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

---

Query: EC:2.4.99.6 (sialyltransferase)
1,546 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The effect of temperature on the activity of galactosyl- and sialyltransferases of rat liver Golgi membranes and the galactosyltransferase of serum has been studied. Arrhenius plots for three enzymes were different. Sharp breaks in the curves, indicative of phase transitions were observed for sialyltransferase (28 degree C) of Golgi and galactosyltransferase (34 degree C) of serum but not for galactosyltransferase of Golgi. The activation energy was greater above the break (above 28 degree C) than below for sialyltransferase of Golgi; The activation energy was lower (above 34 degree C) for galactosyltransferase of serum than below. Electron microscopic freeze replicas showed a patchy distribution of particles which increased as the temperature was raised accompanied by smooth areas. This was interpreted as representing lateral phase separation of the membrane components.
...
PMID:The effect of temperature on the galactosyl- and sialyltransferases and on the ultrastructure of Golgi membranes. 95 16

Levels of plasma sialyltransferase were measured in a patient with disseminated carcinoma of the testes. Initial enzyme values, elevated six fold above those in normal controls, were among the highest thus far encountered in a population of patients with various stages and types of malignancy. During a remarkable respose to chemotherapy with cis-diaminodichloroplatinum, plasma sialyltransferase levels fell markedly. Serial measurement of this enzyme may aid in evaluation of tumor responsiveness to therapy in patients whose disease is not readily measurable.
...
PMID:Alterations in plasma sialyltransferase associated with successful chemotherapy of a disseminated tumor. Case report. 99 Nov 25

Two variant mouse L cell lines (termed CL 3 and CL 6) have been selected for resistant to ricin, a galactose-binding lectin with potent cytotoxic activity. The resistant lines exhibit a 50 to 70% decrease in ricin binding and a 300- to 500-fold increase in resistance to the toxic effects of ricin. Crude membrane preparations of CL 3 cells have increased sialic acid content (200% of control), while the galactose, mannose, and hexosamine content is within normal limits. Both the glycoproteins and glycolipids of CL 3 cells have increased sialic acid, with the GM3:lactosylceramide ratios for parent L and CL 3 cells being 0.29 and 1.5, respectively. In contrast, the membranes of CL 6 cells have a decrease in sialic acid, galactose, and hexosamine content with mannose being normal. Both cell lines have specific alterations in glycosyltransferase activities which can account for the observed membrane sugar changes. CL 3 cells have increased CMP-sialic acid:glycoprotein sialyltransferase and GM3 synthetase activities, while CL 6 cells have decrease UDP-GlcNAc:glycoproteinN-acetylglucosaminyltransferase and DPU-galactose:glycoprotein galactosyltransferase activities. The increased sialic acid content of CL 3 cells serves to mask ricin binding sites, since neuraminidase treatment of this cell line restores ricin binding to essentially normal levels. However, the fact that neuraminidase-treated CL 3 cells are still 45-fold resistant to ricin indicates that either a special class of productive ricin binding sites is not being exposed or that the cell line has a second mechanism for ricin resistance.
...
PMID:Isolation and characterization of two mouse L cell lines resistant to the toxic lectin ricin. 100 11

Incubation of mouse thymocytes with mitogenic concentrations of concanavalin A causes a 2-fold increase in cell-surface-associated (but not total cell) sialyltransferase activity (ectosialyltransferase, CMP-N-acetylneuraminate:D-galactosyl-glycoprotein N-acetylneuraminyltransferase, EC 2.4.99.1) as judged by incorporation of [14C]sialic acid into endogenous cell acceptors and into added desialylated fetuin acceptor. The concanavalin-A-induced enhancement of enzymic activity is essentially complete within 1 hr after addition of mitogen and remains at elevated levels for 12 hr, declining rapidly thereafter. Intact cells labeled previously with [14C]sialic acid and then incubated briefly with hydrolytic enzymes, including neuraminidase and insoluble trypsin, released 43-66% of total cell-associated radioactivity without appreciably changing cell viability. Alterations in sialyltransferase activity due to concanavalin A treatment could not be explained by a mitogen-mediated (a) uptake of radioactive precursors, (b) cell death, (c) increased product catabolism, or (d) activation of sialyltransferase by mitogen binding to the enzyme. Furthermore, the process does not require active protein synthesis. The results are consistent with a rapid concanavalin-A-induced exposure of potential enzymic activity that was previously inaccessible to substrate.
...
PMID:Effect of concanavalin A on expression of cell surface sialyltransferase activity of mouse thymocytes. 108 27

