Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:P15088 (mast cell)
 14,925 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

On the basis of morphological and biochemical differences, the exocrine pancreatic tissue has been divided in peri- and teleinsular regions. In the present study the enzymatic profile of these regions has been investigated by the immunofluorescent technique using antibodies against nine pancreatic enzymes (alpha-amylase, lipase, chymotrypsinogen A, trypsinogen, elastase, carboxypeptidase A and B, DNase and RNase A). These antibodies were specific to their antigens without cross reaction. By immunofluorescence, most acinar cells of the normal rat pancreas were positive to the nine enzymes tested. However, an inhomogeneity in the staining pattern was found; specifically, the cells located in the periinsular region of many islets showed a brighter fluorescence than acinar cells in the teleinsular tissue. These data add a new parameter to describe the inhomogeneity of the exocrine pancreas.
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PMID:Immunohistochemical localization of exocrine enzymes in normal rat pancreas. 11 Aug 72

Agarose gel electrophoresis (at pH 8.6) was used for qualitative determination of pancreatic enzymes in duodenal juice. The various enzymes were identified by staining techniques with specific chromogenic substrates, by quantitative determination of enzymes in eluates of gel slices, and by immunoelectrophoresis. The various protein bands corresponded to the following enzymes (from the anode to the cathode): chymotrypsin, trypsin, carboxypeptidase A, chymotrypsin, amylase (around the slit), lipase, elastase, and trypsin. The method was applied to a study of exocrine pancreatic function in 10 adults and 83 children suspected of having malabsorption. The duodenal juice, also analyzed for trypsin and amylase content, was collected in fasting condition and after a test meal of water. In patients with normal pancreatic function, all the enzyme bands were present and easy to recognize. In 87 patients carboxypeptidase A was present as two bands in 68 (80%), anodal trypsin as two bands in 39 (45%), and cathodal trypsin as two bands in 85 (97%). Electrophoresis of duodenal juice gave as much information from the fasting sample as after the test meal. Six children with pancreatic insufficiency (cystic fibrosis and Shwachmar's syndrome) had no or only faintly stained enzyme bands and a strongly stained albumin-containing band most anodally. The method is simple, rapid, and useful in routine work. The combination of this qualitative test with a quantitative one (e.g. trypsin determination) provides good information about exocrine pancreatic function.
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PMID:Agarose gel electrophoresis of duodenal juice in normal condition and in children with malabsorption. 43 37

The catalytic concentrations of lipase and carboxypeptidase A in sera of patients with and without pancreatic diseases show no correlation. 40 sera out of 44 with elevated values for lipase, derived from a collective of 135 different sera, showed no increase in the catalytic concentrations of carboxypeptidase A. The demanding titrimetric determination of lipase cannot be replaced by the more simple colorimetric determination of carboxypeptidase A for the laboratory diagnosis of pancreatic diseases.
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PMID:[Lipase and carboxypeptidase A in human serum: no correlation (author's transl)]. 54 41

Changes in the activities of three gastric and nine pancreatic enzymes plus colipase were determined during postnatal development and weaning in calves. In calves exclusively milk-fed for 2, 7, 28, 56, 70 and 119 d, the enzyme activities per kilogram of empty live weight increased with age for chymotrypsin, elastase, carboxypeptidases A and B, ribonuclease and alpha-amylase, decreased for chymosin, lysozyme and colipase but showed no change in the case of pepsin, trypsin, lipase and phospholipase A2 compared with animals at birth. The greatest increase was that in alpha-amylase activity (about 50-fold between d 2 and 119). In calves weaned between d 28 and 56, all the activities were higher than in milk-fed animals, except that of chymosin (which was slightly lower) and that of colipase (which did not change). At 119 d of age, chymotrypsin, carboxypeptidase A, alpha-amylase and lipase were 1.6- to fourfold higher in ruminants than in preruminants. Thus, most enzyme activities were modified first by colostrum and milk intake, and again upon weaning by development of the forestomachs and ingestion of solid food. These ontogenic patterns might be under the control of many gut regulatory peptides, the plasma concentrations of which changed simultaneously. Some gastric and pancreatic enzymes were correlated to plasma concentrations of these gut regulatory peptides.
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PMID:Gastric and pancreatic enzyme activities and their relationship with some gut regulatory peptides during postnatal development and weaning in calves. 137 46

