Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound   Target Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound

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Query: EC:3.2.1.20 (alpha-glucosidase)
4,237 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Feeding sodium deoxycholate orally to rats for four days caused depression of the activity of the small intestinal enzymes lactase, sucrase, maltase, alkaline phosphatase, and N-acetyl-beta-glucosaminidase. The first four are brush border enzymes, the last a lysosomal enzyme. Alkaline phosphatase activity recovered very rapidly and rebounded to above the normal level within 24 hours. The activity of the three disaccharidases returned to normal within seven days while no recovery was observed within 96 hours of the activity of the lysosomal enzyme, N-acetyl-beta-glucosaminidase, after removing the bile salt from the diet.
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PMID:Deoxycholate depresses small-intestinal enzyme activity. 114 Jun 27

1. Intestinal brush border enzymes have heterogeneous rates of turnover, the largest proteins having the fastest turnover. Since the membrane faces the intestinal lumen, the effects of pancreatic factors were examined in mediating this turnover. Surgical subtotal pancreatectomy was used as an experimental model to study the turnover of brush border proteins in the absence of most pancreatic secretions. 2. Subtotal (95%) pancreatectomy of rats was found to cause elevations by about 50% of total activity and specific activities of certain brush border enzymes (maltase, sucrase, lactase), but not of others (alkaline phosphatase, trehalase). Rats were judged to be functionally deficient in pancreatic proteolytic enzymes (a) by demonstration of vitamin B-12 malabsorption, which was corrected by trypsin, and (b) by the finding of only about 20% of proteolytic activity appearing in the lumen after a test meal when compared to control. 3. To measure protein turnover in vivo the method of double labelling was used, where [3H]- and [14C]valine were administered intraduodenally in sequence 10 h apart. With this technique, a high 3H/14C ratio is correlated with rapid turnover. Proteins with apparent molecular weights of about 200 000-270 000 were found to turn over more rapidly than smaller proteins. 3H/14C ranged from 4.7 to 6.2 in animals without pancreatic insufficiency. In the face of decreased pancreatic proteolysis, the 3H/14C ratio was 2.3-3.1, similar to that of proteins with a slow half life. 4. Estimates of relative synthetic rates of large brush border proteins were lower than normal in pancreatectomized animals, but were constant over the period of the labelling experiment. The high enzyme levels in the face of lower synthetic rates confirms that, at the new steady rate, degradation rates must be slower for large brush border proteins in pancreatic insufficiency. 5. In vitro, using purified brush borders, unfractionated pancreatic enzymes were found to remove sucrase, maltase and lactase, but not alkaline phosphatase and trehalase. The enzyme most potent in this respect was the pancreatic protease, elastase. Non-proteolytic enzymes (amylase, lipase, phospholipase A) were inactive in removing enzyme from the brush border. The addition of elastase to pancreatectomized animals in vivo restored the rapid turnover rate of large brush border proteins. 6. A model is thus proposed for the normal catabolism of some large intestinal brush border proteins. It is suggested that the surface of intestinal absorptive cells is being constantly remodelled, and that certain surface enzymes are in part removed from the membrane by the action of pancreatic proteases. A possible special role for elastase is suggested.
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PMID:The possible role of pancreatic proteases in the turnover of intestinal brush border proteins. 114 88

Jejunal biopsies from 19 adult Greenland Eskimos were studied regarding disaccharidases, two intracellular beta-galactosidases, and morphological appearance. Fifteen of the patients (79%) had low lactase activity, and 3 of these (16%) had sucrase-isomaltase deficiency as well. Two patients had low trehalase activity. Microscopical appearance was essentially normal in all the biopsies, except for a certain stromal plasma cell infiltration. All the patients with low lactase activity had a measurable residual activity of brush border lactase, which was localized in the middle and apical parts of villi, as normally seen for digestive enzymes. Lysosomal acid beta-galactosidase and cytosol hetero beta-galactosidase were not altered. In the patients with sucrase-isomaltase deficiency there was a complete absence of active sucrase-isomaltase complex. The residual maltase, as well as the very weak residual isomaltase, was exerted exclusively by the heat stable maltases (maltase II and III). The material is the first one in which multiple, but not generalized disaccharidase deficiencies are demonstrated.
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PMID:Intestinal disaccharidases in Greenland Eskimos. 115 47

