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)

alpha-glucosidases are cellular enzymes, able to split the polysaccharides into glucose. In subcellular fractions from rat and trout hepatocytes, the distribution patterns of neutral alpha-glucosidase and of glucose-6-phosphatase appear to be very similar, i.e., closely linked to the endoplasmic reticulum, and are somewhat related to the particular glycogen. The data suggest a probable role of neutral alpha-glucosidase in cell physiology and in carbohydrates metabolism.
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PMID:[Similar distribution of the activities of neutral alpha-glucosidase (gamma-amylase) and glucose-6-phosphatase in subcellular fractions from rat and trout livers]. 3 99

Tissues from the cerebral cortex, liver and myocardium of a patient with Lafora disease were obtained at autopsy and were studied biochemically. 1. Glucose content in the myocardium and liver was almost nil while that in the controls was 0.66 mg/g wet weight in the former and 8.80 mg/g wet weight in the latter. Glycogen content in the cerebral cortex and myocardium was about 10 and 3 times more than in controls. 2. Polyglucosan extracted from the cerebral cortex, liver and myocardium had a longer exterior glucose chain than that in the liver of the control but a normal, alpha or beta 1,4-glucosidic linkage was observed. 3. The activities of glucose-6-phosphatase and amylo-1,6-glucosidase in the cerebral cortex, liver and myocardium were well preserved. The activities of acid maltase in the three organs mentioned above and of neutral maltase in the myocardium were elevated twice and one and half times more than the control. Phosphorylase levels in the myocardium were extremely small, while in the cerebral cortex and liver normal activities were observed. In light of these findings, glycogen metabolism in Lafora disease is discussed.
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PMID:Biochemical studies on tissues from a patient with Lafora disease. 17 19

Oral administration of embelin (75 mg/kg per day, daily for 15 and 30 days) to male rats caused significant elevation in the uptake of D-glucose, L-alanine, L-leucine and calcium in small intestinal segments. Embelin also produced significant increases in intestinal brush border membrane-associated enzymes (sucrase, lactase, maltase, alkaline phosphatase and leucine aminopeptidase) in both intestinal homogenates and partially purified brush border membrane preparations. Significant increases were also noted for microsomal glucose-6-phosphatase and cytosolic lactate dehydrogenase. Increase in brush border membrane-associated total lipids, phospholipids, cholesterol, triacylglycerol, unesterified fatty acids and ganglioside sialic acid were seen but not in the cholesterol/phospholipid molar ratio. All these changes returned to control or near control levels following withdrawal of the drug.
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PMID:Effects of embelin, a male antifertility agent, on absorptive and digestive functions of rat intestine. 192 15

Administration of Embelin, an experimental antifertility agent, to male rats (20 mg/kg body wt/day, daily for 15 and 30 days), caused an elevation in the uptake of D-glucose, L-alanine, L-leucine, and calcium in the small intestinal segments. An increase was also noted in the intestinal brush border membrane (BBM)-associated enzymes, sucrase, lactase, maltase, alkaline phosphatase, and leucine aminopeptidase in both the intestinal homogenates and partially purified BBM preparations, particularly after 30-day administration of the drug. Embelin treatment also caused a significant increase in the microsomal glucose-6-phosphatase and the cytosolic enzyme, lactate dehydrogenase. In the Embelin-treated animals BBM-associated total lipids, phospholipids, cholesterol, triacylglycerol, unesterified fatty acids, ganglioside-sialic acids as well as the cholesterol/phospholipids molar ratio showed a considerable increase. All these changes in the Embelin-treated animals were restored back to the normal or near normal biochemical makeup when the drug therapy was withdrawn and the animals were allowed to recover for another 15 and 30 days, respectively.
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PMID:Changes in glucose/amino acid/calcium uptake and brush-border membrane-associated enzymes in rat small intestine after the administration of embelin (plant benzoquinone), an antifertility agent. 211 47

The effect of eight doses of 10,000, 20,000 and 30,000 UI of vitamin D2 administered every other day to three groups of rats, on the activities of some enzymes in the animals' liver was evaluated. In general terms, findings revealed a decrease in the activities of glucose-6-phosphatase, phosphorylase and arginase. Likewise, an increase of the activities of maltase and of glutamic oxaloacetic and glutamic pyruvic transaminases was observed. Furthermore, the activities of cholinesterase and alpha-amylase also varied depending on the vitamin D2 doses administered.
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PMID:[Effect of hypervitaminosis D on the activity of various enzymes in the rat liver]. 282 Mar 34

