Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0030305 (pancreatitis)
 16,014 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

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.
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PMID:[Activity and subcellular distribution of lysosomal enzymes in acute pancreatitis induced by CDE diet in mice]. 899 57

The aim of the experiment was to establish and quantify the changes in the activity of acid phosphatase in the pancreas, liver, spleen and kidneys during the course of experimental pancreatitis. The experiment was carried out on 65 male rats of Wistar strain, whose weight varied from 250 to 350 g. The animals were standard fed. They drank only water 24 hours before operation. The rats were randomly divided into three groups: A--intact animals group which were not operated and were used to mark initial biochemical parameters (15 rats), B--the experimental group of animals which were injected by retrograde way with sodium taurocholate into the common bile-pancreatic duct to induce acute necrotic pancreatitis (50 rats). After laparotomy an injection needle was inserted into the common bile-pancreatic duct via the proximal part of the duodenum (Aho's method). After 2, 6, 12, 24, 48 hours rats were anaesthetised again, and thoracotomy was performed by taking blood for amylase determination from the left ventricle of the heart. Then the animals were given an overdose of ketamine, and the organs were removed during laparotomy and frozen at the temp. of -20 degrees C. Alpha-amylase activity in the blood serum was determined by the enzymatic method. Acid phosphatase activity was assayed by spectrophotometric methods using a substrate which releases 4-methyloumbeliferol reacting with the enzyme. The authors concluded that the activity of membranous fraction of acid phosphatase changed non-specifically over the course of experimentally induced acute pancreatitis in rats, but statistically significant difference was found in the enzyme's activity during different periods of pancreatitis only in the pancreas and in the liver.
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PMID:Acid phosphatase activity in different organs as a marker of acute pancreatitis. 1197 40

Polish accomplishments in clinical and experimental pancreatology concern acute (AP) and chronic (CP) pancreatitis. Special notice was drawn in Polish studies on hemostasis disorders in acute experimental pancreatitis (AEP), and resulting clinical implications (possibility of thrombotic-embolic complications leading to hemorrhagic defects associated with coagulation factors consumption). Studies on lysosomal hydrolases role in AEP pathogenesis were discussed. In those studies notice was drawn to initiating role of zymogen activation by lysosomal hydrolases, especially beta-glucuronidase, with smaller activity of acid phosphatase and cathepsin in this process. It was stated, that also lysosomal enzymes are released from macrophages obtained from bronchoalveolar lavage fluid in AEP. It was revealed that prostacyclin (PGI(2)) shows stabilizing effect on lysosomes in liver and kidneys in AEP. Platelets activating factor antagonist inhibits pulmonary lysosomal hydrolases activity in such conditions. Polish studies concerning reactive forms of oxygen role in AEP pathogenesis are one of the first in Europe. Oxidative-antioxidative balance was disturbed in acute pancreatitis course and associated multiorgan changes both under experimental conditions and in humans. Oxidative stress as an early prognostic symptom in AP in humans was also emphasized, showing correlation of oxidative stress indicators with phospholipase A serum activity and polymorphonuclear elastase in plasma of patients with different degree of this disease. In a range of clinical studies special attention should be given to studies concerning lipid disorders as an AP etiological factor in humans. Clear decrease in lipoprotein lipase activity in AP in humans was determined. Polish studies concerning importance of sphincterectomy in acute gallstone derivative pancreatitis (AGP) were presented. Polish researchers accomplishments in chronic alcoholic pancreatitis (CAP) etiopathogenesis were discussed.
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PMID:Pancreas; pancreatitis--Polish accomplishments. 1507 70

Enzymes are biocatalysts and because of their remarkable properties, they are extensively used in medical diagnosis. Researches in the last two decades have concentrated more on enzymes such as creatine kinase-MB, alanine transaminase, aspartate transaminase, acid phosphatase, alkaline phosphatase etc. for clinical applications. Enzymes are the preferred markers in various disease states such as myocardial infarction, jaundice, pancreatitis, cancer, neurodegenerative disorders, etc. They provide insight into the disease process by diagnosis, prognosis and assessment of response therapy. Even though the literature on the use of enzymes in various disease conditions has accumulated, a comprehensive analysis is lacking and hence this review.
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PMID:Enzymes in clinical medicine: an overview. 2426 1


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