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)

Brush border membrane-bound digestive enzymes such as disaccharidases (lactase, sucrase, and maltase), leucine aminopeptidase N, and alkaline phosphatase were measured in jejunum from pigs experimentally infected with porcine epidemic diarrhea virus (PEDV). Three piglets from the infected and control groups were euthanized by electrocution and subjected to necropsy at 24, 36, 48, 60, and 72 hours post-inoculation (hpi). The infection of PEDV to jejunum resulted in significant decreases in brush border membrane-bound digestive enzymes such as disaccharidases (lactase, sucrase, and maltase), leucine aminopeptidase N, and alkaline phosphatase. PEDV replication results in massive destruction of villous enterocytes leading to a marked reduction of intestinal epithelial surface and brush border membrane-bound digestive enzyme activity. Reduced enzymatic activity and villous atrophy in the small intestine is thought to result in a maldigestive and malabsorptive diarrhea.
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PMID:Decreased activity of brush border membrane-bound digestive enzymes in small intestines from pigs experimentally infected with porcine epidemic diarrhea virus. 1675 79

(-)-Epigallocatechin-3-gallate (EGCG), a component of catechins, has been shown to reduce blood glucose levels. In the present study, we investigated the antidiabetic activity and its mechanism of lipophilic EGCG derivative (L-EGCGd) in streptozotocin (STZ)-induced diabetic rats. L-EGCGd was chemically modified from traditional hydrophilic EGCG. After 30 days treatment, plasma levels of glucose were significantly reduced by 40.5+/-7.0% and 17.0+/-2.8% in groups administered 50 or 25 mg kg(-1)d(-1) L-EGCGd, respectively, as compared with that in the diabetic control group. Lipid metabolites, such as total cholesterol (TC), triglyceride (TG) and low-density lipoprotein cholesterol (LDLC) were effectively attenuated by L-EGCGd administration, but plasma HDLC levels did not change significantly. The oral glucose tolerance test (OGTT) greatly revealed the improved ability of glucose tolerance with treatment of L-EGCGd. L-EGCGd only retarded the postprandial rise in blood glucose with sucrose loading but not glucose loading. And activity of alpha-glucosidase was inhibited by 50% at the concentration of 246.6 microg ml(-1) L-EGCGd. As a result, we first demonstrated that the purified form of compound L-EGCGd possessed the hypoglycemic effect under its role of alpha-glucosidase inhibition, and therefore should be possibly accepted as an alternative oral medication protecting patients against postprandial hyperglycemic toxicity on the treatment of diabetes and its complications.
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PMID:Antidiabetic activity of lipophilic (-)-epigallocatechin-3-gallate derivative under its role of alpha-glucosidase inhibition. 1718 56

The hydrolysis of sucrose, the principal dietary source of carbon for aphids, is catalysed by a gut alpha-glucosidase/transglucosidase activity. An alpha-glucosidase, referred to as APS1, was identified in both a gut-specific cDNA library and a sucrase-enriched membrane preparation from guts of the pea aphid Acyrthosiphon pisum by a combination of genomic and proteomic techniques. APS1 contains a predicted signal peptide, and has a predicted molecular mass of 68 kDa (unprocessed) or 66.4 kDa (mature protein). It has amino acid sequence similarity to alpha-glucosidases (EC 3.2.1.20) of glycoside hydrolase family 13 in other insects. The predicted APS1 protein contains two domains: an N-terminal catalytic domain, and a C-terminal hydrophobic domain. In situ localisation and RT-PCR studies revealed that APS1 mRNA was expressed in the gut distal to the stomach, the same localisation as sucrase activity. When expressed heterologously in Xenopus embryos, APS1 was membrane-bound and had sucrase activity. It is concluded that APS1 is a dominant, and possibly sole, protein mediating sucrase activity in the aphid gut.
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PMID:Molecular characterisation of a candidate gut sucrase in the pea aphid, Acyrthosiphon pisum. 1736 94

Dietary carbohydrates provide an important source of energy for flight, and contribute to longevity and fecundity of mosquitoes. The most common sugar mosquitoes ingest is sucrose, and digestion of this substance is carried out mainly by alpha-glucosidases. In the current work, we tested the efficiency of sucrose on Anopheles aquasalis female diet. The best longevity (days) was reached when sugar was available in the diet, whereas most only blood fed females were dead 6 days after emergence. Three alpha-glucosidase isoforms were detected in the adult female midgut, named alphaGlu1, alphaGlu2 and alphaGlu3. These are acidic alpha-glucosidases with optima pH around pH 5.5. alphaGlu1 and alphaGlu2 are present in both secreted and membrane-bound forms, whereas alpha-Glu3 only in anchored to membranes. The alpha-glucosidase activity is concentrated mainly in the posterior midgut (70%), both in non-fed or 10% sucrose fed females. The single form of these alpha-glucosidases seemed to be approximately 70 kDa polypeptides, although alphaGlu2 is presented in >or=600 kDa self-aggregates. Km values of alphaGlu1, alphaGlu2 and alphaGlu3 differed significantly from each other, supporting the statement that three alpha-glucosidases are produced in the female midgut. Together, all data suggest that sugar is an essential component of A. aquasalis female diet. In addition, alpha-glucosidases are synthesized in the same place where sucrose is digested and absorbed, the midgut.
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PMID:Sugar digestion in mosquitoes: identification and characterization of three midgut alpha-glucosidases of the neo-tropical malaria vector Anopheles aquasalis (Diptera: Culicidae). 1744 10