Long-term dietary administration of the adrenal hormone dehydroepiandrosterone (DHEA) to male Sprague-Dawley rats induced significant alterations in the activities of enzymes involved in liver carbohydrate metabolism. Although glycogen synthase activity was increased and phosphorylase decreased, glycogen stores were reduced. This was presumably related to lysosomal glycogen degradation, since alpha-glucosidase was increased. All rate-limiting enzymes of glucose metabolism which were studied (glucose-6-phosphate dehydrogenase, total hexokinases, pyruvate kinase, fructose-1,6-bisphosphatase) revealed markedly reduced activity, only glucose-6-phosphatase activity was increased. These enzymatic changes point to a far-reaching metabolic shift towards energy loss via decreased glucose consumption and increased glucose output. The enzyme pattern induced by DHEA is in many respects opposite to that induced in preneoplastic and neoplastic liver lesions by chemical hepatocarcinogens.
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PMID:Dehydroepiandrosterone induced alterations in rat liver carbohydrate metabolism. 284 96

Post-mortem brain samples from patients with either Huntington's disease, Alzheimer-type dementia or appropriate controls were assayed for endoplasmic reticulum enzymes, NADPH-cytochrome c reductase, neutral alpha-glucosidase, inosine diphosphatase, alpha-mannosidase and glucose-6-phosphatase and for Golgi enzymes, fucosyl- and galactosyl-transferases. In Alzheimer-type dementia there was a selective decrease in alpha-glucosidase activity in the temporal cortex. In Huntington's disease there was a selective decrease of putamen alpha-glucosidase and fucosyl-transferase activities. It is suggested that these changes reflect highly specific alterations in glycoprotein synthesis and processing and may contribute to the underlying pathology of these disorders.
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PMID:Loss of endoplasmic reticulum-associated enzymes in affected brain regions in Huntington's disease and Alzheimer-type dementia. 293 94

Glycogen content and six major enzymatic activities involved in glycogen metabolism were analysed in chorionic villi (CV). Glycogen levels were found to be lower than those known to exist in liver and muscle. Activities of alpha-glucosidase, amylo-1,6-glucosidase, phosphorylase b and phosphorylase kinase were detectable by standard methods. The enzymatic activities of glucose-6-phosphatase and phosphorylase a were undetectable. These findings suggest that CV biopsies can be useful for first-trimester diagnosis of glycogen storage disease types II, III and VI, but not for type I (glucose-6-phosphatase deficiency).
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PMID:Enzymatic activity of glycogen metabolism in chorionic villi. 302 29

The intestinal microvilli of fetal origin in human amniotic fluid were purified by Ca2+ precipitation of contaminating organelles followed by differential centrifugation of microvillar membranes. In the purified preparation, the specific activity of the microvillar marker-enzymes maltase and sucrase increased about 77-fold over that in cell-free amniotic fluid. Significant contamination of the purified preparation by endoplasmic reticulum (microsomes) and lysosomes was ruled out on the basis of a low content of the marker enzymes glucose-6-phosphatase (microsomes) and acid phosphatase (lysosomes). Amniotic fluid microvilli contain typical enzymes of the fetal intestine including maltase, sucrase, trehalase, alkaline phosphatase and gamma-glutamyltransferase, and their morphology by electron microscopy resembles that of vesiculated intestinal microvilli. Prenatal detection of genetic diseases due to a deficiency of a protein expressed in these membranes or associated to abnormal microvilli seems feasible.
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PMID:Fetal intestinal microvilli in human amniotic fluid. 302 83

The effect of vitamin C deficiency on various enzymes of the intestinal epithelium has been studied in guinea pigs. Brush border sucrase and alkaline phosphatase activities were considerably enhanced (p less than 0.001), but leucine aminopeptidase levels were reduced in scorbutic animals compared to the control group. There was essentially no change in the activity of maltase under these conditions. Kinetic studies with sucrase and alkaline phosphatase in control and scorbutic animals revealed that augmentation of the enzyme activities in scurvy is due to enhanced enzyme contents. Lactate dehydrogenase, succinate dehydrogenase, glucose-6-phosphatase and Mg+2 ATPase also exhibited reduced activities in the intestine of vitamin-C-deficient animals. Observed alterations in the activities of intestinal enzymes in scurvy were restored to control levels upon feeding of vitamin C to scorbutic guinea pigs.
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PMID:Alterations in the activities of intestinal enzymes in vitamin-C-deficient guinea pigs. 627 90


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