acid-phosphatase and Pancreatitis

Topics: Acid Phosphatase; Ascites; Chyle; Drainage; Humans; Hypertension, Portal; Kidney Failure, Chronic; Lymph; Pancreatitis; Shock, Hemorrhagic; Sympathetic Nervous System; Thoracic Duct

To elucidate the reason and mechanisms of neutralization of protease inhibitors and antioxidants by proteolytic enzymes and oxidants.. The trial included 92 patients with exacerbation of chronic pancreatitis. 47 of them had chronic recurrent pancreatitis (CRP), 45 patients had chronic fibrozing pancreatitis (CFP). Measurements were made of blood catalase and ceruloplasmin (according to P. Hubl, R. Breschneider and O. Houchin, respectively), alpha1-antitrypsin (by Reiderman), schiff bases (by B. Fletcher et al.), dienic conjugates (by Z. Placer), serum acid phosphatase (by Bodansky), acid phosphatase of polynuclear cells (by R. Nartsissiv), NBT-test was made according to B. Park.. Exacerbation of CRP was associated with enhancement of free radical lipid peroxidation (FPOL), release of proteolytic and lysosomal enzymes from acinar cells, a fall in catalase level. Catalase depression depends on the level of blood lysosomal enzymes and partially on FPOL activity. In CFP moderate activity of FPOL and trypsin is associated with normal levels of lysosomal enzymes and catalase. In both pancreatitis forms, alpha1-antitrypsin levels are low. This lowering is primary and unrelated with inflammatory process in the pancreas. A trypsin rise in both forms depends on lowering of alpha1-antitrypsin which via trypsin inhibits formation of lysosomal enzymes in polynuclear cells. Inability of protease inhibitor to block proteolytic (lysosomal) enzymes manifests in initial intraacinar activation of trypsin from trypsinogen, in inflammatory focus under polynuclear cells release of lysosomal enzymes and in proteolytic enzymes release from the affected acinar structures.. Lack of alpha1-antitrypsin--protease inhibitor--and depression of antioxidant catalase are main and intermediate elements in activation of mechanisms of proteolytic aggression and FPOL.

Topics: Acid Phosphatase; alpha 1-Antitrypsin; alpha 1-Antitrypsin Deficiency; Biomarkers; Catalase; Ceruloplasmin; Chronic Disease; Free Radicals; gamma-Glutamyl Hydrolase; Humans; Lipid Peroxidation; Lysosomes; Neutrophils; Oxidoreductases; Pancreatitis; Trypsin

Activation of digestive zymogens by lysosomal enzymes has been suggested as a triggering event in acute pancreatitis (AP). chloroquine (CQ), a weak base that accumulates in the lysosomes and increases their pH, can inhibit the activity of lysosomal enzymes. In the present study, we examined the effect of CQ on choline-deficient, ethionine-supplemented (CDE) diet-induced AP. CQ-diphosphate (15-50 mg.kg-1) or vehicle was given intraperitoneally at 0, 24, and 48 h to female CD1 mice that were fed with either normal diet or CDE diet. For mortality studies, animals were observed for 168 h. Serum and pancreas samples were collected from animals sacrificed 56 h after the start of the CDE diet. Treatment with CQ at 50 mg.kg-1 significantly (p < 0.05) improved the survival of mice with CDE diet-induced AP. In the normal pancreas, CQ decreased the specific activity of lysosomal enzymes cathepsin B1, beta-hexosaminidase, beta-glucuronidase, and acid phosphatase. In the pancreas with AP, CQ did not modify the activity of cathepsin B1, whereas it increased the latency of all enzymes. In conclusion, our results confirm the beneficial effect of CQ on survival of mice with CDE diet-induced AP and suggest that this effect of CQ may be due to its stabilizing action on lysosomes.

Topics: Acid Phosphatase; Acute Disease; Amylases; Animals; beta-N-Acetylhexosaminidases; Cathepsin B; Chloroquine; Diet; Female; Glucuronidase; Hydrogen-Ion Concentration; Lipase; Lysosomes; Mice; Organ Size; Pancreas; Pancreatitis

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.

