Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:3.1.3.1 (alkaline phosphatase)
 47,916 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Cytoplasmic extracts of interferon-treated primary chick embryo cells contain an enzyme activity that synthesized an inhibitor of chick cell-free protein synthesis. The same activity was detected in extracts of cells treated with mock preparations of interferon, but at <0.3% of the level found in interferon-treated cell extracts. The enzyme was activated by double-stranded RNA and could be isolated by binding to columns of poly(I)-poly(C)-agarose. In the column-bound state, the enzyme reacted with ATP to synthesize the inhibitor, which could then be continuously eluted from the column. The inhibitor was purified and its structure and function were compared with those of the low molecular weight inhibitor of protein synthesis made by an enzyme from interferon-treated mouse L cells. The avian and mammalian inhibitors comigrated on thin layers of polyethyleneimine-cellulose during chromatography in three different solvent systems, and they coeluted as a series of peaks from columns of DEAE-cellulose during sodium chloride gradient elution. Digestion with bacterial alkaline phosphatase or snake venom phosphodiesterase yielded products that similarly comigrated. Functionally, the two inhibitors were interchangeable: both inhibited protein synthesis in extracts of mammalian and avian cells, producing 50% inhibition at a concentration of about 0.3 nM (AMP equivalents). We conclude that the chick cell-derived oligonucleotide inhibitor has a structure that is closely related or identical to that of the inhibitor made in the mouse system, and that both preparations inhibit cell-free protein synthesis in a non-species-specific manner.
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PMID:Oligonucleotide inhibitor of protein synthesis made in extracts of interferon-treated chick embryo cells: comparison with the mouse low molecular weight inhibitor. 27 8

To identify the factors which control glycogen synthesis in Saccharomyces cerevisiae, we have studied the regulation of glycogen metabolism during sporulation, since in vivo glycogen has been reported to undergo significant changes in concentration during this process. We examined the concentration of a number of key glycolytic intermediates and enzymes in strains that sporulate at different rates and those that are deficient in sporulation. There were no significant changes found in the adenylate energy charge or cyclic AMP levels throughout sporulation. Although significant alterations occurred in the levels of glucose-6-phosphate, fructose-6-phosphate, fructose-1,6-bisphosphate, phosphoenolpyruvate, and ATP during sporulation, only the fourfold increase in fructose-1,6-bisphosphate appeared to correlate with glycogen synthesis in all of the strains examined. Only limited changes occurred in the level of a number of glycolytic and gluconeogenic enzymes which were examined during this process. Intracellular glucose content underwent a dramatic 30- to 40-fold increase in sporulating cells. Comparison of strains with different rates of sporulation demonstrated that this increase in glucose content coincides with the time of glycogen degradation in each strain. Both the increase in glucose content and the degradation of accumulated glycogen were not observed in nonsporulating alpha/alpha strains, or in cells incubated in NH(4) (+) supplemented sporulation medium. Although glucose appears to be the direct product of glycogen degradation, a 10-fold increase in a nonspecific alkaline phosphatase occurs at this time, which may be degrading phosphorylated sugars to glucose. All of the strains examined released extracellular glucose while suspended in acetate sporulation medium. It is concluded that most of the changes in the glycolytic pathway that occur during sporulation, with the exception of glycogen degradation and the concomitant increase in intracellular glucose pools, are a response to the transfer to sporulation medium and are independent of sporulation-specific processes. Inhibition of sporulation with ammonium ions resulted in a different pattern of change in all of the glycolytic intermediates examined, including a twofold increase in cyclic AMP levels. Ammonia did not interfere with glycogen synthesis, but prevented sporulation-specific glycogen degradation. The levels of the glycolytic enzymes examined were not affected by ammonia.
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PMID:Relationship of glycolytic intermediates, glycolytic enzymes, and ammonia to glycogen metabolism during sporulation in the yeast Saccharomyces cerevisiae. 36 17

