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

In a random, controlled study of very low birth weight (VLBW) infants from 3 to 8 weeks of age, 17 infants were fed soy isolate formula supplemented with calcium (92 mg/kg/day), phosphorus (44 mg/kg/day), and vitamin D (500 IU/kg/day), and 15 were fed a new whey-predominant, low osmolality formula designed for small preterm infants. Mean birth weight (1,206 g, SD 178) and gestational age (30 weeks, SD 1.9) of the soy-fed group were not significantly different from the whey formula group (1,143 g, SD 158, and 30 weeks, SD 1.8, respectively). Caloric and protein intakes were not different between the formula groups throughout the study period. However, mean weight gain in g/kg/day was significantly greater for the whey formula group: 15.3 g, SD 2.5, vs. 11.3 g, SD 2.3, p less than 0.0001. Serum protein and albumin were higher in the whey formula-fed group during the latter 2 weeks of the study (p less than 0.05). The incidence of vomiting, gastric residual, abdominal distension, diarrhea, and constipation was low and not different between the two groups. No infant developed necrotizing enterocolitis. Serum calcium, phosphorus, alkaline phosphatase, 25-hydroxy vitamin D and parathyroid hormone were similar in both groups, and no infant developed radiographic evidence of rickets. Although soy isolate formula supplemented with calcium, phosphorus, and vitamin D was not associated with rickets, no fewer complications were observed with this lactose-free, low solute formula.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Comparison of calcium- and phosphorus-supplemented soy isolate formula with whey-predominant premature formula in very low birth weight infants. 633 95

A phoA-lacZ gene fusion was used to isolate mutants altered in the alkaline phosphatase signal sequence. This was done by selecting Lac+ mutants from a phoA-lacZ fusion strain that produces a membrane-bound hybrid protein and is unable to grow on lactose. Two such mutant derivatives were characterized. The mutations lie within the phoA portion of the fused gene and cause internalization of the hybrid protein. When the mutations were genetically recombined into an otherwise wild-type phoA gene, they interfered with export of alkaline phosphatase to the periplasm. The mutant alkaline phosphatase protein was found instead in the cytoplasm in precursor form. DNA sequence analysis demonstrated that both mutations lead to amino acid alterations in the signal sequence of alkaline phosphatase.
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PMID:Mutations that alter the signal sequence of alkaline phosphatase in Escherichia coli. 633 78

Using recombinant DNA techniques, we have constructed phoA-lacZ gene fusions. Two of the fusions encode hybrid proteins containing approximately half of alkaline phosphatase at the amino terminus joined to beta-galactosidase. For the one fusion strain analyzed in detail, it was shown that the hybrid protein is found in the membrane fraction of cells. In its membrane location, the beta-galactosidase activity of the hybrid is not sufficient to support cell growth on lactose. Unexpectedly, fusions containing phoA and lacZ joined in the wrong translational reading frame were also obtained. These fusions direct the phosphate-regulated synthesis of beta-galactosidase, apparently via a translation restart mechanism. Thus, when gene fusions are constructed, the presence of properly regulated beta-galactosidase activity does not necessarily indicate that a hybrid protein is being produced.
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PMID:In vitro construction and characterization of phoA-lacZ gene fusions in Escherichia coli. 640 7

Late results of Billroth I (BI) partial gastrectomy for peptic ulcer in 19 patients were compared with those in 19 patients who had undergone Billroth II (B II) operation. The groups were matched for age and sex and were re-examined 21 to 27 years postoperatively. The study included notation of abdominal symptoms and haematologic status and tests of calcium metabolism with serum D-vitamin concentrations [S-25(OH)D2 and S-25(OH)D3], A-vitamin absorption, lactose and d-xylose tolerance and barium meal transit time to assess intestinal function, gastroscopy with biopsies, and measurement of bone mineral density, using the 241Am gamma ray attenuation method. In the paired comparisons of B I and B II patients, no significant difference was found in haematologic status or results of intestinal function tests. The serum alkaline phosphatase activity was significantly higher after B II than after B I, whereas S-25(OH)D2 and S-25(OH)D3 were significantly higher in the B I group. Other data for calcium metabolism showed no significant intergroup difference. Bone mineral density likewise was not significantly different in the two groups, but in both of them the values were significantly lower than in healthy control subjects. Most patients in both Billroth groups had atrophic mucosal gastritis.
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PMID:Long-term follow-up after Billroth I and II partial gastrectomy. Gastrointestinal tract function and changes in bone metabolism. 649 79