Yeast alpha-glucosidase I (Cwh41p) encoded by CWH41 is an endoplasmic reticulum (ER) membrane-bound glycoprotein (833 residues), which plays an important role in the early steps of the N-glycosylation pathway. In this study functional expression of three truncated fragments of Cwh41p, all containing the catalytic region, was investigated. Cwht1p (E35-F833), with deletion of the N-terminus and transmembrane domain, was expressed as a catalytically active fragment while R320-F833(Cwht2p) and M526-F833 (Cwht3p) were not detected. Significantly higher glucosidase I activity was found in a soluble extract from yeast overexpressing CWHT1 (1,400 U/g biomass) than yeast overexpressing CWH41 (300 U/g biomass). Cwht1p was purified as a soluble 94 kDa non-glycosylated protein with a specific activity (3,600 U/mg protein) comparable to that of the soluble alpha-glucosidase I (3000 U/mg protein). These findings indicate that the active conformation of the enzyme is not dependent on protein glycosylation and suggest that the M1-I28 region of Cwh41p carries an ER-targeting signal sequence. In addition, two highly conserved carboxylic acid residues, E580 and D584 of Cwht1p (corresponding to E613 and D617 of Cwh41p), located within the catalytic domain of yeast enzyme were subjected to mutation. Substitution of each residue with Ala resulted in low expression and undetectable glucosidase I activity. These findings indicate that E613 and D617 play a crucial role in maintaining alpha-glucosidase I activity.
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PMID:Truncations and functional carboxylic acid residues of yeast processing alpha-glucosidase I. 1745 96

Human maltase-glucoamylase (MGAM) is one of the two enzymes responsible for catalyzing the last glucose-releasing step in starch digestion. MGAM is anchored to the small-intestinal brush-border epithelial cells and contains two homologous glycosyl hydrolase family 31 catalytic subunits: an N-terminal subunit (NtMGAM) found near the membrane-bound end and a C-terminal luminal subunit (CtMGAM). In this study, we report the crystal structure of the human NtMGAM subunit in its apo form (to 2.0 A) and in complex with acarbose (to 1.9 A). Structural analysis of the NtMGAM-acarbose complex reveals that acarbose is bound to the NtMGAM active site primarily through side-chain interactions with its acarvosine unit, and almost no interactions are made with its glycone rings. These observations, along with results from kinetic studies, suggest that the NtMGAM active site contains two primary sugar subsites and that NtMGAM and CtMGAM differ in their substrate specificities despite their structural relationship. Additional sequence analysis of the CtMGAM subunit suggests several features that could explain the higher affinity of the CtMGAM subunit for longer maltose oligosaccharides. The results provide a structural basis for the complementary roles of these glycosyl hydrolase family 31 subunits in the bioprocessing of complex starch structures into glucose.
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PMID:Human intestinal maltase-glucoamylase: crystal structure of the N-terminal catalytic subunit and basis of inhibition and substrate specificity. 1803 14

Hemipterans are characterized by the absence of the peritrophic membrane, an anatomical structure that envelopes the food bolus in the majority of insects. However, the microvillar membranes of many hemipteran midgut cells are not in direct contact with the food bolus, due to the existence of the so-called perimicrovillar membrane (PMM), which covers the microvilli extending into the gut lumen with dead ends. alpha-Glucosidase is a biochemical marker for PMM in the seed sucker bug Dysdercus peruvianus (Heteroptera: Pyrrhocoridae). In this article, we report that adults of the major hemipteran infra-orders (Sternorrhyncha, Auchenorrhyncha, and Heteroptera) have PMM and a major membrane bound alpha-glucosidase, which has properties similar to those of the D. peruvianus enzyme. A polyclonal antibody raised against the enzyme of D. peruvianus recognized the enzymes present in PMM from the above-mentioned hemipteran groups. The same antibody was also able of recognizing perimicrovillar alpha-glucosidase from thrips. No PMM nor membrane-bound alpha-glucosidase were found in Psocoptera and Phthiraptera midguts. This suggests that PMM and PMM-bound-alpha-glucosidase are widespread among insects of the order Hemiptera and of the sister order Thysanoptera. The data support the hypothesis that PMM may have originated in the Condylognatha (Paraneopteran taxon including Hemiptera and Thysanoptera) ancestral stock and are associated with plant sap feeding.
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PMID:Occurrence of midgut perimicrovillar membranes in paraneopteran insect orders with comments on their function and evolutionary significance. 1808 29

