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)

The adaptive modulation hypothesis posits that the expression of digestive proteins should be modulated in response to intake of their respective substrates. A corollary of this hypothesis suggests that dietary flexibility and digestive plasticity should be correlated. We examined these two hypotheses in two granivorous Chilean birds (Zonotrichia capensis and Diuca diuca) that differ in dietary breadth. D. diuca is a strict granivore, whereas Z. capensis also eats insects. In field-caught birds, the activity of the intestinal dipeptidase aminopeptidase-N was positively correlated with intake of insects in Z. capensis but not in D. diuca. This is the first field documentation of modulation of intestinal enzymes by diet in birds. Intestinal maltase and sucrase activities were not correlated with seed (vs. insect) intake in either species. In the laboratory, captive birds of both species exhibited similar modulation of membrane-bound intestinal hydrolases when fed on synthetic diets of contrasting carbohydrate and protein composition. Maltase, sucrase, and aminopeptidase-N activities were significantly higher in birds fed on the carbohydrate-free than those on the carbohydrate-containing diet. Activities of the three enzymes were positively correlated. Therefore, this increase probably resulted from nonspecific increases of all enzymes resulting from intake of the carbohydrate-free diet. Principal components analysis separating the effect of diet on specific and on nonspecific modulation revealed that diet had a strong effect on nonspecific activity of intestinal enzymes in both Z. capensis and D. diuca. Diet also significantly affected aminopeptidase-N activities when the effect of diet on nonspecific modulation was removed. Birds fed on the carbohydrate-free, high-protein diet had significantly higher specific aminopeptidase-N activities than those fed on the carbohydrate-containing diet. Our results cast doubts on the notion that dietary flexibility and the plasticity of the gut's enzymes are necessarily correlated and on the general validity of the adaptive modulation hypothesis.
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PMID:Dietary flexibility and intestinal plasticity in birds: a field and laboratory study. 954 55

Intestinal ischemia necessitates rapid re-establishment of blood flow to prevent irreversible anoxic tissue damage. However, reperfusion results in additional injury as a consequence of the generation of oxygen free radicals. To date, no clear-cut marker to differentiate between ischemia versus reperfusion injury is available. In this regard, previous studies from our laboratory utilizing a rat in vitro lipid peroxidation model demonstrated that the generation of free radicals resulted in the inactivation of only the intestinal brush border alkaline phosphatase enzyme, with no effect on other membrane-bound digestive enzymes. Current studies were designed to assess the possibility of alkaline phosphatase being a specific marker of the reperfusion injury in canine and human ex vivo ischemia/reperfusion models. Small bowels harvested from canines and organ donors were subjected to ischemia followed by reperfusion. Brush border membrane enzymes, alkaline phosphatase, sucrase, maltase, and gamma-glutamyl transpeptidase were assayed in mucosal extracts from intestines with ischemia versus reperfusion. In both experimental models, there was no change in any enzyme activity with warm ischemia alone. In contrast, alkaline phosphatase activity was significantly decreased in both the canine and human reperfusion models, with no change in specific activities of sucrase, maltase, and gamma-glutamyl transpeptidase. Our data indicate that the alkaline phosphatase enzyme activity may represent a potential marker of intestinal reperfusion injury and may permit quantitative assessments of therapeutic interventions in human intestinal reperfusion injury.
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PMID:Decrease in mucosal alkaline phosphatase: a potential marker of intestinal reperfusion injury. 1021 63

The inhibitory effects of natural and synthetic inhibitors on the intestinal membrane-bound hydrolase, alpha-glucosidase (AGH), were evaluated by using an immobilized cyanogen bromide-activated Sepharose 4B support. Immobilized AGH (iAGH) inhibition study by synthetic inhibitors (acarbose and voglibose) revealed that the magnitude of inhibition differed from that in the free AGH (fAGH) study: IC50 value of acarbose in iAGH-maltase assay system, 340-430 nM; fAGH, 11 nM. iAGH-maltase inhibition by both inhibitors was influenced by blocking reagents with different functional groups (COOH, OH, CH3, and NH2 groups). On the other hand, significant iAGH-sucrase inhibitory activity was observed only when using the negatively charged support induced by 0.1 M beta-alanine. The Km values obtained in the iAGH assay system were similar to those from the fAGH method. With natural inhibitors, the iAGH-sucrase inhibitory activity of D-Xylose, with in vivo glucose suppression, increased twice compared to that in fAGH. Green tea extract gave almost the same inhibition for both AGH assay systems.
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PMID:Evaluation of alpha-glucosidase inhibition by using an immobilized assay system. 1099 9