The molecular basis for the accumulation of a substance which displays the immunological reactivity of alpha-1-antitrypsin within vesicles of liver parenchymal cells of individuals with hepatic cirrhosis and serum alpha-1-antitrypsin deficiency remains unclear. We recently reported that serum from a patient with alpha-1-antitrypsin deficiency and hepatic cirrhosis was substantially deficient in sialyltransferease (EC 2.4.99.1) an enzyme which transfers sialic acid from cytidine 5'-monophosphate-N-acetylneuraminic acid to a variety of asialoglycoprotein acceptors. In the present report we have extended these studies to include serum from five additional patients with alpha-1-antitrypsin deficiency and juvenile hepatic cirrhosis as well as a liver specimen obtained at autopsy of one of these patients. We find the sialytransferase activity in serum from six patients with alpha-1-antitrypsin deficiency and hepatic cirrhosis to be 50% of healthy pediatric control values and 30% of pediatric patients with liver disease. However, serum from family members homozygous for alpha-1-antitrypsin deficiency but without hepatic cirrhosis, and serum from patients with a variety of other kinds of liver disease, failed to exhibit the marked sialytransferase deficiency. Similar assays carried out on a homogenate of a liver sample from one patient with alpha-1-antitrypsin deficiency and hepatic cirrhosis indicated that the deficiency of sialyltransferase activity was not demonstrable in liver. Furthermore, a comparative kinetic analysis of serum and liver sialytransferase in normal and afflicted individuals failed to detect differences in substrate affinities which might account for a decrease in functional sialyltransferase capacity in individuals with alpha-1-antitrypsin deficiency and hepatic cirrhosis. These observations suggest that the serum sialyltransferase deficiency in such patients probably arises after chronic and extensive liver disease involving hepatic accumulation of alpha-1-antitrypsin rather than the enzyme deficiency being the primary cause of the hepatic cirrhosis and alpha-1-antitrypsin deficiency.
...
PMID:Cytidine-5'-monophosphate-N-acetylneuraminic acid. Asialoglycoprotein sialic acid transferase activity in liver and serum of patients with juvenile hepatic cirrhosis and alpha-1-antitrypsin deficiency. 108 50

alpha 1-Antitrypsin phenotypes Pi M and Z, purified by the thiol-disulfide exchange procedure, were desialylated by treatment with neuraminidase covalently coupled to Sepharose and used as acceptors of sialic acid in an assay system for serum sialic acid transferase (CMP-N-acetylneuraminate:D-galactosyl-glycoprotein N-acetylneuraminyltransferase, EC 2.4.99.1) activity. Both asialoantitrypsins were equally effective as acceptors in contrast to native Pi Z antitrypsin which did not accept any sialic acid. Serum sialyltransferase activity was determined in 38 adult alpha 1-antitrypsin deficient individuals (Pi Z, MZ, FZ, SZ) with normal liver function and was found to be of the same magnitude as the activity in normal individuals (Pi M). Equal activities were also found in 5 Pi Z patients with cirrhosis of the liver. The results strongly argue against the concept that sialyltransferase deficiency provides the molecular basis for alpha 1-antitrypsin deficiency.
...
PMID:The serum sialyltransferase activity in alpha 1-antitrypsin deficiency. 108 69

Membrane-associated sialyltransferase complexes in Escherichia coli K-235 can be dissociated by lipid deletion and reassembled by the addition of undecaprenyl phosphate, a unique membrane-bound lipid coenzyme. Following disruption of the cells by pressure disintegration and centrifugal fractionation, the sialyltransferase activity is assocatied with both a "particulate" and "soluble" complex. Kinetic studies as well as sugar nucleotide, metal ion, pH, ammonium sulfate, and thiol reagent requirements showed these two complexes contained functionally identical enzymatic activities. Isopycnic sucrose density gradient centrifugation studies carried out on unfractionated total membranes established that these sialytransferase activities were associated with membrane hybrids composed of different relative amounts of inner and outer membranes. Enzyme localization studies employing DPNH oxidase, a marker for the inner membrane, and relative phospholipid to protein composition determinations in the two complexes, provided added support for this conclusion. Sialyl polymer synthesis was not dependent on the incorporation of other monosaccharides and had no demonstrable metal ion requirement. Kinetic studies showed that the Km for cytidine 5-monophospho-N-acetylneuraminic acid in intact soluble and particulate enzyme preparations was 8.1 times 10-5M and 9.2 times 105M, respectively. Similarly, both enzyme complexes had nearly identical Vmax values. Following reassembly of delipidated enzyme preparations, however, there was a 10-fold increase in the Km value for the particulate enzyme and a 3-fold increase for the soluble enzyme. This increase was accompanied by an increase of approximately the same magnitude in the Vmax values. Since the lipid coenzyme was limiting in intact enzyme preparations, the increase in Vmax reflected an increase in the concentration of the active lipid in reconstituted complexes. Sialyl polymer synthesis in intact membrane preparations was stimulated by the exogenous addition of lipid. Insertion of the carrier lipid was dependent on temperature. At 37 degrees, a 120% increase in sialytransferase activity was observed while only a 35% increase was observed at 30 percent. At 20 degrees, no stimulation occurred. Fluidity of the lipid phase is apparently required for proper function of this membraneassociated enzyme complex. Thus, at 20 degrees, a temperature below the membrane lipid transition temperature, the lipids are relatively immobile.
...
PMID:Properties of membrane-associated sialyltransferase of Escherichia coli. 109 67

