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)

Recent studies have demonstrated that the human intestinal enzymes of carbohydrate digestion and metabolism can be regulated by dietary sugars. These studies have utilized direct assay of intestinal mucosal enzyme activity. Mucosa has been obtained by the use of peroral jejunal biopsy techniques which provide 10-15 mg of mucosa in a safe, simple and reproducible manner. Dietary sucrose, as compared to dietary glucose, increases the activities of the jejunal disaccharidases, sucrase and maltase, but not lactase. Fructose reproduces the sucrose effect and appears to be the active principle in the sucrose molecule. Lactose deprivation or lactose feeding does not alter lactase activity. Fructose has been useful in treating one patient with sucrase-isomaltase deficiency. Jejunal glycolytic enzyme activities are also regulated by dietary sugars. Certain enzymes are highest with specific dietary carbohydrates, lower with other sugars and lowest on a carbohydrate-free diet. The regulation of human jejunal glycolytic enzyme activity takes place in hours, whereas the change in disaccharidase activity occurs in 2-5 days. The mechanism of this regulation is not known. Additional investigations have shown that jejunal glycolytic enzyme activities but not the disaccharidases are controlled by oral folic acid as well. This effect occurs within 1 day also. The mechanism is unknown. Large doses of folate have been of benefit in a few patients with certain glycolytic enzyme deficiency states. Preliminary studies have demonstrated that selected patients with chronic undiagnosed intestinal disorders fail to manifest an adaptive response of their jejunal glycolytic enzyme activities to dietary sugars. This condition has been termed a "maladaptation syndrome.".
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PMID:Diet and intestinal enzyme adaptation: implications for gastrointestinal disorders. 16 4

Studies have been done on the effect of Penicillin, Streptomycin and Isonicotinic Acid hydrazide on small intestinal oligosaccharidase and it was observed that the drug penicillin inhibited the enzyme lactase and sucrase by 62.7% and 34.7% respectively, whereas I.N.H. inhibited the enzyme sucrase and maltase by 57.1% and 56.14% respectively. Streptomycin did not show any inhibitory effect on those enzymes. Lactose tolerance test showed impairment of lactose absorption in case of penicillin. Fasting serum sugar level was diminished both in penicillin and streptomycin and the absorption capacity was increased after oral administration of streptomycin.
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PMID:Studies on the effect of penicillin, streptomycin and isonicotinic acid hydrazide on small intestinal oligosaccharidase. 115 32

The localization of disaccharidases in kidney has been studied by means of the multiple indicator dilution technique. A pulse injection of a solution containing Evans blue dye (plasma marker), creatinine (extracellular marker), and a (14)C-labeled disaccharide (lactose, sucrose, maltose, and alphaalpha-trehalose), is made into the renal artery of an anesthetized dog, and the outflow curves are monitored simultaneously from renal venous and urine effluents. Lactose and sucrose have an extracellular distribution. Trehalose and maltose remain extracellular from the postglomerular circulation. About 75% of filtered tracer maltose or trehalose is extracted by the luminal surface of the nephron. Thin-layer chromatography of urine samples shows that all of the excreted (14)C radiolabel is in the form of the injected disaccharide. Following the administration of phlorizin, all of the filtered radioactivity is recoverable in the urine, but chromatography of the urine samples now reveals that there is a significant excretion of [(14)C]glucose, approximating the amount previously extracted under control conditions (in the absence of phlorizin). It has been verified that no hydrolysis of maltose or trehalose to their constituent glucose subunits occurred during the transit of tracer between the point of injection (renal artery), and the point of filtration (glomerular basement membrane). Similarly, after addition of [(14)C]disaccharides to fresh urine there is no chromatographically recoverable [(14)C]glucose. It is concluded that there exist alpha-glucosidases with maltase and trehalase activity along the brush border of the proximal tubule and that these disaccharidases are located spatially superficial to the glucose transport receptors.
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PMID:Brush border disaccharidases in dog kidney and their spatial relationship to glucose transport receptors. 472 44

Newborn rats born to iron deficient mothers (IDM) were found to have significantly lower hemoglobin, sucrase, lactase and maltase levels compared to control newborn rats. Rats born to IDM and nursed by IDM, when sacrificed at 21 days of age, had statistically significantly lower hemoglobin, serum iron, sucrase, lactase and maltase levels compared to control rats. Rats born to IDM, but nursed by iron sufficient mothers (ISM) and sacrificed at 21 days of age, had hemoglobin, serum iron and sucrase levels compared to control rats whereas lactase and maltase were not corrected by 21 days of nursing by ISM. Rats burn to IDM and nursed by either IDM or ISM for 21 days were given intramuscular iron dextran and placed on iron sufficient diet (ISD) for 7 days. These animals experienced correction of the hemoglobin, serum iron, sucrase and maltase levels compared to control rats, whereas intestinal lactase was not corrected by 7 days of ISD and intramuscular iron. Rats born to ISM, nursed by IDM and sacrificed on day 21 had significantly lower hemoglobin, serum iron and intestinal lactase levels compared to control rats. Rats both to ISM and nursed by IDM were given intramuscular iron dextran on day 21 and placed on an ISD from day 21-28. These animals had a return in hemoglobin, serum iron, sucrase and maltase levels comparable to control rats. Rats born to and nursed by ISM and maintained on an iron deficient diet from day 21-84 had significantly lower hemoglobin, serum iron, sucrase, lactase and maltase levels compared to control rats. Rats born to and nursed by ISM, maintained on iron deficient diet from day 21-84, and then given intramuscular iron dextran on day 84 and maintained on an ISD until day 92, experienced correction of the hemoglobin, serum iron and lactase levels compared to control rats. Intramuscular iron and 7 days of ISD did not correct the sucrase and maltase levels in these rats. Lactose tolerance tests in iron deficient rats showed flat curves compared to controls. After iron treatment, lactose tolerance curves returned to control values. Iron deficiency in rats in utero, during the nursing and postweaning period causes, in addition to anemia, a reduction in jejunal disaccharidase activity because of an alteration in the enzymes of the brush border membrane. Varying degrees of reduction and response of certain disaccharidases to iron treatment are dependent on the time of iron deprivation in relationship to the intra-uterine and postnatal development of the digestive and absorptive functions in the small intestine. Alterations in the levels of disaccharidases demonstrated in this paper represents another aspect of the spectrum of biochemical effects of iron deficiency.
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PMID:Disaccharidase levels in iron deficient rats at birth and during the nursing and postweaning periods: response to iron treatment. 707 2