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:3.2.1.26 (invertase)
4,927 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Intestinal adaptation was studied in six patients with massive obesity treated by jejuno-ileal bypass operation. Glucose absorption in the jejunum was measured by a perfusion technique. The morphometric and enzymatic measurements were carried out on biopsies from the proximal jejunum and the distal ileum. Results obtained before and six months after the operation were compared. The glucose absorption per unit length of jejunum was unchanged at a glucose concentration of 66 mmol/l in the perfusate but increased significantly at a glucose concentration of 133 mmol/l (p less 0.025). The mean sucrase activity did not change, whereas the lactase activity increased significantly in the jejunum and ileum. The mean villus height increased significantly, while the epithelial cell height and cell width were unchanged both in the jejunum and the ileum, suggesting that the operation resulted in epithelial cell hyperplasia. The glucose absorption in the jejunum was positively correlated with the villus height (r = 0.76), which suggests that the increased glucose absorption was related to an increased number of epithelial cells.
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PMID:Intestinal adaptation after jejuno-ileal bypass operation for massive obesity. 97 97

Intestinal sucrose hydrolysis and absorption of monosaccharide products was studied in vivo utilizing the segmental perfusion technique in diabetic and control rats. The proximal jejunum was perfused with 20 mM sucrose, 140 mM NaCl and 0.5% PEG with 14C-PEG, as the nonabsorbable marker. Rates of sucrose hydrolysis and adsorption of monosaccharide products (fructose, and glucose) were determined. There were no statistically significant differences between the diabetic and control rats. This indicates that the previously reported increase in sucrase activity in diabetes does not correlate with enhanced rates of sucrose hydrolysis. Several possibilities for the interpretation of these results are discussed.
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PMID:Intestinal digestion and absorption of sucrose in experimental diabetes. 102 Jun 13

Infants and young children are particularly susceptible to a recently identified viral enteritis which is highly contagious and seems both common and universal. In this disease, virus invades the upper intestinal epithelium, causing acute diarrhoea with early fever and vomiting. We studied a similar disease in pigs, infecting three-week-old animals with transmissible gastroenteritis virus (TGE), which also invades the upper intestinal epithelium. In this model, diarrhoea is massive 16-40 hours after infection, when stools contain increased electrolytes but no excess of sugar. In the jejunum of intact pigs at the 40-hour stage we found altered Na+ and water flux, decreased mucosal activities of disaccharidases and Na+, K+-ATPase, but normal adenylate cyclase activity. At the same stage the response of Na+ flux to glucose was blunted in jejunal epithelium studied in Ussing short-circuit chambers and in suspensions of villous cells; Cl- flux responded normally to theophylline, and thymidine kinase and sucrase activities of cells isolated from jejunal villi were similar to those found in crypt cells. Probably by 40 hours after infection most virus has been shed from the mucosa. Viral diarrhoea clearly differs from enterotoxigenic diarrhoea. Consideration of its pathogenesis must take into account the dynamic nature of the mucosal epithelium and the factors governing differentiation of enterocytes as they migrate from crypt to villus. Sufficient information is available now to characterize one specific and apparently prevalent viral enteritis in man and to identify additional viral enteritides. There is hope that preventative therapy can be developed. Our understanding of the mechanisms of viral diarrhoea is limited, but the availability of an animal model and the promise of others makes us optimistic that these deficiencies can be remedied. Greater understanding of the pathogenesis of viral diarrhoea should better the active therapy of affected infants and children.
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PMID:Viral gastroenteritis: recent progress, remaining problems. 104 55

Digestive enzymatic activities (disaccharidases, alkaline phosphatase, peptide hydrolases) have been determined in the mucosa of 14 patients with chronic pancreatitis. All had an abnormal secretin-pancreozymin test. Four patients had insulin-dependent diabetes mellitus, four a pathological glucose tolerance test. Nine patients had steatorrhoea. Maltase, sucrase, and alkaline phosphatase activity was significantly elevated in patients with exocrine pancreatic insufficiency, whereas those of lactase, trehalase, and peptide hydrolase were normal. Patients with steatorrhoea had higher maltase and sucrase activity than those without steatorrhoea, whereas decreased glucose tolerance had no effect on brush border enzymatic activity. It is suggested thatdecreased exocrine rather than decreased endocrine pancreatic function is responsible for the increase in intestinal disaccharidase and alkaline phosphatase activity, possible by the influence of pacreatic enzymes on the turnover of brush border enzymes from the luminal side of the mucosal membranes or by direct hormonal stimulation though cholecystokinin.
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PMID:Influence of exocrine and endocrine pancreatic function on intestinal brush border enaymatic activities. 109 2

