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)

1. Pig intestinal sucrase and maltase activities increase markedly, and lactase activity decreases, during the second week of post-natal life. Correlations noted between the time course describing these changes and that found previously to describe a decline in the ability of the pig intestine to take up macromolecules suggest that both events are subject to the same type of developmental control. 2. Injection of epidermal growth factor (EGF) into 3-day-old piglets increase sucrase and maltase activities measured 3 days later. These increases, which are not seen when measuring other hydrolase enzymes, are confined to the mid and distal regions of the small intestine. 3. Dexamethasone injected into 3-day-old piglets inhibits lactase and, on occasion, sucrase activities without affecting other intestinal hydrolases. Significant increases in sucrase and maltase activities also occur in distal intestine following injection of EGF plus dexamethasone into 3-day-old pigs. 4. Cytochemical analysis shows EGF effects on sucrase and maltase activities to be exerted in crypt and basal villus enterocytes produced post-natally. Dexamethasone inhibits lactase activity mainly by acting on mid and upper villus enterocytes produced before birth. 5. EGF appears to increase sucrase and maltase activities by extending the time during which young enterocytes continue to accumulate these enzymes in their brush-border membranes. Dexamethasone appears to cause a more fundamental change in the biochemistry of older enterocytes. accompanied by an increasing ability of these cells to transport neutral amino acids through a sodium-dependent mechanism (see James, Smith, Tivey & Wilson, 1987a).
J Physiol 1987 Dec
PMID:Epidermal growth factor selectively increases maltase and sucrase activities in neonatal piglet intestine. 332 84

Although sucrase-isomaltase appears in the small intestine at quite different stages of development in man as compared with most mammals, we find that in human embryo also the appearance of sucrase-isomaltase mRNA closely parallels that of sucrase and isomaltase activities, as we have previously found to be the case in baby rabbits. Also, in the proximal-distal gradient of human embryonic intestine (proximal small intestine greater than distal small intestine greater than colon) the levels of these enzyme activities and those of the corresponding mRNA correlate closely. Finally, glucocorticosteroid treatment of a human colon carcinoma cell line (Caco-2) in vitro or of baby rabbits in vivo leads to a parallel increase of both sucrase and isomaltase activities and of sucrase-isomaltase mRNA. We conclude that in man also, in spite of the different timing in development, the biosynthesis of sucrase-isomaltase is most likely to be controlled at the level of transcription or perhaps of the mRNA stability.
Biochem Biophys Res Commun 1987 Dec 16
PMID:The biosynthesis of intestinal sucrase-isomaltase in human embryo is most likely controlled at the level of transcription. 342 4

A rapid, enzyme-linked colorimetric assay, for the sequential determination of nanomole quantities of glucose and fructose in the same sample, has been developed for the measurement of fructosyl transferase activity in plant extracts. The assay extends the conventional dehydrogenase-linked assay for these sugars by utilizing the intermediary electron carrier, phenazine methosulfate, to couple NADP reduction to the production of a formazan dye from the tetrazolium salt, thiazolyl blue, in a form suitable for measurement using a microtiter plate reader. When the microtiter plate assay was used to measure the activities of yeast invertase and sucrose:sucrose fructosyl transferase from Lolium temulentum, results obtained were very similar to results obtained using the conventional procedure. The rapidity, small scale, and ease of execution of the method offers considerable advantages over the conventional hexose assay and is particularly suitable for screening of large numbers of small samples, exploiting both the speed of the microtiter plate reader and the facility of for microcomputer processing of data. The potential of this method for use with other enzyme systems and other metabolites is discussed.
Anal Biochem 1987 Dec
PMID:Colorimetric microtiter plate assay of glucose and fructose by enzyme-linked formazan production: applicability to the measurement of fructosyl transferase activity in higher plants. 344 22

