Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:3.2.1.20 (alpha-glucosidase)
 4,237 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

In order to evaluate the renal metabolism of amylase and immunoreactive trypsin (IRT) in chronic pancreatic disease, we assayed amylase, IRT and creatinine in serum and urine and gamma-glutamyl transferase (GGT) in dialyzed urine as well as alpha-glucosidase (AGL) and ribonuclease (RNase) in 24 control subjects, 34 patients with pancreatic cancer, 52 with chronic pancreatitis and 32 with extra-pancreatic diseases. Urinary amylase and IRT outputs were found to be more elevated in chronic pancreatitis than in control subjects. The levels of serum amylase, its renal inputs and outputs were correlated with the corresponding IRT values. Multiple regression analyses (dependent on amylase or IRT urinary outputs, circulating levels of the two enzymes, creatinine clearance and the excretion of GGT, AGL and RNase predictor variables) showed significant correlations. The standardized partial regression coefficients found to be significant were: GGT, RNase and serum amylase for amylase, and GGT and RNase for IRT. No difference was found between amylase and IRT outputs in patients with chronic pancreatitis, taking the presence or the absence of alcohol abuse, exocrine insufficiency and pancreatic pseudocysts into consideration. Urinary GGT excretion correlated with serum amylase and IRT levels.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Renal handling of amylase and immunoreactive trypsin in pancreatic cancer and chronic pancreatitis. 169 Oct 65

Urinary excretion of alpha-glucosidase (AGL), gamma-glutamyltransferase (GGT) and ribonuclease (RNase), and serum amylase and immunoreactive trypsin (IRT) were determined in 38 control subjects, 48 patients with pancreatic cancer, 77 with chronic pancreatitis and 47 with extrapancreatic diseases in order to ascertain the presence of a renal tubular damage and to investigate its etiology. A significantly increased frequency of pathological results for all urinary enzymes was documented in the various groups of patients as compared to controls. Significant correlations were detected among AGL, GGT and RNase. Considering the subjects as a whole, GGT and RNase excretions correlated with serum IRT and amylase; the two urinary enzymes were found to be higher when jaundice was present. In chronic pancreatic disease enzymuria was related to increased serum pancreatic enzymes; in extrapancreatic diseases it was associated to hyperbilirubinemia. The vast majority of patients with pancreatic cancer and elevated urinary enzymes presented hepatic metastases and/or jaundice. We can conclude that an anatomical and functional tubular impairment is detectable in some patients with chronic pancreatic and extrapancreatic diseases. Tubular damage seems to least in part to be related to pancreatic inflammation and necrosis in chronic pancreatic disease, while jaundice may be found to play an important role in diseases of the hepatobiliary tract. In pancreatic cancer, liver dysfunction (presence of liver metastases and/or extrahepatic cholestasis) also appears to be involved in altering tubular cells.
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PMID:Renal tubular dysfunction in pancreatic cancer and chronic pancreatitis. 256 74

Enhancement of human NK cytotoxicity in the presence of fresh Viscum album extract and some commercial V. album extracts Iscador correlated strictly with an increased formation of lytic effector cell/K562 tumor cell conjugates in the single-cell assay. Both activities were completely destroyed by pretreatment of V. album extracts with pectinase, hemicellulase, amyloglucosidase and alpha-glucosidase, but not with proteases and RNase, i.e., the activities are linked to a polysaccharide. The active component in V. album extract was non-dialysable at a molecular weight cutoff of 10,000. Inhibition of both activities was observed with D-galacturonic acid, poly-galacturonic acid and pectins. The site of galacturonic acid-specific interaction could be identified on the effector cells. The rate of effector cell/tumor cell conjugate formation in the presence of V. album extracts, as well as the abrogation of both activities by pretreatment of V. album extracts with exoglycosidases specific for sugars other than galacturonic acid indicated an action of the NK cytotoxicity-enhancing component on the basis of a bridging mechanism. However, no conclusive results could be obtained for the structural specificity of the site interacting with the target cells.
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PMID:Biochemical characterization of a component in extracts of Viscum album enhancing human NK cytotoxicity. 270 32