Four diacylated pelargonidin (Pg: SOA-4 and SOA-6), cyanidin (Cy: YGM-3), and peonidin (Pn: YGM-6) 3-sophoroside-5-glucosides isolated from the red flowers of the morning glory, Pharbitis nil cv. Scarlett O'Hara (SOA), and the storage roots of purple sweet potato, Ipomoea batatas cv. Ayamurasaki (YGM), were subjected to an alpha-glucosidase (AGH) inhibitory assay, in which the assay was performed with the immobilized AGH (iAGH) system to mimic the membrane-bound AGH at the small intestine. As a result, the acylated anthocyanins showed strong maltase inhibitory activities with IC(50) values of <200 microM, whereas no sucrase inhibition was observed. Of these, SOA-4 [Pg 3-O-(2-O-(6-O-(E-3-O-(beta-D-glucopyranosyl)caffeyl)-beta-D-glucopyranosyl)-6-O-E-caffeyl-beta-D-glucopyranoside)-5-O-beta-D-glucopyranoside] possessed the most potent maltase inhibitory activity (IC(50) = 60 microM). As a result of a marked reduction of iAGH inhibitory activity by deacylating the anthocyanins, that is, Pg (or Cy or Pn) sophoroside-5-glucoside, acylation of anthocyanin with caffeic (Caf) or ferulic (Fer) acid was found to be important in the expression of iAGH (maltase) inhibition. In addition, the result that Pg-based anthocyanins showed the most potent maltase inhibition, with an IC(50) value of 4.6 mM, and the effect being in the descending order of potency of Pg > Pn/Cy strongly suggested that no replacement at the 3'(5')-position of the aglycon B-ring may be essential for inhibiting iAGH action.
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PMID:alpha-Glucosidase inhibitory action of natural acylated anthocyanins. 2. alpha-Glucosidase inhibition by isolated acylated anthocyanins. 1130 52

Cedar waxwings (Bombycilla cedrorum) feed predominantly on fruits that are rich in simple sugars and low in nitrogen, supplementing this diet with arthropod prey during the summer months as well as flowers and tree sap in springtime. In contrast, thrushes feed extensively on fatty, protein-rich invertebrate prey, supplemented with sugary and lipid-rich fruits. Simple sugars and fats are digested and/or absorbed by distinctly different physiological mechanisms, which suggests the possibility of contrasting digestive strategies in animals specialized to diets containing one of these two energy sources. In this study, we quantified enzymatic activity of three membrane-bound intestinal enzymes of cedar waxwings and five species of thrushes to explore this aspect of their digestive physiology. These enzymes catalyze the final steps in the digestion of carbohydrates (sucrase-isomaltase and maltase-glucoamylase) and protein (aminopeptidase-N). The two carbohydrases are homologous enzymes with overlapping functions; both enzymes catalyze the hydrolysis of maltase and isomaltase. The membrane-bound digestive enzyme systems that we described for cedar waxwings and thrushes can be explained by the particular nutrients contained within their respective natural diets. Consistent with previous work, cedar waxwings displayed intestinal sucrase activity, whereas thrushes did not. Correspondingly, cedar waxwings eat some foods containing sucrose, whereas thrushes do not. Sucrase-isomaltase conferred all maltase and isomaltase activity in cedar waxwings. In contrast, all maltase and isomaltase activity in thrushes was necessarily sucrase independent, which indicated the presence of maltase-glucoamylase. The absence of sucrase-independent maltase activity in cedar waxwings suggests that sucrase-isomaltase obviates the need for maltase-glucoamylase. Indeed, total maltase and isomaltase activities were much higher in cedar waxwings than in thrushes. Neither waxwings nor thrushes eat starchy foods; sucrase-isomaltase in waxwings and maltaseglucoamylase in thrushes probably function in digesting glycogen in animal foods. We suggest that digestive traits associated with specialization to monosaccharide-rich fruits (lack of a grinding gizzard) by frugivorous waxwings and thrushes may prevent utilization of starchy seeds. Total aminopeptidase-N activity in cedar waxwings was indistinguishable from the allometric pattern among thrush species, but the distribution of this enzyme along the intestines of waxwings and thrushes was distinctly different, which demonstrates that total enzyme activity can be insufficient as a descriptor of the functional activity of brush border enzymes. Aminopeptidase-N activity peaked in the anterior part of the intestines of thrushes and in the terminal portion of the intestines of waxwings, which suggests contrasting strategies for protein digestion from fatty versus sugary diets, respectively.
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PMID:The membrane-bound intestinal enzymes of waxwings and thrushes: adaptive and functional implications of patterns of enzyme activity. 1143 43

