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)

Secretion of acid phosphatase and invertase was examined in an inositol-requiring ino1 mutant of the yeast Saccharomyces cerevisiae. Inositol starvation is known to block plasma membrane expansion, presumably due to restricted membrane phospholipid synthesis. If membrane expansion and extracellular protein secretion are accomplished by the same intracellular transport process, one would expect secretion to fail coordinately with cessation of plasma membrane growth in inositol-starved cells. In glucose-grown, inositol-starved cells, plasma membrane expansion and acid phosphatase secretion stopped coordinately, and intracellular acid phosphatase accumulated. In sucrose-grown, inositol-starved cells, plasma membrane growth halted, but secretion of both acid phosphatase and invertase continued until the onset of inositol-less death. Although glucose-grown and sucrose-grown cells differ in their ability to secrete when deprived of inositol, they exhibited the same disturbances in phospholipid synthesis. Phosphatidylinositol synthesis failed, and its precursors phosphatidic acid and CDP-diglyceride accumulated equally in both cultures. Sucrose-grown yeast cells appear to accomplish normal levels of extracellular protein secretion by an inositol-independent mechanism. In glucose-grown yeasts, both plasma membrane expansion and secretion are inositol dependent.
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PMID:Secretion can proceed uncoupled from net plasma membrane expansion in inositol-starved Saccharomyces cerevisiae. 638 2

To define reproducible conditions for the homogenization of small-intestinal biopsy samples, tissue homogenization has been studied by the use of three different homogenizers. Tissue samples of increasing wet weights (0.5-10.8 mg) were homogenized in a fixed volume (1 ml) before DNA and protein were determined. The DNA to protein ratio was calculated for all wet weights and used as a measure for reproducible homogenization. The minimum tissue wet weight needed for analysis (2 mg) was determined from the values obtained for the DNA to protein ratio. Highly sensitive techniques are described in detail for the assay of brush border (maltase, lactase, sucrase, neutral alpha-glucosidase, alkaline phosphatase, gamma-glutamyl transferase, leucyl-beta-naphthylamidase), basolateral membrane (5'-nucleotidase), and mitochondrial (succinate dehydrogenase) marker enzymes and for four acid hydrolases (acid phosphatase, acid beta-D-galactosidase, N-acetyl-beta-D-glucosaminidase, acid diesterase) in human and rat jejunal mucosa. Linear kinetics have been established for all enzyme assays. The optimal dilution of tissue homogenate for the assay of the various enzymes has been determined to enable the determination of a maximum number of enzymes in each homogenate. The range of enzyme activities in samples of human and rat jejunal mucosa has been determined.
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PMID:Enzyme activities in human and rat jejunal mucosa. 667 54

A series of marker enzymes for brush borders, basolateral membrane, and lysosomes were assayed in mucosal biopsy specimens from patients with untreated and treated coeliac disease and from controls. The brush border enzymes lactase, sucrase, neutral alpha-glucosidase, alkaline phosphatase, and leucyl-beta-naphthylamidase showed reduced activities in the untreated state and complete or partial normalization during treatment. The lysosomal marker enzyme acid phosphatase increased in activity in untreated coeliac disease and was normalized by treatment. The brush border enzyme gamma-glutamyl transferase was nearly normal in untreated patients and slightly increased in treated patients. The basolateral membrane marker, 5'-nucleotidase, was reduced both in untreated and treated patients, whereas the lysosomal marker N-acetyl-beta-glucosaminidase was normal in the untreated state and decreased during treatment. The possible pathogenetic role of the three latter enzymes in coeliac disease is discussed. The patterns of the other enzymes are suggested to be attributable to the morphologic changes in the mucosa.
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PMID:Jejunal mucosal enzymes in untreated and treated coeliac disease. 667 55