Iodine incorporation into thyroglobulin is known to occur within the lumen of the thyroid follicle. Since incorporation of sialic acid, which occupies a terminal position in the oligosaccharide chains, is also a later event in thyroglobulin synthesis, the possibility that sialic acid might be incorporated after thyroglobulin secretion was investigated. In one experimental approach normal rat thyroid hemilobes were incubated with radioactive precursors. Thyroglobulin, analyzed by equilibrium centrifugation in RbCl, had a median density which varied according to the moiety labeled in the following increasing order: leucine smaller than galactose smaller than sialic acid smaller than iodine. The molecules having the highest density were labeled only with iodine. In the second approach, thyroid hemilobes were taken from rats treated with cycloheximide for 16 hours to stop protein synthesis and allow nascent molecules to be secreted, and incorporation of precursors into thyroglobulin was analyzed by sucrose gradient centrifugation. Leucine incorporation was 6% of control but the amino acid was found in the NH2-terminal position. N-Acetylmannosamine (sialic acid precursor) and galactose incorporation were also completely inhibited whereas iodine incorporation was 10% of control. Incorporation was not restored by thyrotropin treatment, and the sialyltransferase and iodination systems were reduced only to 50 to 70% of control. The results indicate that sialic acid is incorporated only in nascent thyroglobulin and not in thyroglobulin molecules already secreted into the follicular lumen. A large fraction of the iodine incorporation also seems to occur in newly synthesized thyroglobulin.
...
PMID:The site of sialic acid incorporation into thyroglobulin in the thyroid gland. 111 19

Glycosyltransferase enzymes were measured in homogenates of normal and neoplastic colon epithelium. The levels for exogenous galactosyltransferase and fucosyltransferase and endogenous N-acetylglucosaminyl-transferase were higher in the normal tissue. The levels for exogenous and endogenous sialyltransferase and endogenous galactosyltransferase and fucosyltransferase were comparable in the homogenates of normal and cancer cells. Incorporation of fucose and galactose into purified carcinoembryonic antigen (CEA), used as an exogenous acceptor by colon glycosyltransferases, was demonstrated by immunoprecipitation with rabbit antiserum to human CEA. The normal fucosyltransferase and galactosyltransferase showed higher activity with CEA than did the tumor enzymes.
...
PMID:Alterations in glycosyltransferase activity in human colon cancer. 111 12

Incubation of HeLa cells in the presence of millimolar concentrations of propionate, butyrate, or pentanoate increases the specific activity of CMP-sialic acid:lactosylceramide sialyltransferase 7-20-fold within 24 h. Longer-chain saturated fatty acids or acetate are much less effective, decanoate showing no induction. Unsaturated fatty acid analogs of butyrate and other compounds are ineffective. Only the three most effective compounds also produce characteristic smooth extended cell processes in HeLa cells. Butyrate (5 mM) induces the sialyltransferase after a 4-h lag, producing maximum specific activity by 24 h. The amount of sialyl-lactosylceramide, the glycolipid product of the enzyme, increases during that time 3.5 times more than in control cultures. No other glycosphingolipid enzyme is significantly altered by butyrate exposure. The cellular shape changes occur 2-3 h later than the increase of sialyltransferase activity, and both processes require the continuous presence of inducer and the synthesis of RNA and protein but not the synthesis of DNA or the presence of serum.
...
PMID:Morphological alterations and ganglioside sialyltransferase activity induced by small fatty acids in HeLa cells. 114 84


<< Previous 1 2 3 4 5 6 7 8 9 10 Next >>

---