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)

Nucleic acid synthesis in tissues of rapid growth is preferentially done using dietary purines and pyrimidines via the salvage pathway. In the case of a low protein intake, dietary nucleotides may be semiessential for cell replication of gut, lymphocytes, and bone marrow, and especially in those intestinal diseases in which the mucosa is altered, dietary nucleotides may have a role in intestinal development. The effect of dietary nucleotides on intestinal weight and length, gut mucosal weight, intestinal protein and DNA contents, and lactase, maltase, and intestinal mucosal activities was assessed in a controlled way. Weanling (21-day-old) rats were separated into two groups of 36, each receiving blindly a basal diet containing glucose polymers (C) or a basal diet with lactose as the main carbohydrate (L) for 15 days. Those fed with L developed a syndrome of chronic diarrhea and malnutrition. Ten rats of each group were sacrificed at that time. The rest of the animals of each group were separated into two subgroups. The first was fed with the C diet and the second with the C diet supplemented with 50 mg/100 g of each of the following nucleotides: AMP, GMP, CMP, UMP, and IMP (CN). Thus the subgroups CC, CN, LC, and LN were formed. Rats were sacrificed after 4 weeks and gut separated into three segments corresponding to duodenum, jejunum, and ileum. Analysis of variance was used to compare the effect of diet or segments. DNA and lactase, maltase, and sucrase activities increased in the LN group with respect to LC especially in jejunum and ileum but there were not any differences between CC and CN.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Effect of dietary nucleotides on intestinal repair in rats with experimental chronic diarrhea. 212 43

To investigate further the pathophysiology of rotavirus-induced diarrhea, changes in specific activities of eight relevant intestinal enzymes [alkaline phosphatase, thymidine kinase, lactase, maltase, sucrase, Na+,K+-adenosine triphosphatase (ATPase), adenylate and guanylate cyclases] were measured following infection of suckling mice with murine rotavirus (epizootic diarrhea of infant mouse strain) and compared with age-matched control mice. The concentration of lactose within the lumen of the gastrointestinal tract during infection was also measured. During the course of infection, activities of alkaline phosphatase and lactase decreased, whilst the activity of thymidine kinase increased. Precocious maturation profiles of sucrase and maltase enzymes were observed. No significant changes were detected in the activities of Na+,K+-ATPase or the adenylate and guanylate cyclases. These results are discussed in relation to existing and novel hypotheses on the pathogenesis of rotavirus-induced diarrhea.
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PMID:Intestinal enzyme profiles in normal and rotavirus-infected mice. 289 74

Binding sites for horseradish peroxidase (HRP), with unusual properties, were detected on the surface of cultured and isolated cells after the cells (on cover slips) had been quickly dried, fixed in cold methanol, and post-fixed in a paraformaldehyde solution. The reaction for surface-bound HRP was suppressed by micromolar concentrations of glycoproteins such as invertase, equine luteinizing hormone (eLH) or human chorionic gonadotropin (hCG). The reaction was also suppressed by 20 mM CDP, UDP, GTP, NAD, and ribose 5-phosphate. Two to six times higher concentrations of GMP, fructose 1-phosphate, galactose 6-phosphate, mannose 6-phosphate, fructose 6-phosphate, and glucose 6-phosphate were required to suppress the binding reaction. AMP, ATP, heparin, mannan, and eight non-phosphorylated sugars showed relatively low competing potencies but fucoidin and alpha-lactalbumin were strong inhibitors. No addition of Ca2+ was required for the binding of HRP to the cell surface. However, calcium-depleted, inactive HRP did not compete with the binding of native (calcium-containing) HRP whereas H2O2-inactivated HRP suppressed the binding. GTP, NAD, ribose 5-phosphate, and EGTA accelerated the release of previously-bound HRP from the cell surface whereas glycoproteins (invertase, eLH, and hCG) did not do so. Addition of Ca2+ to GTP, NAD, ribose 5-phosphate or to EGTA prevented the accelerated release of HRP from the cell surface. It is suggested that calcium, present either in the surface membrane or in HRP itself, is involved in the binding of HRP to the cell surface and in the inhibition of binding by GTP, NAD, and ribose 5-phosphate. It is also suggested that alpha-lactalbumin, GTP, UDP, and CDP compete with the binding of HRP to a glycosyltransferase on the cell surface.
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PMID:Unusual binding sites for horseradish peroxidase on the surface of cultured and isolated mammalian cells. Suppression of binding by certain nucleotides and glycoproteins, and a role for calcium. 309 11

Current models for nucleotide sugar use in the Golgi apparatus predict a critical role for the lumenal nucleoside diphosphatase. After transfer of sugars to endogenous macromolecular acceptors, the enzyme converts nucleoside diphosphates to nucleoside monophosphates which in turn exit the Golgi lumen in a coupled antiporter reaction, allowing entry of additional nucleotide sugar from the cytosol. To test this model, we cloned the gene for the S. cerevisiae guanosine diphosphatase and constructed a null mutation. This mutation should reduce the concentrations of GDP-mannose and GMP and increase the concentration of GDP in the Golgi lumen. The alterations should in turn decrease mannosylation of proteins and lipids in this compartment. In fact, we found a partial block in O- and N-glycosylation of proteins such as chitinase and carboxypeptidase Y and underglycosylation of invertase. In addition, mannosylinositolphosphorylceramide levels were drastically reduced.
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PMID:Guanosine diphosphatase is required for protein and sphingolipid glycosylation in the Golgi lumen of Saccharomyces cerevisiae. 839 37

To determine the nutritional role of nucleotides, the in vitro and in vivo effects of exogenous nucleotides on the development of intestine were investigated. First, the in vitro effects of nucleotides on the proliferation and maturation of enterocytes were studied by using a human colon tumor cell line (Caco-2) and a rat normal small intestinal crypt cell line (IEC-6). Second, the in vivo effects of nucleotides were also studied in early weaned rats fed nucleotide-unsupplemented or high-nucleotide-supplemented diet. Nucleotide composition resembled that of human milk (CMP:UMP:AMP:IMP:GMP = 10:1:1:1:1, in weight). Nucleotide supplement did not enhance Caco-2 cells proliferation; however, it significantly enhanced maltase and sucrase activities. In contrast, nucleotides supplement enhanced ICE-6 cells proliferation and maltase activity. CMP, predominantly contained in the mixture, enhanced most effectively the proliferation and maturation of cells. In the in vivo experiment, nucleotides significantly enhanced sucrase activity in the intestinal mucosa of early weaned rats. The results presented here suggest that a nucleotide supplement may enhance enterocyte proliferation and/or maturation in vivo and in vitro. Therefore exogenous nucleotides may play an important role in the development of the intestine.
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PMID:In vitro and in vivo effects of exogenous nucleotides on the proliferation and maturation of intestinal epithelial cells. 1036 Feb 45

The distinct biosynthesis pathways for microbial exopolysaccharide production provide different engineering strategies to tailor the chemical structures of the final polymers. This review focuses on the latest insights in the various pathways and identifies bottlenecks as well as promising targets for tailoring microbial polysaccharide production. The main engineering strategies includes the combinatorial assembly of glycosyltransferases and engineering of the Wzx and Wzy proteins for flipping of repeating units as well as polymerization. In the case of synthase based polysaccharides, the use of epimerases or engineering approaches of the synthase itself as well as overexpression of c-di-GMP levels is identified as one of the most promising strategies. For sucrase-based biosynthesis, the in vitro production by engineered sucrase enzymes or adjusted production conditions is shown as a very promising method.
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PMID:Recent insights in microbial exopolysaccharide biosynthesis and engineering strategies. 2936 63