The calmodulin content of heat-treated extracts of rat mammary tissue and isolated cells was measured by using stimulation of cyclic nucleotide phosphodiesterase (PDE) activity and radioimmunoassay (r.i.a.) procedures. The calmodulin content of mammary tissue increased 2.5-fold near the time of parturition, remained at the elevated level during lactation, then, after the onset of involution, decreased to values similar to those measured from mammary tissue of pregnant rats. When tissue from 15 animals in different stages of pregnancy, lactation and involution were compared, the r.i.a. gave 2.6-fold higher results than the PDE assay. To investigate further the increase in calmodulin content of mammary tissue, secretory and myoepithelial cells were enzymically dissociated from rat mammary tissue during different stages of pregnancy, lactation and involution. Protein, DNA, lactose, glucose-6-phosphate dehydrogenase and alkaline phosphatase were assayed to characterize the cell fractions. By using r.i.a., the calmodulin content per mg of protein in isolated secretory-cell fractions was high near parturition, then decreased and remained relatively constant during lactation. The amount of calmodulin expressed per mg of DNA in secretory cells did not show a marked change near parturition, suggesting a constant amount of calmodulin per cell. The calmodulin content of myoepithelial cells dissociated from mammary tissue and measured by using r.i.a. was 6-fold lower than in secretory cells and remained relatively constant during the course of lactation. The changing levels of calmodulin in rat mammary tissue during development are suggested to be related to proliferation and destruction of secretory epithelial cells, events that occur near parturition and involution respectively.
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PMID:Calmodulin content of rat mammary tissue and isolated cells during pregnancy and lactation. 674 53

A hybrid beta-galactosidase molecule containing a substantial portion of the amino-terminal sequence of the maltose-binding protein is inserted in the cytoplasmic membrane of E. coli; in this location, the protein has very low enzymatic activity. The strain producing it is, therefore, Lac-. Selection for derivatives of the fusion strain that are able to grow on lactose yields mutants in which the hybrid protein has become cytoplasmic, and thus has higher enzymatic activity. Among such derivatives, we have isolated a temperature-sensitive conditional lethal mutant that accumulates the precursor of the maltose-binding protein in the cytoplasm, and also accumulates precursors of alkaline phosphatase, lambda receptor protein and the ompF gene gene product. A number of periplasmic proteins are, however, properly localized at the nonpermissive temperature. The temperature-sensitive lesion has been genetically mapped to 2.5 min on the E. coli map, within or near a cluster of genes responsible for cell division and septation. The principle behind the genetic selection employed here should be useful in obtaining other secretion mutants to characterize the cell's secretion machinery.
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PMID:E. coli mutant pleiotropically defective in the export of secreted proteins. 702 50

Escherichia coli K-12 mutants showing reduced alkaline phosphatase activity were isolated as 5-fluorouracil-plus-adenosine-resistant derivatives of a upp pho (either phoS or phoT) strain. One class of these mutants displayed a temperature-sensitive alkaline phosphatase-negative phenotype, a pleiotropic defect for growth on some substrates, an increased sensitivity to toxic compounds (e.g., EDTA, mitomycin, and chloramphenicol), and alterations in the expression of some membrane proteins. It phenotypically differed from previously described mutants. The mutation was located at min 8.5 close to the phoA gene and defines a new genetic locus we called napA (for negative alkaline phosphatase pleiotropic phenotype). As these mutants have lost the ability to grow on lactose and galactose, Lac+ and Gal+ revertants were isolated that simultaneously recovered the parental phenotype.
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PMID:New pleiotropic alkaline phosphatase-negative mutants of Escherichia coli K-12. 704 92