The mechanism of inhibition by 2-deoxy-D-glucose of the synthesis of yeast wall polysaccharides and glycoproteins was investigated in Saccharomyces cerevisiae cells and protoplasts. The extent of the inhibition of mannan and glucan synthesis was found to be dependent on whether glucose or mannose was used as the carbon source in the medium. During growth on glucose, 2-deoxy-D-glucose inhibited more intensively mannan than glucan formation. Biosynthesis of wall glucan was strongly suppressed in mannose medium. Selective incorporation of 2-deoxy-D-glucose occurred into that polysaccharide, synthesis of which was more inhibited under given conditions. Suggestive evidence has been obtained that the decisive factor for the proportion of glucan and mannan in the walls is the direction of glucose 6-phosphate/mannose 6-phosphate interconversion dependent on the exogeneous hexose. No close correlation was found between the inhibition of mannan synthesis and the appearance of the mannan-protein enzymes invertase and acid phosphatase. Effect of 2-deoxy-D-glucose was therefore investigated on the parallel synthesis of protein, mannan and several extracellular and intracellular enzymes in protoplasts grown on glucose and mannose. The results obtained pointed out that the hindrance of the secretion of mannan-protein enzymes is of a complex nature and related more to the inhibition of synthesis of the protein moiety than to the inhibition of glycosylation. Synthesis of several enzymes was found to be a subject of a metabolic control by 2-deoxy-D-glucose or its metabolites.
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PMID:Mechanism of 2-deoxy-D-glucose inhibition of cell-wall polysaccharide and glycoprotein biosyntheses in Saccharomyces cerevisiae. 110 Mar 78

In the course of work concerned with the inhibition of small intestinal carbohydrate digesting enzymes, experiments were performed on rats and two healthy volunteers using tris as a sucrase inhibitor. The following results were obtained: (1) Tris does not lower the blood glucose in fasting rats after oral or subcutaneous doses up to 500 mg/kg, when administered as neutral solution (pH 7.0). (2) Tris reduces reduces the glycemia in rats and human subjects after a sucrose load. In addition, the insulinemia caused by administration of sucrose is reduced in man. This smoothing effect on both curves is dose-dependent. A delay of gastric emptying by tris could be excluded. (3) After a glucose or matose load in rats, tris has no effect on the blood sugar curve. (4) The marked smoothing effect of tris is after sucrose loading is probably caused by its well-known in vitro inhibitory effect on intestinal sucrase activity of pigs and humans.
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PMID:Inhibition of sucrase by tris in rat and man, demonstrated by oral loading tests with sucrose. 111 Jun 27

The molecular forms of yeast invertase have been studied. It is shown that by gel filtration on Sephadex G-200 it is possible to demonstrate the presence not only of a light, carbohydrate-free, invertase, and a heavy invertase containing 50% carbohydrate, but also of a continuous spectrum of molecular forms that probably represent the sequential addition of mannose to the light form during the secretion process, which culminates in the formation on the heavy enzyme that is found outside the cytoplasmic membrane. The elution volume-void volume ratio in Sephadex G-200 varies from 1.75 of the light to 1.05 of the heavy invertase. The separation of invertase has also been achieved by ion-exchange chromatography and by isoelectric focusing and is facilitated by removal of the heavy form by ammonium sulphate precipitation. During the protoplasting process the removal of the cell wall is accompanied by the loss of most of the heavy form. Thintermediate forms are exclusively detected inside the protoplast, together with the light invertase and a small amount of heavy invertase. The effect of 2-deoxy-D-glucose and cycloheximide on the biosynthesis and distribution of molecular forms of yeast invertase has also been studied. In the presence of 10 mM glucose Saccharomyces 303-67 repressed cells readily synthesize invertase during the two-hour incubation period. Upon the addition of 2-deoxy-D-glucose, at a concentration of 75 mu g/ml, the observed inhibition in the cells is 60%, but if the activity is measured after breaking the cells, only a 31% inhibition is found, revealing an accumulation of invertase inside the protoplast. 2-Deoxy-D-glucose originates a pile-up of the light and intermediate forms at the expense of the formation of the heavy enzyme, showing that the inhibition of the glycosilation and, therefore, the secretion process, has taken place. In the absence of de novo invertase synthesis originated by cycloheximide, the glycosilation process still takes place as indicated by the accumulation of the heavy form at the expense of the light, carbohydrate-free, enzyme.
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PMID:Molecular forms of yeast invertase. 111 70