Pancreatic juices were collected by selective reverse catherism of the chief pancreatic duct in two patients, one free from pancreatic disease and the other having a pancreas cancer. They were analysed in detail especially in order to get information on the mechanism of enzyme excretion. The variations of the digestive enzyme activities (amylase, lipase, trypsin, chymotrypsin, carboxypeptidase A and B) were not superimposable among them or with the fluctuations of the protein concentration in the pancreatic juice samples. These results agree with a non-parallel enzyme-excretion mechanism by the pancreas. However deep electrophoresis analyses of pancreatic juice samples showed that the ratio of each digestive enzyme concentration remained almost constant in the same patient. This observation disagrees with the above conclusion and suggests that the data obtained by using classical methods for estimating digestive enzyme activities have to be considered prudently. By another way, two main significant differences were reported by analysing the ionic composition of the pancreatic juice samples following their origin. The pancreatic juice samples of the patient having a pancreas cancer had a lower and more variable Na+ concentration than those coming from the patient who was free from pancreas disease. They had a HCO3- concentration which was almost constant, contrary to what was observed for the pancreatic juice secreted by the other patient.
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PMID:[Detailed analysis of human pancreatic secretions collected by retrograde catheterization. Parallel or non-parallel excretion of digestive enzymes?]. 138 69

In patients exhibiting chronic alcohol abuse, the accumulation of fat droplets in pancreatic acinar cells, as well as changes in pancreatic secretion, can be interpreted as early signs of pancreatic damage. Using rats, (the animals were fed for 9 +/- 1 months with a solution of 20% v/v ethanol, combined with either a normal or a fat enhanced diet) we tested whether or not these symptoms are related both to each other and to morphological lesions of the tissue. Based on six separate histological criteria, the lesions were classified into five stages of severity. In order to characterize the secretory capacity of the pancreas, we measured the outputs of lipase, alpha-amylase, trypsin, chymotrypsin, carboxypeptidase A, elastase, and phospholipase A. Compared with the control group, we found that the alcohol-fed animals exhibited a significantly higher degree of morphological damage to the pancreas, as well as an increased frequency of fat accumulation in the acinar cells, and, with the exception of alpha-amylase, a rise in the level of enzyme secretion. In the animals exhibiting the highest degree of tissue damage, however, both fat accumulation and hypersecretion appeared to be diminished. This diminution could possibly be interpreted as the first sign of chronic pancreatitis. Increased consumption of fat did not change either the level of fat accumulation in the acinar cells, or the level of pancreatic secretion. Within the group of alcohol-fed rats, the most pronounced levels of hypersection were found in animals exhibiting cellular fat accumulation. However, the secretion levels of the alcohol-fed animals exhibiting no such fat accumulation did not differ significantly from that of the control group. Therefore, a relationship appears to exist in rats between fat accumulation in acinar cells and the level of pancreatic secretion.
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PMID:[Correlation between acinar cell fat accumulation and secretory capacity of the rat pancreas in the early stage of alcohol-induced pancreatopathy]. 163 69

A mouse spleen-derived mast cell line (PT-18) was employed to examine the mechanisms of adenosine 3':5'-monophosphate (cAMP)-mediated inhibition of antigen-induced lipid mediator biosynthesis. Specifically, we tested the hypothesis that increasing cAMP in mast cells inhibits lipid mediator biosynthesis by a mechanism independent of effects on histamine release (degranulation) or changes in cytosolic calcium concentration. Forskolin inhibited antigen-induced prostaglandin D2 (PGD2), leukotriene C4 (LTC4), and leukotriene B4 (LTB4) production by 30-50%. In contrast, forskolin had no inhibitory effect on antigen-induced increases in cytosolic calcium concentration, as monitored by the calcium indicator fura-2, or histamine release from the cells. The combination of the phosphodiesterase inhibitor isobutylmethylxanthine with forskolin inhibited the antigen-induced production of PGD2 and LTC4 by 90-100% and histamine release by about 60%. These responses were accompanied by a virtual abolition of the antigen-induced increase in cytosolic calcium. To test further the hypothesis that increasing cAMP can lead to inhibition of lipid mediator biosynthesis in the absence of effects on cytosolic calcium, we employed the calcium ionophores A23187 and ionomycin. Forskolin alone or in combination with isobutylmethylxanthine had no effect on ionophore-induced increases in cytosolic calcium but effectively inhibited leukotriene biosynthesis. In addition, increasing cyclic AMP led to an inhibition of ionophore-induced production of platelet-activating factor and liberation of arachidonic acid. These data suggest that a relatively modest increase in cAMP-dependent protein kinase activity in mast cells leads to inhibition of the lipase-catalyzed cleavage of arachidonic acid from membrane phospholipids in the absence of measurable effects on either histamine release or changes in cytosolic calcium concentration. This effect results in a selective inhibition of the biosynthesis of lipid mediators including LTC4, LTB4, PGD2, and platelet-activating factor.
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PMID:Inhibition by adenosine 3':5'-monophosphate of eicosanoid and platelet-activating factor biosynthesis in the mouse PT-18 mast cell. 169 Nov 75