Topics: Acid Phosphatase; Acute Disease; Amylases; Animals; beta-N-Acetylhexosaminidases; Biochemical Phenomena; Biochemistry; Cathepsins; Centrifugation; Choline Deficiency; Diet; Ethionine; Female; Glucuronidase; Lipase; Lysosomes; Mice; Pancreas; Pancreatitis; Subcellular Fractions

The main purpose of this study was to investigate the influence of early total parenteral nutrition on acute sodium-taurocholate-induced pancreatitis in rats. Total parenteral nutrition did not change the survival rate, serum amylase, calcium or liver transaminase level on the degree of pancreatic damage, but reduced serum acid phosphatase and lactate dehydrogenase levels. Hyperglycemia occurred during the use of total parenteral nutrition. Total parenteral nutrition is not harmful in the course of acute experimental pancreatitis, and could be used with few side effects.

Topics: Acid Phosphatase; Acute Disease; Amylases; Animals; Calcium; Disease Models, Animal; Hyperglycemia; L-Lactate Dehydrogenase; Liver; Male; Pancreatitis; Parenteral Nutrition, Total; Rats; Rats, Sprague-Dawley; Transaminases

The fine structural changes and the reactivity for acid phosphatase (AcPase) and thiamine pyrophosphatase (TPPase) were studied in thin sections from rat pancreatic acinar cells exposed to dl-ethionine for 2-10 days. The cells from ad libitum and pair-fed controls exhibit occasionally 0.2-0.6 microns circular profiles showing reaction for AcPase and considered as presumptive lysosomes. At days 2 and 4 of dl-ethionine treatment the acinar cells exhibit presumptive lysosomes, autophagosomes and membrane-bounded cytoplasmic areas devoid of electron density and AcPase activity, containing scattered membranous elements. These regions were named lesioned areas. On 6th, 8th and 10th days a membrane bound anomalous cytoplasmic structure that represents a dense pile of layered membrane-like material (multilayered bodies, MB) was seen. The MBs consistently show AcPase activity and in rare instances TPPase activity. Freeze fracture studies reveal that the limiting membrane of the MBs has intramembranous particles whereas the multilayered membranous contents are devoid of such particles. The structure and disposition of the lamellae of the MBs seen in the replicas are similar to those of artificially prepared phospholipidic membranes.

Topics: Acid Phosphatase; Acute Disease; Animals; Ethionine; Freeze Fracturing; Intracellular Membranes; Lysosomes; Male; Microscopy, Electron; Pancreas; Pancreatitis; Rats; Thiamine Pyrophosphatase; Vacuoles

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

In 110 patients with acute pancreatitis the authors studied the activity of intracellular enzymes in the blood (LDH, CPC, ALaT, ASaT, transamidinase) in a complex with indices characterizing the condition of the membrane cell systems, in particular: activity of acid phosphatase, content of 17-ketosteroids, activity of plasma chemiluminescence, concentration of beta-lipoproteins in blood. Complex study of these indices makes it possible to make a sufficiently objective judgement of the severity of the membrane disorders in acute pancreatitis and verity the form and control the treatment of the disease.

Topics: 17-Ketosteroids; Acid Phosphatase; Acute Disease; Adolescent; Adult; Aged; Cell Membrane; Creatine Kinase; Enzyme Activation; Female; Humans; Isoenzymes; L-Lactate Dehydrogenase; Lipids; Male; Middle Aged; Pancreatitis; Transaminases

Both ethanol abuse and protein deficiency result in pancreatic injury. Moreover, these two variables frequently coexist. As lysosomal enzymes may play a role in the initiation of pancreatic injury, the aim of this study was to determine the effects of ethanol consumption and protein deficiency on pancreatic lysosomal stability. For 3 weeks, male Sprague-Dawley rats were match-fed (in groups of four) isocaloric amounts of one of the following liquid diets: (1) protein-sufficient diet, (2) protein-sufficient diet containing ethanol as 36% of the total energy, (3) protein-deficient diet, and (4) protein-deficient diet containing ethanol as 36% of energy. Pancreatic lysosomal stability was assessed by determining (a) latency, as indicated by the percentage increase in lysosomal enzyme activity in pancreatic homogenate induced by Triton X-100, and (b) by the percentage of lysosomal enzyme remaining in the supernatant after sedimentation of the lysosomal pellet from the pancreatic homogenate. Protein deficiency was associated with a decrease in latency and an increase in supernatant enzyme. Ethanol administration was associated with a decreased latency. Both protein-deficient and ethanol-fed animals exhibited higher pancreatic activities of cathepsin B, a lysosomal protease capable of activating trypsinogen. In addition, protein-deficient animals exhibited higher pancreatic activities of acid phosphatase, N-acetyl-glucosaminidase, and beta-glucuronidase. As lysosomal enzymes are postulated to play a role in the initiation of pancreatitis, these results suggest that ethanol consumption and protein deficiency may at least partly exert their toxic effects on the pancreas by altering pancreatic lysosomal stability and increasing the glandular content of cathepsin B.