We have devised a genetic selection for mutant yeast cells that fail to properly deliver the vacuolar glycoprotein CPY to the lysosome-like vacuole. This has allowed us to identify mutations in eight VPL complementation groups that result in aberrant secretion of up to approximately 90% of the immunoreactive CPY. Other soluble vacuolar proteins are also affected by each vpl mutation, demonstrating that a sorting system for multiple vacuolar proteins exists in yeast. Mislocalized CPY apparently traverses late stages of the secretory pathway, since a vesicle-accumulating sec1 mutation prevents secretion of this protein. Despite the presence of abnormal membrane-enclosed organelles in some of the vpl mutants, maturation and secretion of invertase are not substantially perturbed. Thus vpl mutations define a new class of genes that encode products required for sorting of newly synthesized vacuolar proteins from secretory proteins during their transit through the yeast secretory pathway.
Cell 1986 Dec 26
PMID:Protein sorting in yeast: mutants defective in vacuole biogenesis mislocalize vacuolar proteins into the late secretory pathway. 353 26

Tunicamycin apparently inhibited the biosynthesis of glucose, galactose, and maltose transport systems in Saccharomyces cerevisiae. Under the conditions used, the antibiotic also blocked the biosynthesis of invertase, a well-known yeast glycoprotein, as well as the glycosylation of a marker mannoprotein of the yeast cell wall. However, the antibiotic did not affect certain proteins which did not contain carbohydrate. It seems, therefore, that these sugar carriers are glycoproteins.
J Bacteriol 1986 Dec
PMID:Inhibition of biosynthesis of Saccharomyces cerevisiae sugar transport system by tunicamycin. 353 86

We have constructed a PRC1-SUC2 gene fusion that directs the synthesis in Saccharomyces cerevisiae of a hybrid polypeptide consisting of a 433-residue amino-terminal domain derived from the yeast vacuolar protease carboxypeptidase Y (CPY; EC 3.4.16.1) and a 511-residue carboxyl-terminal domain derived from the secreted yeast enzyme invertase (EC 3.2.1.26). Fractionation data indicated that this amount of CPY primary sequence is sufficient to quantitatively divert invertase to the yeast vacuole. The phenotypic consequence of localizing active invertase to the vacuole has enabled us to select for mutants that "mislocalize" the hybrid protein to the cell surface. The corresponding mutations that lead to this effect are all trans-acting and recessive, and they define at least eight complementation groups. These vacuolar protein targeting (vpt) mutants also exhibit hybrid protein independent defects in wild-type CPY delivery to the yeast vacuole. Precursor forms of CPY accumulate in the mutants and are secreted into the yeast periplasm and extracellular medium. The vpt mutants should provide useful information pertaining to the mechanisms by which yeast cells regulate vacuolar protein traffic.
Proc Natl Acad Sci U S A 1986 Dec
PMID:Isolation of yeast mutants defective in protein targeting to the vacuole. 353 17

No D-glucosylfructoses except sucrose, neither the alpha(1----1)- nor the alpha(1----3)- or the alpha(1----5)- or the alpha(1----6)-disaccharide possess substrate properties for beta-fructosidase from yeast. The two latter ones, leucrose and isomaltulose, however, are non-competitive (leucrose) or uncompetitive (isomaltulose, Palatinose) inhibitors of beta-fructosidase from yeast. Due to the high substrate specificity of invertase, assays of its activity have predictive power for cariological aspects of sugar substitutes carrying glycoside bonds between glucose and fructose.
Z Ernahrungswiss 1986 Dec
PMID:[A stepwise method of evaluating sugar substitutes--a preliminary study using enzymes. 2. Beta-fructosidase from yeast]. 354 94