Searching for a physiological role of T4 RNA ligase [polyribonucleotide synthetase (ATP); poly(ribonucleotide):poly(ribonucleotide) ligase (AMP-forming), EC 6.5.1.3] activity, we developed an acellular system of plasmolyzed Escherichia coli cells infected by T4 bacteriophage. Upon incubation of this system with [gamma-32P]ATP, 32P was transferred into a large number of polyribonucleotides, mostly up to 300-400 residues long. The bulk of 32P in the product polyribonucleotides was found in 5'-terminal phosphate groups, suggesting that they originated by a phosphorylation reaction catalyzed by the endogenous polynucleotide kinase (EC 2.7.1.78). Indeed, these products were not seen in an acellular system from uninfected cells, and their amount and complexity increased with the progress of infection. Analysis of the 32P-labeled polyribonucleotide products by gel electrophoresis, either before or after digestion with alkaline phosphatase (EC 3.1.3.1), revealed that a small fraction of the 32P resided in phosphodiester bonds of several tRNA-sized chains. This specific 32P transfer from [gamma-32P]ATP into phosphodiester bonds was apparently catalyzed by successive polynucleotide kinase and RNA ligase reactions. The possible relationship of the 32P transfer to RNA ligase was investigated next by using a system from cells infected with T4 am M69 (an amber mutant deficient in RNA ligase). Transfer of 32P from [gamma-32P]ATP into phosphodiester bonds was not detected in the am M69 system. However, addition of purified RNA ligase to the am M69 system restored the specific 32P transfer. A system from cells infected with T4 psu-b delta 33 (a deletion mutant lacking the entire tRNA region) sustained the specific 32P transfer into tRNA-sized products, indicating that they were not derived from transcripts of T4 tRNA genes. These data may reflect a role of RNA ligase in posttranscriptional conversion of presumably host polyribonucleotides into novel tRNA species during T4 infection.
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PMID:RNA ligase reaction products in plasmolyzed Escherichia coli cells infected by T4 bacteriophage. 39 2

The induction of beta-galactosidase and alkaline phosphatase by the nucleoid of Escherichia coli was studied. Only the membrane-associated form was active in the presence of S 30. The induction of beta-galactosidase showed an absolute requirement for the inducer and was enhanced by cyclic AMP and cyclic GMP. Further-more, in our hands, the synthetic activity of the membrane-associated nucleoid proved to be far higher than that of the soluble system described by Zubay. Our results suggest that membrane shield the structure which is necessary for the integrity of the initiation step of both transcription and translation.
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PMID:[Synthesis of specific proteins by the nucleoid of Escherichia coli]. 40 27

Treatment of cultured fibroblasts from patients with unbalanced chromosomal aberrations with a mixture of isoproterenol, theophylline and ascorbic acid resulted after 48 hours in an at least three-fold increase of alkaline phosphatase activity on a per cell basis, whereas cells from normal healthy individuals did not show this dramatic response. Cells were studied from patients with trisomy 21 (14 cases), trisomy 18 (3 cases), trisomy 13 (1 case), pentasomy X (1 case), Turner syndrome (2 cases), and Klinefelter syndrome (1 case), and no exception was noted. The mechanism of this phenomenon is not clear, but it is speculated that increased cyclic-AMP levels caused by the action of isoproterenol on adenylcyclase may account for excessive reactions of unbalanced cells as compared to normal cells. This simple biochemical diagnostic procedure might become useful in screening programs for unbalanced chromosomal abberations.
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PMID:High alkaline phosphatase activity in isoproterenol stimulated fibroblast cultures from patients with numerically unbalanced chromosomal aberrations. 46 48

The membrane glycoprotein enzyme, alkaline phosphatase was induced in cultured human fibroblasts by dibutyryl cyclic AMP, sodium butyrate, the serum glycoprotein fetuin, the Tamm-Horsfall urinary glycoprotein, and by a number of inhibitors of DNA synthesis. The uninduced basal enzyme activity increased at later stages of growth when the cells became confluent. Induction by dibutyryl cyclic AMP or fetuin was most effective when the agents were added after the cells had reached stationary phase and was maximal after at least two days of exposure. The levels of induction resulting from the addition of pairs of the agents, dibutyryl cyclic AMP, n-butyrate and fetuin were additive indicating that these have different modes of action. The inhibitors of DNA synthesis, cytosine arabinoside, hydroxyurea, and methothrexate were less effective inducers. Bromodeoxyuridine which also has non-DNA mediated effects induced to the same extent as dibutyryl cyclic AMP. Similar experiments with sex- and age-matched cell strains derived from patients with cystic fibrosis failed to detect differences in the levels of induction from those observed in normal cells. In addition, the combined inductive effects of Tamm-Horsfall glycoprotein, isoproterenol and theophylline, were similar with normal and cystic fibrosis cells.
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PMID:Induction of alkaline phosphatase in cultured human fibroblasts. Comparison of normal cells and those from patients with cystic fibrosis. 48 38