Topics: Acetylglucosaminidase; Acid Phosphatase; Alcohol Drinking; Animals; Cathepsin B; Dietary Proteins; Glucuronidase; Intracellular Membranes; Lysosomes; Male; Pancreas; Pancreatitis; Protein Deficiency; Rats; Rats, Inbred Strains

Topics: Acid Phosphatase; Alkaline Phosphatase; Chronic Disease; Glycogen; Humans; Neutrophils; Pancreatitis; Peroxidase; Phagocytosis

The liver affection in acute experimental pancreatitis (AEP) could be reflected by changes of enzymatic activity in the liver and in serum. The histoenzymatic studies of the liver of dogs with AEP of different severity and time of duration induced according to Elliott's method were performed and the constellation of serum enzymatic activities considering treatment with prostacyclin was estimated. The histoenzymatic reactions on succinic dehydrogenase, lactic dehydrogenase and alkaline phosphatase were depressed with progression of time and severity of AEP. In contrast, the reaction on acid phosphatase was augmented at the same time. Serum AspAT, AlAT and alkaline phosphatase were augmented in the later phase of AEP, but acid phosphatase and beta-glucuronidase were not significantly changed. The treatment with PGI2 limited both histoenzymatic reactions and alterations of serum enzymatic activities. These results support the significance of changes in enzymatic activities in the course of liver reaction on pancreatogenic noxa during acute pancreatitis, and suggest the protective effect of PGI2 against liver injury in this disease.

Topics: Acid Phosphatase; Acute Disease; Alanine Transaminase; Alkaline Phosphatase; Animals; Aspartate Aminotransferases; Dogs; Epoprostenol; Female; L-Lactate Dehydrogenase; Liver; Male; Pancreatitis; Succinate Dehydrogenase

The pulmonary complications are severe sequeles of acute pancreatitis. The pathogenesis of these complications is unsolved. The purpose of this work was to evaluate the status of lung lysosomes and phospholipase A activity in acute experimental pancreatitis (AEP) and the effect of heparin as a potentially protective agent. Taurocholate-induced AEP in rats lasting 24 and 48 hours was treated with heparin intraperitoneally (2 mg/kg every 8 hours). The total activity of cathepsins and B-glucuronidase in lysosomal enriched subfraction increased markedly during 48 hours of AEP in untreated animals, but the relative free activity was maximal after 24 hours. Free activity of cathepsins and acid phosphatase in supernatant was maximal after 24 hours. The phospholipase A activity was maximally elevated (more than twofold) after 48 hours. Heparin prevented the increase of activity of B-glucuronidase, depressed the relative free activity of all investigated lysosomal hydrolases and inhibited the phospholipase A activity in the lung homogenate. Our results indicate the significance of labilization of lung lysosomes and increment of phospholipase A activity in the lungs in the damage of this organ during AEP in the rats, and suggest the beneficial effect of heparin on these factors.

Topics: Acid Phosphatase; Acute Disease; Amylases; Animals; Cathepsins; Glucuronidase; Heparin; Hydrolases; Lipase; Lung; Lung Diseases; Lysosomes; Male; Pancreatitis; Phospholipases; Phospholipases A; Rats

