title: [Activity and subcellular distribution of lysosomal enzymes in acute pancreatitis induced by CDE diet in mice].
abstract: The aim of the present study was to analyze the activity and subcellular distribution of the lisosomal enzymes and the stability of the lisosomes in acute pancreatitis induced by CDE diet in mice. The activity and the latency of the catepsin-B1 enzymes, acid phosphatase, beta-hexosaminidase and beta-glucuronidase in normal pancreas and in pancreatitis induced by CDE diet were determined. The distribution of the acid phosphatase lisosomal marker was determined in subcellular fractions obtained by differential centrifugation. The activity of the catepsin-B1 enzyme increased 47% in the pancreas of mice with pancreatitis induced by CDE diet. The acid phosphatase activity was not modified and the beta-hexosaminidase and beta-glucuronidase was decreased. The specific activity of the acid phosphatase lisosomal marker also increased in the subcellular fraction containing the zimogene granules and decreased the latency (parameter indicative of lisosome stability) of all the lisosomal enzymes analyzed in the pancreatic homogenate. These results suggest that the lisosomal enzymes, specially the catepsin-B1, and the decrease in the stability of the lisosomes may play a role in the pathogenesis of acute pancreatitis.
authors.affiliation: Institut de Recerca, Hospital de la Santa Creu i Sant Pau, Barcelona.
authors.forename: S
authors.initials: S
authors.lastname: Guillaumes
authors.forename: I
authors.initials: I
authors.lastname: Blanco
authors.forename: A
authors.initials: A
authors.lastname: Villanueva
authors.forename: M D
authors.initials: MD
authors.lastname: Sans
authors.forename: P
authors.initials: P
authors.lastname: Clavé
authors.forename: A
authors.initials: A
authors.lastname: Chabás
authors.forename: A
authors.initials: A
authors.lastname: Farré
authors.forename: F
authors.initials: F
authors.lastname: Lluís
mesh_terms: D000135:Acid Phosphatase / Q000032:analysis; D000208:Acute Disease; D000681:Amylases / Q000097:blood; D000818:Animals; D001669:Biochemical Phenomena; D001671:Biochemistry; D002403:Cathepsins / Q000032:analysis; D002498:Centrifugation; D002796:Choline Deficiency / Q000150:complications; D004032:Diet; D005001:Ethionine / Q000008:administration & dosage; D005260:Female; D005966:Glucuronidase / Q000032:analysis; D008049:Lipase / Q000097:blood; D008247:Lysosomes / Q000201:enzymology*; D051379:Mice; D010179:Pancreas / Q000201:enzymology / Q000473:pathology; D010195:Pancreatitis / Q000201:enzymology* / Q000209:etiology / Q000473:pathology; D013347:Subcellular Fractions / Q000201:enzymology*; D001619:beta-N-Acetylhexosaminidases / Q000032:analysis
chemical_list: D008049:Lipase; D000135:Acid Phosphatase; D000681:Amylases; D005966:Glucuronidase; D001619:beta-N-Acetylhexosaminidases; D002403:Cathepsins; D005001:Ethionine