Among 135 infants and children with a supposed malabsorption syndrome, a deficiency of isomaltase-saccharase of the duodenal mucosa was detected in 5 cases by measuring the disaccharidases directly in the mucosa homogenate. In one instance a deficiency of lactase was found in addition. In all patients the villi were of normal length, with an increased cell infiltration of the stroma detected in two cases. The loading tests with xylose-sucrose yielded a diminuished rise in the blood glucose level. Three of the patients were dwarfish, but only one showed an increased growth after the reduction of sucrose in the supplied diet. As a result of adaptation difficulties in the change of diet, one patient had to be treated with an additional saccharase substitution.
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PMID:[Hereditary deficiency of isomaltase and saccharase responsible for a malabsorption syndrone (author's transl)]. 116 88

The acute effects of intraduodenal administration of ethanol, 5 g/kg body weight, on intestinal activities of lipid-reesterifying and disaccharidase enzymes of the small bowel were studied. Results were compared to those produced in controls receiving isocaloric amounts of glucose by the same route. Acyl-CoA:monoglyceride acyltransferase, acyl-CoA synthetase (acid:CoA ligase (AMP) EC 6.2.1.3), sucrase, and lactase assays were performed on jejunal samples; acyl-CoA synthetase assay was performed on ileal samples. Ethanol produced greater activities of the lipid-reesterifying enzymes in the jejunum than did glucose. Ileal specific activity of acyl-CoA synthetase was also increased in the experimental group. No effect of ethanol on jejunal disaccharidase enzyme activities was noted. It is concluded that ethanol given acutely has a specific stimulating effect on intestinal enzymes involved in lipid absorption.
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PMID:The effect of acute ethanol treatment on lipid-reesterifying enzymes of the rat small bowel. 116 87

Small intestinal lactase activity in the health adult is either the same as in early infancy or may drop to very low levels. The behavior of the enzymatic state varies with the ethnic group studied. In those adults with low lactase activity little information is availalbe as to the age at which the lactase decreases. We attempted to determine a) the frequency of low intestinal lactase activity and b) the age at which the change occurs. For this purpose we reviewed in a large number of intestinal biopsies both histologically as well as for disaccharidase activities. The biopsies were obtained from a heterogeneous group of Caucasians, including patients, their siblings and parents. The patients were those with failure to thrive in whom no organic cause could be elicited, and those with the irritable colon syndrome. Patients ranged in age from 6 weeks to 50 years and out of a total of 1, 077 jejunal biopsies, 172 morphologically normal biopsies were selected. The milk drinking habits of 118 subjects and their families were elicited and 31 oral lactose tolerance tests performed. The mucosal lactase activity and sucrase-to-lactase ratio in those 172 individuals were plotted against age. In the first 3 years the mean lactase activity was 32.1 plus or minus 10.1 mumoles/g protein per min and the sucrase-to-lactase ratio was 1.7 plus or minus 0.5 with no change from year to year. However, after age 5 two separate groups emerge. A small group (24.6% of the population) with low lactase activity, and a second group possessing the same mean value for lactase activity as noted in the first 3 years. The low lactase activity group included children and adults with clinical lactose intolerance. These individuals consumed relatively small amounts of milk and when 12 of them were tested with an oral lactose tolerance test the result was a "flat" curve with a maximum rise in blood glucose of 9 plus or minus 3.2 mg/100 ml. The second group consumed more milk averaging 1 quart/day with no discomfort and when 19 were tested with oral lactose tolerance tests the values were normal. This study indicates that low lactase activity in the Caucasian population may make its appearance at the age of 5 years.
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PMID:Correlation of lactase activity, lactose tolerance and milk consumption in different age groups. 117 20


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