Majority of literature data support the significance of proteases activation in pathogenesis of acute pancreatitis. The ability of cathepsins to the activation of trypsinogen was shown and the labilization of lysosomes of pancreas in different models of acute experimental pancreatitis (AEP) was reported. In present work the dynamic of lysosomal changes during the course of AEP in dogs is evaluated. AEP was induced in 17 mongrel dogs by Elliot's method. Six healthy dogs served as a control group (I). Pancreatitic dogs were killed after 6 hr (G. II, n = 5), after 12 hrs (G. III, n = 5), and after 24 hrs (G. IV, n = 6 survivors). The pancreata were removed and divided into segments A (less advanced changes, [B] most advanced changes) and C (intermediate changes). The lysosomal enriched subfraction was isolated from the C segments at 15 000 X g for 20 min. The total (T) and free (F) activity of beta-glucuronidase (beta-G), acid phosphatase (AP), acid cathepsins (Cs) was estimated and the value F/T (relative free activity-r.f.a.) was calculated as an index of lysosomal stability. The progressive increase of r.f.a. of hydrolases in whole homogenate and in lysosomal enriched subfraction depending on time of AEP was observed suggesting labilization of pancreatic lysosomes. This labilization was more expressed in corresponding parts of organ with more advanced pathological changes. The differences between part A and B were most evident after 6 hrs of AEP. The labilization of lysosomes is more pronounced after 12 and 24 hrs than after 6 hrs in analogical parts of organ. These results indicate that labilization of lysosomes in pancreas correspond to the degree of pathological changes of pancreatic tissue.

Topics: Acid Phosphatase; Acute Disease; Animals; Cathepsins; Disease Models, Animal; Dogs; Female; Glucuronidase; Hydrolases; Lysosomes; Male; Pancreas; Pancreatitis; Reference Values; Time Factors

The effects of hormonal or cholinergic stimulation on survival and on activities of lysosomal enzymes and amylase in pancreatic tissue and ascites were studied in rats with induced pancreatitis. Pancreatitis per se caused an increase of the activities of cathepsin D, N-acetyl-beta-D-glucosaminidase and amylase, and a decrease of acid phosphatase in pancreatic tissue. Pancreatic protein concentration was not influenced. In pancreatitic rats administration of cerulein or carbachol markedly decreased survival rate. Cerulein increased the activities of cathepsin D and amylase in ascites and cathepsin D and acid phosphatase in pancreatic tissue. Carbachol increased the activities of cathepsin D and amylase in ascites and acid phosphatase in pancreatic tissue. Both cerulein and carbachol decreased the activity of amylase in pancreatic tissue. Administration of secretin or the anticholinergic drug Pro-Banthine did not influence survival rate or the activities of lysosomal enzymes and amylase in ascites. In pancreatic tissue the activity of acid phosphatase was slightly increased by secretin or Pro-Banthine. In conclusion, the results show a nonparallel alteration of lysosomal enzyme activities in pancreatic tissue in rats with pancreatitis. Cerulein and cholinergic stimulation decreased survival rate and brought about a marked increase of cathepsin D activity in ascites and, in the case of cerulein, also in pancreatic tissue. The implication of lysosomes and especially the catheptic proteases in the pathogenesis and outcome of acute pancreatitis deserves further attention.

Topics: Acetylglucosaminidase; Acid Phosphatase; Acute Disease; Amylases; Animals; Ascitic Fluid; Carbachol; Cathepsin D; Cathepsins; Ceruletide; Hexosaminidases; Lysosomes; Male; Pancreas; Pancreatitis; Propantheline; Rats; Rats, Inbred Strains; Secretin

Nine lysosomal enzymes and alkaline phosphatase have been assayed in human pancreatic juice from controls and patients with chronic calcifying pancreatitis. Specific activities were evaluated by a nonparametric test (Wilcoxon) with a probability of 2 P less than or equal to 0.5. The values of acid phosphatase, alpha-glucosidase, beta-glucosidase and alpha-galactosidase are significantly higher in pathological juices; the values of alpha-mannosidase and beta-glucuronidase are also increased in the same patients but at the limit of significance. Alkaline phosphatase, beta-hexosaminidase and alpha-fucosidase follows the same trend but the values are not statistically significant between the two groups of patients. Studies on skin cultures of four patients with chronic calcifying pancreatitis demonstrate that the increased specific activities of lysosomal enzymes in the pathological juices do not correspond to a leakage of these enzymes into the extracellular space as described for cystic fibrosis.