We have screened the EUROFAN (European Functional Analysis Network) deletion strain collection for yeast mutants defective in secretory/vacuolar pathways and/or associated biochemical modifications. We used systematic Western immunoblotting to analyse the electrophoretic pattern of several markers of the secretory/vacuolar pathways, the soluble alpha-factor, the periplasmic glycoprotein invertase, the plasma membrane GPI-anchored protein Gas1p, and two vacuolar proteins, the soluble carboxypeptidase Y and the membrane-bound alkaline phosphatase, which are targeted to the vacuole by different pathways. We also used colony immunoblotting to monitor the secretion of carboxypeptidase Y into the medium, to identify disruptants impaired in vacuolar targeting. We identified 25 mutants among the 631 deletion strains. Nine of these mutants were disrupted in genes identified in recent years on the basis of their involvement in trafficking (VPS53, VAC7, VAM6, APM3, SYS1), or glycosylation (ALG12, ALG9, OST4, ROT2). Three of these genes were identified on the basis of trafficking defects by ourselves and others within the EUROFAN project (TLG2, RCY1, MON2). The deletion of ERV29, which encodes a COPII vesicle protein, impaired carboxypeptidase Y trafficking from the endoplasmic reticulum to the Golgi apparatus. We also identified eight unknown ORFs, the deletion of which reduced Golgi glycosylation or impaired the Golgi to vacuole trafficking of carboxypeptidase Y. YJR044c, which we identified as a new VPS gene, encodes a protein with numerous homologues of unknown function in sequence databases.
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PMID:Mutants defective in secretory/vacuolar pathways in the EUROFAN collection of yeast disruptants. 1187 Aug 58

Our objectives were to determine postnatal changes in the maximal enzyme activity (V(max)) and enzyme affinity (K(m)) of jejunal mucosal membrane-bound alkaline phosphatase, aminopeptidase N and sucrase using a porcine model which may more closely resemble the human intestine. Jejunal brush border membrane was prepared by Mg(2+)-precipitation and differential centrifugation from pigs of suckling (8 days), weaning (28 days), post-weaning (35 days) and adult (70 days) stages. p-Nitrophenyl phosphate (0-8 mM), L-alanine-p-nitroanilide hydrochloride (0-28 mM) and sucrose (0-100 mM) were used in alkaline phosphatase, aminopeptidase N and sucrase kinetic measurements. V(max) of alkaline phosphatase was the lowest in the adult (4.27 micromol.mg(-1) protein.min(-1)), intermediate in the suckling (9.75 micromol.mg(-l) protein.min(-l)) and the highest in the weaning and post-weaning stage (12.83 and 10.40 micromol.mg(-l) protein.min(-l)). K(m) of alkaline phosphatase was high in the suckling and weaning stages (5.14 and 9.93 mM) and low in the adult (0.66 mM). V(max) of aminopeptidase N was low in the suckling (7.04 micromol.mg protein(-1).min(-1)) and high in the post-weaning stage (13.36 micromol.mg(-l) protein.min(-l)). K(m) of aminopeptidase N was the highest in the two weaning stages (2.96 and 3.39 mM), intermediate in the adult (2.33 mM) and the lowest in the suckling stage (1.66 mM). V(max) of sucrase increased from the suckling to the adult (0.48-1.30 micromol.mg(-l) protein.min(-l)). K(m) of sucrase ranged from 11.19 to 16.57 mM. There are dramatic postnatal developmental changes in both the maximal enzyme activity and enzyme affinity of jejunal brush border membrane-bound alkaline phosphatase, aminopeptidase N and sucrase in the pig.
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PMID:Postnatal ontogeny of kinetics of porcine jejunal brush border membrane-bound alkaline phosphatase, aminopeptidase N and sucrase activities. 1204 69