Maltase, sucrase, and lactase were measured at pH 4 and pH 6 in normal and intestinalized gastric mucosa. In the normal mucosa the low activities of maltase and lactase seemed to be entirely due to lysosomal enzymes with acid pH-optimum. In intestinal metaplasia, brush border maltase and sucrase, but not lactase, appeared. On the other hand, there was a significant increase in lysosomal lactase (beta-galactosidase) activity.
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PMID:Disaccharidase activities in intestinal metaplasia - contribution of lysosomal brush border enzymes. 117 60

The effect of diets containing various amounts of casein and starch on enzymes bound to the brush border of the small intestine and kidney of rats were investigated with the following results. 1) Diets with low starch and high casein contents resulted in higher specific activity of leucineaminopeptidase in the small intestine than diets with high starch and low casein contents. Diets with high starch and low casein contents increased the specific activity of maltase. 2) Rat small intestine contains at least two isoenzymes of leucineaminopeptidase: one bound to the brush border and the other not bound to it but recoverable in the soluble fraction. Only the former was influenced by the diet. 3) The maximum velocity (Vmax) of leucineaminopeptidase bound to the brush border was twice as much in rats on a high casein diet as in those on a low casein diet, but the Michaelis constant (Km) was approximately the same in both groups of rats. 4) Leucineaminopeptidase and maltase activities in the kidney were not influenced by diet.
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PMID:Effect of diet on enzymes of the brush border of the small intestine and kidney of rats. 120 41

The releases of proteins, maltase, lactase, sucrase, trehalase, alkaline phosphatase, gamma-glutamyltransferase and leucylnaphthylamide-hydrolyzing activity from human intestinal brush bborder membrane vesicles by various enzymes (especially pancreatic proteases) have been studied. The brush border membrane enzymes are not solubilized by digestion with trypsin and chymotrypsin but are largely released after treatment with papain or elastase. Most of the enzymes are fully active after the proteolytic treatment. All proteins released by papain and elastase have been identified by electrophoresis to already known intestinal hydrolases. Electron microscopy of brush border membrane vesicles demonstrates "knob-like" structures (particles) attached to the external side of the membrane. During papain treatment, enzyme removal runs parallel with the disappearance of the particles. During elastase treatment it is not possible to correlate the release of the enzymic activities with the removal of the particles. The results indicate that most of the intestinal hydrolases are surface components attached to the external side of the membrane. They are in accord with the concept that the brush border membrane enzymes are organized within the membrane in a mosaic-like pattern.
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PMID:Enzymic solubilization of the human intestinal brush border membrane enzymes. 127 90

Renal epithelial function, proton flux and sodium stimulated proton flux, was observed in vesicles isolated from the brush border of the proximal tubule of Sockeye Salmon (Oncorhynchus nerka) during migration. Brush border membrane vesicles (BBMV) were isolated from the body kidney of Sockeye Salmon using aggregation/differential centrifugation techniques. Vesicle purity was tested using a series of epithelial and basal lateral markers including alkaline phosphatase, maltase, gamma-glutamyl transferase (GGTP), Mg(2+)-activated ATP-ase, Na(+)+K(+)-activated ATPase, and 5'-nucleotidase and the lysosomal marker acid phosphatase. An enrichment/depletion factor for each marker was determined by comparison of purified BBMV with kidney homogenate. Vesicles exhibit an enrichment factor for alkaline phosphatase, GGTP, maltase, Mg(2+)-activated ATP-ase, Na(+)+K(+)-activated ATPase, and 5'-nucleotidase. A depletion factor was observed for acid phosphatase. Vesicle integrity was tested by measuring the time course of proton flux in the presence of a pH gradient. Amiloride sensitive sodium stimulated proton flux was observed in these vesicles. The presence of sodium caused a saturable increase in the rate of proton flux, indicating the activity of a sodium/proton antiport protein in BBMV.
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PMID:Proton transport and Na+/H+ exchange in vesicles isolated from sockeye salmon (Oncorhynchus nerka) kidneys during migration from salt to fresh water. 132 4