Topics: Acid Phosphatase; Alkaline Phosphatase; alpha-Glucosidases; Calcinosis; Cells, Cultured; Chronic Disease; Cystic Fibrosis; Fibroblasts; Humans; Hydrolases; Lysosomes; Pancreatic Juice; Pancreatitis

Topics: Acid Phosphatase; Acute Disease; Alkaline Phosphatase; Animals; Cats; Electron Transport Complex IV; Esterases; Male; Pancreas; Pancreatitis; Succinate Dehydrogenase

Topics: Acid Phosphatase; Acute Disease; Alkaline Phosphatase; Animals; Cats; Electron Transport Complex IV; Esterases; Exocrine Glands; Male; Pancreatitis; Pylorus; Succinate Dehydrogenase

Topics: Acid Phosphatase; Acute Disease; Alkaline Phosphatase; Animals; Cats; Cytochromes; Electron Transport Complex IV; Histocytochemistry; Kidney; Male; Pancreatitis; Succinate Dehydrogenase; Succinates

Recently developed enzyme tests that are used in (a) identifying high risk populations, (b) diagnosing cancer, (c) following treatment response of cancer patients, and (d) the selection of cancer therapy are summarized. The diagnostic role of methionine adenosyltransferase and CSF monoamine oxidase activity measurements in the diagnosis of schizophrenia are discussed. The role of N-acetyltransferase in the conversion of serotonin to melatonin in the pineal gland and the importance of these changes for the synchronization of the functioning of cells throughout the organism are described. New developments in the determination of immunoreactive trypsin in the early diagnosis of pancreatic diseases are summarized.

Topics: Acid Phosphatase; Aryl Hydrocarbon Hydroxylases; Arylamine N-Acetyltransferase; Breast Neoplasms; Chemistry, Clinical; Clinical Enzyme Tests; Female; Galactosyltransferases; Humans; Male; Neoplasm Staging; Neoplasms; Pancreatitis; Pineal Gland; Prostatic Neoplasms; Schizophrenia; Sialyltransferases; Trypsin

A model of chronic pancreatitis has been created in 13 mongrel dogs. The animals were withdrawn from the experiment 2 months after the beginning of it. According to the author's data, artifically created insufficiency of the constrictors of the common bile and pancreatic ducts in dogs is analogous to unfitness of the sphincter in man and results in the development of the changes in the abdominal cavity, specific for chronic pancreatitis.

Topics: Acid Phosphatase; Alkaline Phosphatase; Animals; Chronic Disease; Common Bile Duct; Disease Models, Animal; DNA; Dogs; Pancreas; Pancreatic Ducts; Pancreatitis; RNA; Sphincter of Oddi

In 12 dogs with acute experimental pancreatitis (AEP) and 6 control animals the "free", "latent" and "total" activity of acid phosphatase, beta-glucuronidase and cathepsins in whole homogenates of the pancreas, in a lysosomal-enriched subfraction and the supernatant of pancreatic tissue was estimated. AEP was induced by injection of bile salts and thrombin solution into the pancreatic duct. In 6 dogs the protection with heparin (1.5 mg/kg/body weight) immediately after producing AEP was applied. In AEP without any protection the free activity of hydrolases in the whole homogenate (80--90%) and in the lysosomal enriched subfraction (75--90%) was higher than in the controls (60--70% and 55--75% respectively), suggesting an augmented lysosomal fragility during the course of AEP. Heparin depressed the free activity of hydrolases to 60--80% in whole homogenates, and 64--75% in the lysosomal enriched subfraction. The release of cathepsins during incubation of the lysosomal-enriched subfraction in acidic medium was lower in the group with heparin treatment. The data obtained suggest the stabilising effect of heparin on the lysosomes of the pancreas during acute experimental pancreatitis in dogs.

Topics: Acid Phosphatase; Acute Disease; Animals; Dogs; Heparin; Hydrolases; Lysosomes; Pancreas; Pancreatitis

Topics: Acid Phosphatase; Acute Disease; Animals; Dogs; Female; Glucagon; Heparin; Histocytochemistry; Lysosomes; Male; Pancreas; Pancreatitis