The safety and effectiveness of sodium cellulose phosphate (SCP) in the treatment of calcium urolithiasis of absorptive hypercalciuria was explored. Eighteen patients with absorptive hypercalciuria with intestinal hyperabsorption of calcium, normal or suppressed parathyroid function, and active stone disease received 10 to 15 Gm SCP daily (2.5 to 5 Gm with meals) and 2 to 3 Gm magnesium gluconate daily (1 to 1.5 Gm twice daily orally separately from SCP) for eight to 54 months, while maintained on a moderate calcium and oxalate restriction. During treatment, serum calcium, immunoreactive parathyroid hormone, and urinary cyclic AMP remained within the normal range. Serum alkaline phosphatase and bone density (measured by photon absorptiometry) did not change significantly or remained within normal limits. Serum concentrations of magnesium, copper, zinc, and iron and blood hematocrit were not significantly altered by therapy. However, urinary calcium returned toward normal, and incidence of renal stone formation markedly decreased. The results suggest that SCP is a safe and an effective drug for absorptive hypercalciuria.
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PMID:Clinical pharmacology of sodium cellulose phosphate. 48 64

After partial hepatoectomy of the rat normal liver a maximum three-fold increase in the activity of alkaline phosphatase is observed in the blood serum, on the second-third day, and by the 14th day becomes almost normal; the activity of adenosine desaminase, AMP-aminohydrolase and 5'-nucleotidase becomes 30-60% as high for one-two days. The activity of the alkaline phosphatase in the liver becomes four times as high and reaches normalcy by the sixth day. The activity of adenosine desaminase and AMP-aminohydrolase increases to a less extent for a fortnight. The activity of 5'-nucleotidase decreases in the first day, then rises and a fortnight later becomes normal. After partial hepatoectomy of the liver injured with deoxicholic acid the activity of all the enzymes in blood serum anr a longer period of time; in the 5'-nucleotidase activity there is no initial drop and its earlier subsequent increase is observed.
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PMID:[Enzyme activity in the regeneration process after partial hepatectomy of normal liver and that injured with deoxycholic acid]. 66 48

Activity of alanine and aspartate aminotransferase, alkaline phosphatase, adenosine, desaminase and AMP-aminohydrolase was determined in rats in the process of the liver regeneration under acute and chronic lesion with CCl4. It is shown that under chronic lesion of the liver with CCl4, in contrast to the acute one, changes in the aminotransferase activity in blood serum are not expressed in the liver, the activity is essentially decreased. A steady increase was observed in the activity of adenosine desaminase, AMP-aminohydrolase and alkaline phosphatase in the liver and blood serum. It is concluded that the normal regenerative process is accompanied by short-term shifts of the enzymes activity in the liver and blood serum. The development of a chronic process results in a characteristic increase in the activity of adenosine desaminase, AMP-aminohydrolase and alkaline phosphatase in the liver and blood serum.
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PMID:[Enzyme activity during regeneration under acute and chronic liver lesion with CCL4]. 68 74

In an 18-year-old boy with Bartter's syndrome, hypophosphatemia was discovered (2.4 mg/100 ml) with normal serum calcium concentration (9.7 mg/100 ml) and elevated alkaline phosphatase level: 528 mU/ml (normal less than or equal to 150). Skeleton X-rays showed osteomalacia on the pelvic bones and metaphyseal rickets on the wrists. Plasma 25-hydroxycholecalciferol (25-OHCC) concentration was 7.2 ng/ml (normal = 13 +/- 4.4), and serum immunoreactive parathyroid hormone (iPTH) concentration 160 micron1Eq/ml (normal less than or equal to 150). Ca infusion (1500 mg/m2/12 h) induced an increase in serum P level to 3.2 mg/100 ml, in tubular phosphate reabsorption from 72 to 90%, while serum iPTH decreased to 33 micron1Eq/ml. Vitamin D2 administration (45 mg) resulted in increased 25-OHCC concentration to 28 ng/ml and in healing of pelvic osteomalacia. However, there was little change of the radiological aspect of the wrist and of serum phosphorus and iPTH concentrations. In a control 6-year-old hypokalemic girl, administration of parathyroid hormone (8 USP/kg) produced a marked phosphaturic response and an increase in urinary cyclic AMP excretion. These data suggest that hypophosphatemia can be attributed to secondary hyperparathyroidism in the patient with Bartter's syndrome. Hypokalemia does not impair the renal activity of parathyroid hormone.
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PMID:Hypophosphatemia and hyperparathyroidism in a case of Bartter's syndrome. 71 93


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