The detailed mechanistic aspects for the final starch digestion process leading to effective alpha-glucogenesis by the 2 mucosal alpha-glucosidases, human sucrase-isomaltase complex (SI) and human maltase-glucoamylase (MGAM), are poorly understood. This is due to the structural complexity and vast variety of starches and their intermediate digestion products, the poorly understood enzyme-substrate interactions occurring during the digestive process, and the limited knowledge of the structure-function properties of SI and MGAM. Here we analyzed the basic catalytic properties of the N-terminal subunit of MGAM (ntMGAM) on the hydrolysis of glucan substrates and compared it with those of human native MGAM isolated by immunochemical methods. In relation to native MGAM, ntMGAM displayed slower activity against maltose to maltopentose (G5) series glucose oligomers, as well as maltodextrins and alpha-limit dextrins, and failed to show the strong substrate inhibitory "brake" effect caused by maltotriose, maltotetrose, and G5 on the native enzyme. In addition, the inhibitory constant for acarbose was 2 orders of magnitude higher for ntMGAM than for native MGAM, suggesting lower affinity and/or fewer binding configurations of the active site in the recombinant enzyme. The results strongly suggested that the C-terminal subunit of MGAM has a greater catalytic efficiency due to a higher affinity for glucan substrates and larger number of binding configurations to its active site. Our results show for the first time, to our knowledge, that the C-terminal subunit of MGAM is responsible for the MGAM peptide's "glucoamylase" activity and is the location of the substrate inhibitory brake. In contrast, the membrane-bound ntMGAM subunit contains the poorly inhibitable "maltase" activity of the internally duplicated enzyme.
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PMID:Luminal starch substrate "brake" on maltase-glucoamylase activity is located within the glucoamylase subunit. 1835 21

The activity of the Bacillus sphaericus binary (Bin) toxin on Culex quinquefasciatus larvae depends on its specific binding to the Cqm1 receptor, a midgut membrane-bound alpha-glucosidase. A 19-nucleotide deletion in the cqm1 gene (cqm1(REC)) mediates high-level resistance to Bin toxin. Here, resistance in nontreated and B. sphaericus-treated field populations of C. quinquefasciatus was assessed through bioassays as well as a specific PCR assay designed to detect the cqm1(REC) allele in individual larvae. Resistance ratios at 90% lethal concentration, gathered through bioassays, were close to 1 and indicate that the selected populations had similar levels of susceptibility to B. sphaericus, comparable to that of a laboratory colony. A diagnostic PCR assay detected the cqm1(REC) allele in all populations investigated, and its frequency in two nontreated areas was 0.006 and 0.003, while the frequency in the B. sphaericus-treated population was significantly higher. Values of 0.053 and 0.055 were detected for two distinct sets of samples, and homozygote resistant larvae were found. Evaluation of Cqm1 expression in individual larvae through alpha-glucosidase assays corroborated the allelic frequency revealed by PCR. The data from this study indicate that the cqm1(REC) allele was present at a detectable frequency in nontreated populations, while the higher frequency in samples from the treated area is, perhaps, correlated with the exposure to B. sphaericus. This is the first report of the molecular detection of a biolarvicide resistance allele in mosquito populations, and it confirms that the PCR-based approach is suitable to track such alleles in target populations.
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PMID:Detection of an allele conferring resistance to Bacillus sphaericus binary toxin in Culex quinquefasciatus populations by molecular screening. 1909 23

The tropical agamid lizard, Lophognathus temporalis, has higher metabolic and feeding rates during the wet season compared to the dry season. Also, lizards from urban sites tend to be larger than those from natural sites, partly due to site differences in food availability. Therefore, we hypothesized that activity of membrane-bound intestinal enzymes and masses of organs related to digestion would differ both seasonally and between urban and natural sites. To test this, we measured activities of aminopeptidase-N (APN), maltase, and sucrase, as well as organ masses. APN activity (micromol min(-1) g(-1)) was highest in the middle portion of the intestine (section 2), followed by the proximal portion (section 1) and then the distal portion (section 3). Maltase activity was highest in section 1 and decreased distally. We detected some sucrase activity in section 1 but none in sections 2 or 3. We found similar enzyme activities within each section irrespective of site or season. However, total enzyme activities were higher during the wet season compared to the dry season for both urban and bush L. temporalis. Total wet season enzyme activity in urban and bush L. temporalis was greatest for APN (25.4; 15.8 micromol min(-1); respectively), then maltase (3.9; 3.6 micromol min(-1); respectively) and then sucrase (0.3; 0.2 micromol min(-1); respectively). The higher total enzyme activities was the result of an increase in intestinal mass during the wet season.
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PMID:Seasonal effects on intestinal enzyme activity in the Australian agamid lizard, Lophognathus temporalis. 1941 91


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