In dogs with acute experimental pancreatitis (AEP) induced according to Elliotts method the total, free and latent activity of lysosomal hydrolases (acid phosphatase, beta-glucuronidase and cathepsins) in whole homogenates and some subfractions of pancreas were studied. The animals were divided into three groups of 6 dogs each: I. control healthy dogs. II. AEP-treated with glucagon (0.33 mg of glucagon in drop infusion 3 times every six hours). III. AEP without any drug treatment. In dogs treated with glucagon the significant decrease of relative free activity of all tested hydrolases (66-80%) in comparison with the group without any treatment (III/80-90%) was found. Moreover significant decrease of total catheptic activity (about 1/3) in the former group was demonstrated. Incubation of lysosomal enriched fraction taken from group II/in medium buffered to pH 5.0 caused decreasing release of catheptic activity (60% of total) in comparison with the group III (75%). The histochemical reaction for acid phosphatase according to Gomoris method in pancreatic acinar cells of dogs treated with glucagon was less intensive than reaction in untreated animals. These results indicate on the less impairment of pancreatic lysosomes in AEP treated with glucagon in comparison with that in untreated animals.

Topics: Acid Phosphatase; Acute Disease; Animals; Cathepsins; Dogs; Glucagon; Glucuronidase; Hydrolases; Lysosomes; Pancreas; Pancreatitis

Adult white mice were continually treated by intraperitoneal injections of normal serum of various species (neat, horse, man, rabbit, mouse) for 3 hours up to 16 days. Control animals received injections of physiological saline under the same conditions. In the mouse pancreas, the repeated intraperitoneal injections of foreign serum conformably resulted in an interstitial edema, a first granulocytic and histiocytic, later on markedly lymphoplasmactyic interstitial inflammation with single dystrophic acinar cells as well as in a mild intersitial fibrosis after 8 or 16, resp., days of serum application. Histochemically, the exocrine pancreas cells showed a moderate increase in activity of adenosintriphosphatase, nonspecif esterase as well as acid and acaline phosphatase. All the changes described were most considerably pronounced after treatment with bovine serum. The interstitial pancreatitis after continual foreign serum applications regarded as the morphologie expression of a pathogenic immune phenomenon of the serum sickness type in case of a serum sickness reaction taking place preferably in the peritoneal cavity.

Topics: Acid Phosphatase; Adenosine Triphosphatases; Alkaline Phosphatase; Animals; Blood; Cattle; Edema; Esterases; Histiocytes; Horses; Humans; Immunization; Leukocytes; Lymphocytes; Male; Mice; Pancreas; Pancreatitis; Peritoneal Cavity; Rabbits; Serum Sickness; Time Factors

Topics: Acid Phosphatase; Acute Disease; Animals; Cathepsins; Dogs; Hemorrhage; Lipase; Pancreatitis; Phospholipases; Trypsin

Topics: Acid Phosphatase; Adenosine Triphosphatases; Alkaline Phosphatase; Animal Nutritional Physiological Phenomena; Animals; Electron Transport Complex IV; Esterases; Ethionine; Female; Pancreas; Pancreatitis; Rats; Succinate Dehydrogenase

Topics: Acid Phosphatase; Adenosine Triphosphatases; Alkaline Phosphatase; Animals; Disease Models, Animal; Dogs; Histocytochemistry; Methods; Pancreas; Pancreatitis; Phosphoric Monoester Hydrolases

Topics: Acid Phosphatase; Animals; Cytoplasm; Esterases; Histiocytes; Histocytochemistry; Microscopy, Electron; Pancreas; Pancreatitis; Prednisone; Rats

Topics: Acid Phosphatase; Animals; Common Bile Duct; Cystic Fibrosis; Cytoplasmic Granules; Dilatation; Dogs; Endoplasmic Reticulum; Golgi Apparatus; Ligation; Male; Microscopy; Microscopy, Electron; Pancreas; Pancreatic Ducts; Pancreatitis; Rats; Sclerosis; Species Specificity

Topics: Acid Phosphatase; Acute Disease; Aminocaproates; Amylases; Animals; Aprotinin; Dogs; Fibrinogen; Heparin; Lysosomes; Necrosis; Pancreas; Pancreatitis; Protease Inhibitors

Topics: Acid Phosphatase; Alkaline Phosphatase; Animals; Histocytochemistry; Humans; Morphine; Pancreas; Pancreatitis; Rats; RNA

Topics: Acid Phosphatase; Alanine Transaminase; Alkaline Phosphatase; Amylases; Aspartate Aminotransferases; Clinical Enzyme Tests; Creatine Kinase; D-Alanine Transaminase; Diagnosis, Differential; Humans; Liver Diseases; Muscular Diseases; Myocardial Infarction; Pancreatitis