The relationships between cellulose accumulation, changes in specific activities of enzymes of sucrose catabolism, levels of UDP-glucose and rate of dark respiration were investigated in the subapical 1 cm-hypocotyl region of 10- to 14-day-old-sunflower seedlings (Helianthus annuus L). The plants were grown under a light/dark regime in vermiculite that was soaked either with distilled water or half-strength Hoagland nutrient solution. At this stage of seedling development, the hypocotyl had ceased to elongate but increased in width. Stem thickening and the rate of cellulose accumulation were promoted by nutrient solution. The levels of the soluble (vacuolar) and wall-associated acid invertases (EC 3.2.1.26) were not correlated with these processes. However, the activities of the soluble (cytoplasmic) and membrane-bound sucrose synthases (EC 2.4.1.13) were larger in hypocotyls that were grown in the presence of nutrient solution. The concentration of UDP-glucose was reduced, and the rate of dark respiration was enhanced in the hypocotyls that were grown in Hoagland solution. The results support the hypothesis that both forms of the enzyme sucrose synthase play a critical role in cellulose biosynthesis of hypocotyl cells that had ceased to elongate and continue to grow by wall thickening.
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PMID:Sucrose metabolism and cellulose biosynthesis in sunflower hypocotyls. 1206 Feb 59

Purified glycopeptides derived from yeast invertase act as highly potent elicitors in suspension-cultured tomato (Lycopersicon esculentum [L.] Mill) cells, inducing ethylene biosynthesis and phenylalanine ammonia lyase half-maximally at concentrations of 1 to 5 nM. We previously demonstrated the presence of a high-affinity binding site that specifically recognized these glycopeptides in cells and microsomal membranes of tomato (C.W. Basse, A. Fath, T. Boller [1993] J Biol Chem 268: 14724-14731). This elicitor-binding site was solubilized in an active form from the microsomal membranes using the neutral detergents n-dodecylmaltoside and n-dodecanoylsucrose and purified 67-fold in a single step by anion-exchange chromatography. Ligand saturation studies and competition experiments with unlabeled glycopeptides and glycans demonstrated that the detergent-solubilized elicitor-binding site retained the high affinity (Kd approximately 1-4 nM) and selectivity of the membrane-bound form. The binding site was found to have a high affinity for N-linked glycans with nine mannosyl residues from fungal glycoproteins, whereas it did not recognize the typical mammalian glycans with nine mannosyl residues, demonstrating further its high selectivity.
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PMID:Solubilization, Partial Purification, and Characterization of a Binding Site for a Glycopeptide Elicitor from Microsomal Membranes of Tomato Cells. 1222 70

Sequential processing of the transmembrane amyloid precursor protein (APP) by the beta-secretase BACE and by the gamma-secretase causes secretion of Abeta peptides. Extracellular aggregation of these peptides in the brain is a major hallmark of Alzheimer's disease. For therapeutic purposes and the development of specific inhibitors, it is important to characterize these secretases. We have established a cellular growth selection system for functional expression of human BACE in the yeast Saccharomyces cerevisiae. A fragment of APP bearing the beta-site, the transmembrane domain and the cytosolic tail was fused to the C-terminus of the yeast enzyme invertase, which is normally secreted to allow cell growth in the presence of sucrose as the sole carbon source. The resulting invertase-APP fusion protein was expressed as a type-I transmembrane protein in intracellular compartments of yeast cells lacking endogenous invertase. In these cells, co-expression of human BACE restored cell growth on selective plates upon cleavage of the invertase-APP fusion protein. The cellular growth selection system presented here can be generally applied to screen for secretases that specifically cleave membrane-bound substrates. Furthermore, this system provides the basis for a high-throughput screen for identifying secretase inhibitors that are active in eukaryotic cells.
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PMID:Human beta-secretase activity in yeast detected by a novel cellular growth selection system. 1259 86


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