The synthesis of platelet-activating factor (PAF) and of the 1-acyl analogue of PAF, 1-acyl-2-acetyl-sn-glycero-3-phosphocholine (1-acyl-2-acetyl-GPC) was examined in seven human cell preparations (lung mast cell, basophil, endothelial cell, neutrophil, eosinophil, lung macrophage, platelet) and in human lung fragments. Cells were activated by either an appropriate receptor-mediated stimulus or by ionophore A23187 in the presence of [3H]acetate. All cell types, with the exception of the platelet, responded to stimulation with at least a twofold increase in the formation of labeled 1-radyl-2-acetyl-GPC as compared with control values. A23187 was the more potent stimulus in all cell types examined except the lung mast cell, in which anti-IgE consistently induced the synthesis of more 1-radyl-2-acetyl-GPC. Human lung fragments stimulated by anti-IgE, Ag Amb a I (after passive sensitization), or A23187 also incorporated [3H]acetate into 1-radyl-2-acetyl-GPC. Subclass analysis of 1-radyl-2-acetyl-GPC produced by each cell indicated that the cell types examined can be divided into two groups according to the predominant type of 1-radyl-2-acetyl-GPC produced. Some cell types (mast cell, basophil, endothelial cell) produced predominantly 1-acyl-2-acetyl-GPC, whereas others (neutrophil, eosinophil, lung macrophage) produced almost exclusively PAF. In some cell types, such as the lung mast cell and the basophil, A23187 stimulation increased the synthesis of PAF relative to 1-acyl-2-acetyl-GPC as compared with anti-IgE stimulation. In the lung fragments, [3H]acetate was predominantly incorporated into 1-acyl-2-acetyl-GPC upon IgE-mediated stimulation (anti-IgE, Amb a I) and into PAF upon A23187 stimulation. The differential production of these two phospholipids was confirmed by determining their sensitivity to lipase A1 and phospholipase A2 hydrolysis and by HPLC. These data demonstrate that 1-acyl-2-acetyl-GPC can be synthesized by a variety of human cells involved in the inflammatory reaction. This finding raises fundamental questions about the biologic role of this molecule and the factors regulating its synthesis within inflammatory cells.
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PMID:Differential synthesis of 1-acyl-2-acetyl-sn-glycero-3-phosphocholine and platelet-activating factor by human inflammatory cells. 207

1. RHC 80267 and R59 022 are selective inhibitors of diacylglycerol (DAG) lipase and DAG kinase enzymes respectively. These inhibitors were examined with regard to their effects on oleoylacetylglycerol (OAG)-and anti-IgE- induced histamine secretion in rat peritoneal mast cells. 2. RHC 80267, 10 microM and R59 022, 50 microM both enhanced OAG-induced histamine release by 30% and 40% respectively. 3. In the concentration range 3-30 microM, R59 022 enhanced anti-IgE-induced histamine release by up to about 40%, whereas RHC 80267 was without effect. 4. The enhancement of anti-IgE-induced histamine release by R59 022 is consistent with a role for protein kinase C in transducing immunological signals to rat peritoneal mast cells. 5. The lack of effect of RHC 80267 in this situation may indicate that in the mast cell, DAG kinase is more active than DAG lipase in degrading physiological levels of DAG.
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PMID:The actions of inhibitors of diacylglycerol kinase and diacylglycerol lipase on histamine release from rat peritoneal mast cells. 244 87

This adaptation of a commercially available kit for automated measurement of carboxypeptidase A (CPA; EC 3.4.17.1) activity in serum with the Cobas Bio centrifugal analyzer extends the linear range to an activity concentration of 82 U/L. Results obtained by the described method correlated closely (r = 0.98) with those by the manual kit method. The reference interval for 150 apparently normal individuals was 0.12-0.91 U/L. Total CVs of the method ranged from 4.0% to 13.1%. Bilirubin and glucose decreased the CPA activity in serum by as much as 98% and 26%, respectively. Substantial CPA activity was found in pancreatic tissue, with little activity in intestinal tissue. CPA activity was not as widely distributed in extra-pancreatic tissues as were amylase and lipase activities. Peak activities of CPA, amylase, and lipase in the sera of patients with acute pancreatitis were significantly correlated (r = 0.45 to 0.78, P less than 0.05-0.01). The optimized diagnostic efficiency of CPA for acute pancreatitis was 0.85 at a cutoff value of 5 U/L. Amylase and lipase exhibited similar optimized efficiencies, and parallel testing did not significantly improve diagnostic accuracy. We conclude that automated analysis for CPA activity, even in the absence of interferences, does not add to the diagnostic information provided by the widely available assays for amylase and lipase activity.
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PMID:Measuring carboxypeptidase A activity with a centrifugal analyzer: analytical and clinical considerations. 246 45


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