The mitochondrial matrix enzyme manganese superoxide dismutase (SOD) of Saccharomyces cerevisiae is encoded in the nucleus. It is synthesized as a precursor with an NH2-terminal extension of 26 amino acids which is cleaved off during import into the mitochondrion. Fusions between the NH2-terminal 34 amino acids of SOD and the cytosolic proteins invertase of yeast and mouse dihydrofolate reductase (DHFR) were tested for in vitro binding and import into mitochondria. Efficient translocation over the mitochondrial membranes takes place in the case of the SOD-DHFR fusion. The SOD-invertase fusion protein does not get translocated and binds to the organelle with only low efficiency. Yeast transformants harbouring the SOD-invertase fusion gene accumulate approximately 95% of the hybrid protein in the cytosol. The remaining material is found in the interior of the mitochondrion, loosely attached to the inner membrane. We conclude that the pre-sequence of SOD is able to deliver a passenger protein to the mitochondrion. The efficiency of protein delivery and translocation across the membrane is, however, influenced by the passenger protein.
EMBO J 1986 Dec 20
PMID:Targeting efficiency of a mitochondrial pre-sequence is dependent on the passenger protein. 354 82

The DNase I sensitivity of chromatin of the yeast SUC2 gene, which encodes two forms of invertase, has been studied both in the genome and in a multicopy plasmid carrying the gene and its flaking sequences. Whereas little if any difference in the DNase I sensitivity of the flanking regions was found between the repressed and the derepressed states, derepression of the gene was accompanied by a large increase in the sensitivity of the transcribed region. A well-defined DNase I hypersensitive site was found centered at approximately 120 bp downstream from the end of the coding region. This site seems to be flanked in the 3' non-coding region by strictly positioned nucleosomes, and the structure of this region changes upon derepression. In the 5' non-coding region two DNase I hypersensitive sites have been found flanking the TATA box and a set of three closely spaced hypersensitive sites occurs in an upstream regulatory sequence. The structure of these latter sites depends on the on-off state of transcription.
Mol Gen Genet 1986 Dec
PMID:DNase I sensitivity of the chromatin of the yeast SUC2 gene for invertase. 355 Mar 82

Yeast invertase, when injected into rats, is endocytosed by the liver, mainly by sinusoidal cells. The work reported here aims at investigating the organelles involved in the intracellular journey of this protein. Experiments were performed on rats injected with 125I-invertase (25 micrograms/100 g body wt) and killed at various times after injection. Homogenates were fractioned by differential centrifugation, according to de Duve, Pressman, Gianetto, Wattiaux and Appelmans [(1955) Biochem. J. 63, 604-617]. Early after injection the radioactivity was recovered mainly in the microsomal fraction P; later it was found in the mitochondrial fractions (ML). At all times a peak of relative specific activity was observed in the light mitochondrial fraction L. After isopycnic centrifugation in a sucrose gradient, structures bearing 125I-invertase, present in P, exhibited a relatively flattened distribution with a density of around 1.17 g/ml, relatively similar to that of alkaline phosphodiesterase a plasma membrane marker. The organelles located in ML were endowed with a more homogeneous distribution, their median equilibrium density increasing up to 30 min after injection (1.20 g/ml----1.23 g/ml); with time the radioactivity distribution became more closely related to the distribution of arylsulfatase, a lysosomal enzyme. ML fractions, isolated 10 min and 180 min after 125I-invertase injection, were subjected to isopycnic centrifugation in Percoll gradient with, as solvent, 0.25 M, 0.5 M and 0.75 M sucrose. The change of density of the particles bearing 125I-invertase, as a function of the sucrose concentration, paralleled the change of density of the lysosomes as ascertained by the behaviour of arylsulfatase. The distribution of radioactivity and arylsulfatase in a sucrose gradient was established after isopycnic centrifugation of the ML fraction of rats injected with 125I-invertase, the animals having received or not an injection of 900 micrograms/100 g body weight of unlabelled invertase 15 h before killing. In agreement with our previous results, a shift towards higher densities of about 25% or arylsulfatase takes place in rats pretreated with unlabelled invertase. At 10 min, invertase preinjection did not change the radioactivity distribution curve. Later, it caused a progressive shift of the distribution towards higher-density regions of the gradient where the arylsulfatase, which had been shifted, was located.(ABSTRACT TRUNCATED AT 400 WORDS)
Eur J Biochem 1986 Dec 15
PMID:Intracellular pathway followed by invertase endocytosed by rat liver. 379 13


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