kidney / Q000201:enzymology*; D008099:Liver / Q000201:enzymology; D010191:Pancreatic Polypeptide / Q000378:metabolism*; D010447:Peptide Hydrolases / Q000145:classification / Q000378:metabolism*; D011480:Protease Inhibitors / Q000494:pharmacology; D013347:Subcellular Fractions / Q000201:enzymology
chemical_list: D011480:Protease Inhibitors; C009725:pancreatic polypeptide, avian; D010191:Pancreatic Polypeptide; D010447:Peptide Hydrolases