We studied the uptake of D-glucose and L-tryptophan by the small intestine and estimated the activities of the intestinal brush border enzymes (sucrase, lactase, NA+-K+-ATPase and alkaline phosphatase) and lysosomal enzymes in rats receiving T-2 toxin orally. considerable decrease occurred in glucose and tryptophan uptake and in brush border sucrase, lactase and (Na+-K+)-ATPase. Alkaline phosphatase activity and release of lysosomal enzymes (acid phosphatase and acid ribonuclease) was unchanged.
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PMID:Effects of T-2 toxin on glucose and tryptophan uptake and intestinal mucosal enzymes. 671 77

Five brush border and 2 lysosomal enzymes were measured in duodenal tissue explants from 21 children and young adults (16 coeliac and 5 non-coeliac) before and after organ culture. Reduced activity of brush border enzymes and increased activity of lysosomal enzymes were recorded in flat mucosas from coeliac patients compared with remission coeliac explants and biopsy specimens from non-coeliac controls. Slightly increased activity of alkaline phosphate and sucrase was recorded during culture (24 h) of coeliac explants. Coeliac specimens in the exacerbation state showed increased activity of acid phosphatase after culture in the presence of gluten, whereas gluten did not provoke detectable alterations in brush border enzyme activities during culture unless the wet weight of material was 1.5 mg or more. In such explants lower activity of brush border enzymes was measured after in vitro gluten exposure than after culture on gluten-free medium. Mucus removed from the specimen surface after culture contained considerable amounts of brush border enzymes and reflected the variations in the tissue homogenates. Culture media contained smaller quantities of enzymes.
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PMID:Brush border and lysosomal marker enzyme profiles in duodenal mucosa from coeliac patients before and after organ culture. 681 57

Cells of a Saccharomyces cerevisiae mutant that is temperature-sensitive for secretion and cell surface growth become dense during incubation at the non-permissive temperature (37 degrees C). This property allows the selection of additional secretory mutants by sedimentation of mutagenized cells on a Ludox density gradient. Colonies derived from dense cells are screened for conditional growth and secretion of invertase and acid phosphatase. The sec mutant strains that accumulate an abnormally large intracellular pool of invertase at 37 degrees C (188 mutant clones) fall into 23 complementation groups, and the distribution of mutant alleles suggests that more complementation groups could be found. Bud emergence and incorporation of a plasma membrane sulfate permease activity stop quickly after a shift to 37 degrees C. Many of the mutants are thermoreversible; upon return to the permissive temperature (25 degrees C) the accumulated invertase is secreted. Electron microscopy of sec mutant cells reveals, with one exception, the temperature-dependent accumulation of membrane-enclosed secretory organelles. We suggest that these structures represent intermediates in a pathway in which secretion and plasma membrane assembly are colinear.
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PMID:Identification of 23 complementation groups required for post-translational events in the yeast secretory pathway. 1505 75

Repressed cells of Saccharomyces cerevisiae, subjected to inhibition of both RNA and protein synthesis, showed a pattern of membrane-bound and cytosol acid phosphatase to the external enzyme which seemed to be linked through a precursor-product relationship. Gel exclusion chromatography did not indicate clear differences between the isoenzymes. Moreover, centrifugation experiments in CsCl and precipitation with concanavalin A suggested that there were no acid phosphatase molecules devoid of carbohydrate. Membrane-bound invertase displayed a molecular weight and a carbohydrate to protein ratio smaller than those of the exocellular enzyme. The values of molecular weight and buoyant density of the membrane-bound enzyme were closer to those found for the cytosol invertase. The stability of the level of the soluble invertase detected in the cytoplasm under derepression conditions, or after RNA or protein synthesis inhibition was found to be only apparent and represented the result of an equilibrium between synthesis and degradation.
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PMID:Metabolic relationship between invertase and acid phosphatase isoenzymes in Saccharomyces cerevisiae. 699 2

