acid-phosphatase and Pancreatic-Diseases

Organophosphorus compounds are widely used in industry, agriculture and for public health purposes. They are among the toxic compounds employed for insect control. The purpose of this work was to study biochemical, histochemical, and histological as well as ultrastructural changes that might occur in the pancreas of adult male Wistar rats as a result of chronic dimethoate intoxication. The treated group received dimethoate orally via gavage (21 mg/kg) daily for 2 months while, the control group was given saline orally (0.1 ml/100 g/day) for the same period. Plasma glucose level was significantly increased while, plasma insulin level was decreased in the intoxicated animals compared with the control group. A patchy reduction of histochemically-detected succinic dehydrogenase enzymatic activity was observed in the pancreas of the intoxicated rats. By contrast, acid phosphatase enzymatic activity was markedly increased in the pancreas of the intoxicated group. No changes were observed in alkaline phosphatase or alpha esterase activities of the intoxicated animals. Light microscopic examination revealed that dimethoate caused patchy degenerative changes of variable severity in many areas of the pancreas affecting both the pancreatic acini and islets of Langerhans. Ultrastructurally, some beta cells revealed dense nuclei with wide perinuclear cisternae. Diminution of the number of beta granules was evident. One month after discontinuation of the dimethoate, all the above mentioned changes induced by dimethoate intoxication persisted. These findings show that chronic exposure to dimethoate insecticide has clear toxic effect on the rat pancreas, which was not reversible within 1 month. Public health education is necessary to raise people awareness about the hazards accompanying the use of such compounds.

Topics: Acid Phosphatase; Animals; Blood Glucose; Dimethoate; Insecticides; Insulin; Islets of Langerhans; Male; Microscopy, Electron; Pancreas; Pancreatic Diseases; Rats; Rats, Wistar; Succinate Dehydrogenase

This study was performed to assess the effects of misoprostol, a synthetic prostaglandin E1 analog, on cerulein-induced pancreatitis. Per group of 10 each, male Wistar rats received either cerulein (2.5 micrograms/kg/h subcutaneously), cerulein and misoprostol (500 micrograms/kg intraperitoneally at 0 and 4 h), or saline. Rats were killed 6 h after the first injection. Misoprostol treatment significantly reduced interstitial edema and acinar cell lesions induced by hyperstimulation. Pancreatic amylase and chymotrypsin contents were increased by cerulein and returned towards control levels in the misoprostol-treated group. The lysosomal volume density and the pancreatic beta-D-glucuronidase activity were significantly increased after hyperstimulation. The two parameters were significantly reduced by misoprostol. A protective effect of misoprostol against lesions induced by cerulein hyperstimulation would be a consequence of a lysosomal stabilizating effect.

Topics: Acid Phosphatase; Acute Disease; Alprostadil; Amylases; Animals; Ceruletide; Chymotrypsin; Edema; Glucuronidase; Male; Microscopy, Electron; Misoprostol; Organ Size; Pancreatic Diseases; Pancreatitis; Prostaglandins E, Synthetic; Rats; Rats, Inbred Strains

The activity of lysosomal enzymes of the pancreas and the liver has been studied during induction and onset of acute hemorrhagic pancreatic necrosis with fat necrosis (AHPN) in mice. We induced AHPN by feeding the animals a choline-deficient (CD) diet containing 0.5% DL-ethionine (CDE). Control animals were fed either laboratory chow or a plain CD DIET. Increased total activities of cathespin B1, beta-galactosidase, and acid phosphatase were found to occur in pancreas homogenates of mice fed the CDE diet for 2 and 3 days. Release of cathespin B1 into pancreas cytosol was observed after 1 day of feeding. beta-galactosidase and acid phosphatase were increased in pancreas cytosol after 2 and 3 days of feeding. Changes in total activity and location of the lysosomal enzymes did not occur in the liver. Feeding the CD and CDE diets resulted in an increase in the free activity of lysosomal enzymes of both the pancreas and the liver, suggesting the existence of alterations in the lysosomal membrane. Pancreas and liver homogenates were stored on ice up to 3 hours, and the free activity of acid phosphatase and beta-galactosidase were determined at various time intervals. The free activity of both enzymes increased progressively for 3 hours in the pancreas but not in the liver. It is concluded that: 1) induction of AHPN in mice is accompanied by an increase in the activity of lysosomal enzymes of the acinar cells of the pancreas; 2) cathepsin B1 may be responsible for triggering an intraparenchymal activation of zymogens, and 3) pancreatic lysosomes are labilized more easily than liver lysosomes.

Topics: Acid Phosphatase; Animals; Cathepsins; Choline Deficiency; Ethionine; Female; Galactosidases; Hemorrhage; Liver; Lysosomes; Mice; Necrosis; Pancreas; Pancreatic Diseases

Acid hydrolases (lysosomal enzymes) were analyzed and compared with trypsin in duodenal juice obtained after a test meal (Lundh test). The possible diagnostic role of acid hydrolases in pancreatic disease was investigated. In all patients with chronic pancreatitis normal values of acid hydrolases but subnormal trypsin activities were found. In pancreatic cancer normal values of acid hydrolases and normal trypsin values were seen in three patients with small tumors, whereas five patients with more advanced cancer of the pancreas had decreased trypsin activity and three of them high activities of acid hydrolases in duodenal juice. In five patients operated on with a gastroenteroanastomosis acid hydrolases were markedly increased. Five patients had no activity of acid hydrolases in the aspirate, probably reflecting technical failure with dislodgement of the catheter from the duodenum to the stomach. In conclusion the assay of acid hydrolases does not seem to increase the diagnostic value of the conventional Lundh test (trypsin).

Topics: Acetylglucosaminidase; Acid Phosphatase; Adult; Aged; beta-Galactosidase; Duodenum; Female; Humans; Intestinal Secretions; Lysosomes; Male; Mannosidases; Middle Aged; Pancreatic Diseases; Trypsin

Topics: Acid Phosphatase; Alkaline Phosphatase; Amylases; Biliary Tract Diseases; Bone Diseases; Clinical Enzyme Tests; Creatine Kinase; Enzymes; Humans; Isoenzymes; Liver Diseases; Male; Muscular Diseases; Myocardial Infarction; Nervous System Diseases; Organ Specificity; Oxidoreductases; Pancreatic Diseases; Prostatic Diseases; Pulmonary Embolism; Transaminases

Topics: Acid Phosphatase; Animals; Dietary Proteins; Ethionine; Glucuronidase; Golgi Apparatus; Inclusion Bodies; Lysosomes; Macrophages; Male; Microscopy, Electron; Organoids; Pancreas; Pancreatic Diseases; Rats; Regeneration

Topics: 5'-Nucleotidase; Acid Phosphatase; Alkaline Phosphatase; Biliary Tract; Biliary Tract Diseases; Bone Diseases; Disease; DNA; Leucyl Aminopeptidase; Liver Diseases; Pancreas; Pancreatic Diseases; Peptide Hydrolases; Phosphoric Monoester Hydrolases; Protein Tyrosine Phosphatases; RNA; Trees