Full-value diets of similar composition were given to male rats weighing 207-230 g, by intravenous (group 1) or intragastric (group 2) routes. The proportion of amino acids, fats and carbohydrates was 9.9:15.7:74.4 (with regard to their calorific value). The diet calorific value comprised 60.6 kcal/rat/day. An average mass increase in group 1 was 2.44 +/- 0.14 g/day, in group 2 - 1.75 +/- 0.11 g/day. The protein content and activities of alpha- and gamma-amylase, invertase, maltase, and glycil-L-leucine dipeptidase were assayed in the intestinal mucosa of the proximal portion of the small intestine in group 1 rats, while a decreased alpha-amylase activity in the distal portion of the small intestine was recorded in the animals of group 2. The mass of the pancreas in the rats of group 1 and 2 was authentically lower than in the control rats which received oral feeding with natural foods. The lowest mass of the pancreas was observed in the rats of group 1. Specific activity of trypsin, lipase and RNase in the pancreatic tissues of rats in groups 1 and 2 was similar. The results of the study have evidenced a lowered function of the digestive system under conditions of artificial feeding, especially in case of intravenous nutrition.
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PMID:[Digestive function of the small intestine and pancreas in rats on artificial feeding]. 309 Jul 82

Homogenates of Giardia lamblia trophozoites exhibited the following hydrolase activities: acid phosphatase (EC 3.1.3.2), proteinase (EC 3.1.4) with urea-denatured hemoglobin and N-benzoyl-DL-arginine-2-naphthylamide as substrates, deoxyribonuclease (EC 3.1.4.5), and ribonuclease (EC 2.7.7.16). beta-N-Acetylglucosaminidase (EC 3.2.1.30), beta-galactosidase (EC 3.2.1.23), beta-glucuronidase (EC 3.2.1.31), alpha-D-glucosidase (EC 3.2.1.20), beta-D-glucosidase (EC 3.2.1.21), and beta-D-xylosidase (EC 3.2.1.37) activities were below the level of detection. Differential and isopycnic centrifugation of homogenates demonstrated that giardial hydrolases were localized in a single-particle population sedimenting at 7200g for 30 min. The particles had a buoyant density in sucrose of 1.15 and exhibited latency. Latency was completely destroyed by Triton X-100 or 15 cycles of freezing and thawing. After centrifugation of Triton- or freeze-thaw-treated particle fractions, the hydrolase activities, though no longer latent, were still sedimentable suggesting tight binding to the organelle membrane. Latency was destroyed simultaneously for all hydrolases, in direct proportion to the amount of Triton added to a particle preparation or to the number of times a particle preparation was subjected to freezing and thawing. These results support the suggestion that the hydrolases of G. lamblia trophozoites are localized in a single-particle population of lysosome-like organelles.
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PMID:Giardia lamblia: localization of hydrolase activities in lysosome-like organelles of trophozoites. 327 50

In order to investigate the role of renal factors in affecting trypsinogen 1 metabolism and excretion in chronic pancreatic disease, serum immunoreactive trypsin (IRT), urinary IRT, gamma-glutamyltransferase (GGT), alpha-glucosidase (AGL) and RNase outputs and the molecular size distribution of serum and urine IRT were studied in 8 control subjects, 18 cases with pancreatic cancer, and 23 cases with chronic pancreatitis. Serum chromatography demonstrated that most immunoreactivity eluted as trypsinogen 1. Smaller amounts of immunoreactivity at higher molecular weights were also observed. Urine chromatography displayed both trypsinogen 1 and heavier molecular forms. An inverse linear correlation was noticed between creatinine clearance and serum trypsinogen 1 levels. Multiple regression analysis (urinary IRT output dependent and GGT, AGL, and RNase predictor variables) showed a significant linear correlation. RNase was found to be the most important parameter in explaining urinary IRT output. Mild variations in the glomerular function seem to be able to influence serum trypsinogen 1 levels. Urinary IRT excretion is principally explained by a disturbance in the tubular reabsorption of low molecular weight proteins, such as RNase.
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PMID:Renal factors in serum trypsinogen 1 metabolism and excretion in chronic pancreatic disease. 336 41