Administration of hydrocortisone increased the sucrase and amylolytic activities in the brush border of the enterocytes along the intestinal villus and decreased the maltase activity in fed chicken. Hydrocortisone does not affect the level of maltase activity in food-deprived chicks.
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PMID:[The effect of hydrocortisone on carbohydrase activity along the intestinal villus in chicks]. 133 10

The brush border of normal small-intestine epithelial cells is rich in enzymes that are involved in the digestive process. Such molecules can be used as markers to analyze cell lineages and differentiation properties of colorectal cancers. Monoclonal antibodies detecting dipeptidyl peptidase-IV, aminopeptidase N, endopeptidase F, sucrase-isomaltase, alkaline phosphatase, maltase-glucoamylase and lactase have been used to analyze the phenotype of colorectal cancers, adjacent mucosa and histologically normal distant mucosa. The avidin-biotin peroxidase complex method was used. Expression of dipeptidyl peptidase-IV, aminopeptidase N, sucrase-isomaltase and alkaline phosphatase was common in non-neoplastic mucosa adjacent to, and distant from, the tumor; in contrast, endopeptidase F, maltase-glucoamylase and lactase were rarely expressed in normal distant mucosa and more frequently expressed in mucosa adjacent to the tumor. Dipeptidyl peptidase-IV, aminopeptidase N, endopeptidase F, sucrase-isomaltase and alkaline phosphatase were frequently expressed in colorectal cancers, whereas maltase-glucoamylase and lactase were rarely expressed. Two general patterns of antibody reactivity were observed: diffuse cytoplasmic and apical; apical reactivity was generally associated with more differentiated tumors. A logistic predictive regression model indicated that enzyme expression in colorectal cancers followed a coordinate pattern, but was unrelated to the location of the tumor, Dukes stage or differentiation grade. In conclusion, expression of brush-border-associated enzymes occurs frequently in colorectal cancers and is regulated in a co-ordinated manner. These markers can be used for the phenotypic sub-classification of colorectal cancers.
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PMID:Intestinal brush-border-associated enzymes: co-ordinated expression in colorectal cancer. 134 6

Expression of brush border hydrolases can reflect the state of differentiation of an epithelium. To determine if expression of these enzymes is disordered in patients with neoplastic or hyperplastic lesions, the activities of alkaline phosphatase, maltase, and dipeptidyl peptidase IV were measured spectrophotometrically in colonoscopic biopsies from the proximal and distal colon and rectum in 50 controls, 17 patients with large bowel adenomas, 29 with carcinoma, and 9 with hyperplastic polyps. In normal controls, a descending cecorectal gradient of alkaline phosphatase activities and an ascending gradient of maltase activities were seen (P < 0.001). Though regional patterns of expression were generally preserved in disease groups, there were significant differences of activities across patient groups for alkaline phosphatase (greater in cancer, adenoma, and hyperplastic groups than in normals; P < 0.05) and for dipeptidyl peptidase IV (greater in hyperplastic polyp group than normals, greater in adenoma than cancer group; P < 0.05). Compared with normal controls, abnormalities of site-specific activities were confined to the rectum in patients with adenoma (maltase decreased, P = 0.02; dipeptidyl peptidase IV increased, P < 0.01) or with carcinoma (alkaline phosphatase increased, P = 0.03) but dipeptidyl peptidase IV activities were increased in all regions in bowels bearing hyperplastic polyps (P < 0.01). These data suggest that neoplastic and hyperplastic lesions, while focal in nature, occur in large bowel epithelium, which is diffusely abnormal in terms of its expression of these enzymes.
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PMID:Neoplasia and hyperplasia of large bowel: focal lesions in an abnormal epithelium. 135 42


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