From the age of 3 months, six groups of rats consisting of six animals each were fed one of three types of diet with either 15% lactose or dextrose. The diets used were a control diet containing 0.6% calcium and 0.45% phosphorus and two high-phosphorus (1.3%) diets with either a normal (0.6%) or a low (0.2%) calcium content. Whereas calcium retention and femur mass appeared to be unaffected, feeding the high-phosphorus diets resulted in significant (P less than or equal to 0.05 or P less than or equal to 0.01) biochemical changes including: decreased plasma phosphorus almost throughout the whole of the study; increased plasma alkaline phosphatase, and urinary total hydroxyproline after 17 and 42 weeks; nephrocalcinosis; depressed urinary calcium, and reduced femur density. With the excretion of nephrocalcinosis and depressed urinary calcium, these changes were more marked if the calcium content of the diet was low than when it was normal, and this difference was associated with a significant (P less than 0.01) inhibiting effect of dietary calcium on the intestinal absorption and urinary excretion of phosphorus. Although lactose, as compared with dextrose, significantly (P less than 0.01) improved the intestinal absorption and retention of calcium during body weight gain, which was reflected by an increased femur mass after 42 weeks, this sugar did not reduce the detrimental effects on bone and soft tissue resulting from feeding the high-phosphorus diets. The results of the study in line with the induction of nutritional secondary hyperparathyroidism and increased bone turnover in rats fed high-phosphorus diets and indicate that lactose-stimulated calcium absorption will not prevent or diminish the biochemical changes associated with this disease; the results also stress the significance of the calcium content of the diet as a factor that may protect the body against excessive dietary phosphorus.
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PMID:Nutritional interrelationships between calcium, phosphorus and lactose in rats. 738 83

Two trials were conducted to determine the effect of lactose on performance, bone integrity and certain blood constituents in postweaning rats and swine. The effect of lactose on calcium and phosphorus and percentage ash content of the small intestine was also determined. In both trials, average daily gains were not influenced by the feeding of diets containing 30% lactose. Feed conversion was depressed in both rats and pigs when 30% lactose was fed. Transitory diarrhea was observed in rats fed 30% lactose, but not in swine. In the rat trial, no significant differences due to treatment were observed for serum Ca of P, but a linear increase (P < .01) in alkaline phosphatase was observed as lactose increased in the diet. Analysis of blood constituents from multiple bleedings during the pig trial showed that in the first 2 weeks, alkaline phosphatase was increased (P < .01) in pigs fed lactose and slightly decreased in those not fed lactose. Lactose affected the change in serum Ca for 0 to 10 weeks (P < .05) as indicated by a marked reduction in serum Ca of pigs not fed lactose and a slight increase for those fed lactoss. Serum calcium decreased in the absence of lactose but increased in the presence of lactose (P < .05) in pigs fed .4% Ca diets. In both trials, breaking strength parameters (peak force and stress) were not affected by dietary lactose. Bones from pigs fed no lactose had a higher stress to strain ratio (P < .05) than those from pigs fed lactose. In the rat trial, stress to strain ratio was variable across all treatments. Percentage of bone ash increased (P < .01) as lactose increased in the diet. Dietary treatments did not affect the mineral content of specific gut segments.
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PMID:Effect of dietary lactose on gain, feed conversion, blood, bone and intestinal parameters in postweaning rats and swine. 741 Feb 80

Duodenal mucosa showed normal morphology, interepithelial lymphocytes, alkaline phosphatase, and sucrase in a girl with growth retardation and iron deficiency, but normal absorption of lactose and xylose after two years of abnormal stools. Mucosal lactase was low. Fourteen months later mucosal damage consistent with coeliac disease was evident, and gluten intolerance was subsequently confirmed by gluten challenge. It is probable that, in some children, the mucosal lesion occurs very gradually, so that at an early stage with normal morphology, suppression of lactase activity and possibly interference with iron absorption may be the only abnormalities.
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PMID:Early or pre-coeliac mucosa: development of gluten enteropathy. 746 78


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