The ingestion of (14)C-labeled 9,10-dimethyl-1,2-benzanthracene particles, the extracellular release of acid phosphatase, ribonuclease, and alpha-glucosidase, and the egestion of preingested dimethylbenzanthracene particles by Tetrahymena taken from logarithmically growing cultures and resuspended in a dilute salt solution were followed in the presence of several pharmacologic agents. Serotonin, caffeine, and, to a lesser extent, dibutyryl cyclic AMP increased the rate of particle ingestion, but did not alter the rate of release of the three acid hydrolases studied. Added catecholamines did not affect either particle ingestion or acid hydrolase release, but particle ingestion was inhibited by the catecholamine antagonists, dichloroisoproterenol, desmethylimipramine, reserpine, and phenoxybenzamine. These drugs also increased the release of acid phosphatase and ribonuclease in 5-h incubations. Desmethylimipramine acted within 1 h to increase acid hydrolase release, but the effect of dichloroisoproterenol developed more slowly and was secondary to a change in cellular content of the hydrolases. Desmethylimipramine increased the energy of activation for the release of acid phosphatase, while dichloroisoproterenol did not. Both of these drugs enhanced the egestion of preingested dimethylbenzanthracene particles, supporting the view that acid hydrolase release occurs through a cytoproct egestion mechanism. Particle ingestion was also inhibited by colchicine, vinblastine, and cytochalasin B, but these agents had no effect on acid hydrolase release, thus further differentiating the properties of the ingestion mechanism from those of the egestion mechanism. It appears that both microtubules and microfilaments play a role in the ingestion process and that this process may be controlled in part by a cyclic AMP-mediated serotoninergic and adrenergic system.
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PMID:Lysosomal physiology in Tetrahymena. 3. Pharmacological studies on acid hydrolase release and the ingestion and egestion of dimethylbenzanthracene particles. 415 46

Axenic Tetrahymena pyriformis, syngen 1, mating type II cells were grown in Cox's defined medium. When washed and transferred into nonnutrient dilute salt solution or resuspended in the defined medium, the intact cells secrete acid hydrolases into the medium. Cells starving in the salt solution release in 5 hr about two-thirds of their beta-glucosidase, beta-N-acetylglucosaminidase, alpha-glucosidase, and amylase activities, about one-third of their deoxyribonuclease and phosphatase activities, smaller amounts of ribonuclease, and only a negligible fraction of their proteinase activity and protein content. During this period there is practically no change in the enzyme activities (except for a sudden increase of ribonuclease activity) and protein content of cells and medium together. Cells resuspended in the nutrient medium secrete enzymes as do the starved cells, but replace this loss, so that there is a continuous increase of the activities in the total system. According to isopycnic centrifugation experiments performed in sucrose gradients, the source of the hydrolases is a special population of lysosomes which disappear from the cells during starvation. This population equilibrates in the high density region of the gradients and contains the various acid hydrolases in about the proportion in which these enzymes appear in the medium.
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PMID:Secretion of acid hydrolases and its intracellular source in Tetrahymena pyriformis. 433 53

Log-phase Tetrahymena were washed and resuspended in a dilute salt solution supplemented with glucose, acetate, pyruvate, or carmine, as desired, and then incubated for 5 h. Intra- and extracellular activities of acid phosphatase, alpha-glucosidase, and ribonuclease were assayed. Extracellular activities were corrected for proteolytic degradation. The three nutritive substrates affected both the amount and pattern of extracellular enzyme release, but carmine had no effect. Intracellular activities declined early in the starvation period, but partially recovered with time, particularly alpha-glucosidase activity. Acetate reduced the decline in acid phosphatase activity; acetate and glucose enhanced the recovery of alpha-glucosidase activity; carmine had no effect on intracellular enzyme activities. Protein content changed little and was unaffected by the addition of substrates. Glycogen content increased during incubation; acetate and glucose enhanced the increase.
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PMID:Lysosomal physiology in Tetrahymena. I. Effect of glucose, acetate, pyruvate, and carmine on intracellular content and extracellular release of three acid hydrolases. 463 42

Preparations of isolated brush border plasma membrane of Hymenolepis diminuta and H. microstoma possess the following enzymatic activities: alkaline phosphohydrolase (E.C. 3.1.3.1); Type I phosphodiesterase (E.E. 3.1.4.1); ribonuclease (E.C. 3.1.4.22); adenosine triphosphatase (E.C. 3.6.1.3); and 5'-nucleotidase (E.C. 3.1.3.5). The following enzymatic activities could not be demonstrated in either membrane preparation: Type II phosphodiesterase (E.C. 3.1.4.18); cyclic adenosine-3', 5'-monophosphate phosphodiesterase (E.C. 3.1.4.17); leucine aminopeptidase (E.C. 3.4.11.1); maltase (alpha-glucosidase; E.C. 3.2.1.20); and lactase (beta-galactosidase; E.C. 3.2.1.23). These data generally agree with those of previous studies in which similar membrane-bound enzymes were demonstrated in intact (living) worms.
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PMID:A comparison of membrane-bound enzymes of the isolated brush border plasma membranes of the cestodes of Hymenolepis diminuta and H. microstoma. 628 Jan 22


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