Temperature-sensitive secretory mutants (sec) of S. cerevisiae have been used to evaluate the stages and localization of glycoprotein oligosaccharide synthesis. At the nonpermissive growth temperature (37 degrees C), the sec mutants accumulate secretory organelles and glycoproteins. Histochemical staining and thin-section electron microscopy reveal that the secreted glycoprotein, acid phosphatase, is contained within one of three distinct organelles that accumulates in different mutants: ER; Golgi-like structures called Berkeley bodies; and 80--100 nm vesicles. When produced at 37 degrees C, invertase and acid phosphatase have less carbohydrate in the mutants that accumulate ER than in other mutants, or than in the wild-type strain. External invertase migrates on SDS-polyacrylamide gels as a heterogeneous species with an apparent molecular weight of 100 to 140 kd. Radiolabeled invertase, immunoprecipitated from extracts of ER-accumulating mutant cells, migrates as a set of three discrete protein species with apparent molecular weights of 79, 81, and 83 kd; the other mutants produce a form more like the secreted enzyme. In each case, removal of N-glycosidically linked oligosaccharides by treatment with endoglycosidase H produces a discrete species that migrates as a protein of 61 kd. Immunochemical analysis of bulk glycoprotein accumulated in the mutants suggests that a major portion of the N-linked oligosaccharide, the outer chain, is added after material passes from the ER.
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PMID:Compartmentalized assembly of oligosaccharides on exported glycoproteins in yeast. 702 44

During the conversion of yeast cells to protoplasts, about half of the yeast chitinase was liberated into the medium, an indication that this portion of the enzyme is located in the periplasmic space. At least part of the remaining chitinase appears to be enclosed in vacuoles or in vesicle that co-purify with them, as indicated by a 14-fold enrichment of the enzymatic activity in a vacuole fraction isolated from a protoplast lysate. When protoplasts were incubated in growth medium, part of the chitinase was liberated in growth medium, part of the chitinase was liberated into the medium. It is concluded that yeast chitinase is a secretory enzyme, like invertase and acid phosphatase. The enzyme appears to be stored in vesicles as a prelude to its secretion into the periplasmic space. The possible function of yeast chitinase in cell division is discussed.
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PMID:Secretory character of yeast chitinase. 703 49

Utilization of sucrose as a source of carbon and energy in yeast (Saccharomyces) is controlled by the classical SUC genes, which confer the ability to produce the sucrose-degrading enzyme invertase (Mortimer and Hawthorne 1969). Mutants of S. cerevisiae strain S288C (SUC2+) unable to grow anaerobically on sucrose, but still able to use glucose, were isolated. Two major complementation groups were identified: twenty-four recessive mutations at the SUC2 locus (suc2-); and five recessive mutations defining a new locus, SNF1 (for sucrose nonfermenting), essential for sucrose utilization. Two minor complementation groups, each comprising a single member with a leaky sucrose-nonfermenting phenotype, were also identified. The Suc2 mutations isolated include four suppressible amber mutations and five mutations apparently exhibiting intragenic complementation; complementation analysis and mitotic mapping studies indicated that all of the suc2 mutations are alleles of a single gene. These results suggest that SUC2 encodes a protein, probably a dimer or multimer. No invertase activity was detected in suc2 probably a dimer or multimer. No invertase activity was detected in suc2 mutants,--The SNF1 locus is not tightly linked to SUC2. The snf1 mutations were found to be pleiotropic, preventing sucrose utilization by SUC2+ and SUC7+ strains, and also preventing utilization of galactose, maltose and several nonfermentable carbon sources. Although snf1 mutants thus display a petite phenotype, classic petite mutations do not interfere with utilization of sucrose, galactose or maltose. A common feature of all the carbon utilization systems affected by SNF1 is that all are regulated by glucose repression. The snf1 mutants were found to produce the constitutive nonglycosylated form of invertase, but failed to produce the glucose-repressible, glycosylated, secreted invertase. This failure cannot be attributed to a general defect in production of glycosylated and secreted proteins because synthesis of acid phosphatase, a glycosylated secreted protein not subject to glucose repression, was not affected by snf1 mutations. These findings suggest that the SNF1 locus is involved in the regulation of gene expression by glucose repression.
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PMID:Mutants of yeast defective in sucrose utilization. 704 Jan 63


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