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

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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)

Rat, rabbit and human bone marrow cells were cultured according to the method previously reported for cells of rat origin [1] and were exposed, or not (control), to corrosion products of a Co-Cr orthopaedic alloy as well as to metal salts containing Co2+, Cr3+ and Cr6+. Cells were cultured for 21 days and analysed for the following biochemical parameters: intracellular MTT reduction (i.e. cell viability/proliferation), alkaline phosphatase (ALP) activity and protein production. Morphological observations included both histochemistry (detection of ALP-positive cells, calcium and phosphate deposits) and scanning electron microscopy (SEM). Control cultures of rat and rabbit cells showed higher proliferation rates than human cells at the start of culture, but they all reached similar values on day 21. Protein production was parallel to cell proliferation. In contrast, ALP activity of rat cultures was much stronger than rabbit or human cultures. All cell types were able to develop the osteogenic phenotype in vitro.Co-Cr extract caused inhibitory effects on cell viability, on ALP activity and, to a lower extent, on protein production of all rat, rabbit and human cell cultures. Compared to rat and rabbit cultures, human cultures were the most sensitive to metal ions exposure.
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PMID:The use of rat, rabbit or human bone marrow derived cells for cytocompatibility evaluation of metallic elements. 1534 64

Several extracellular DNases were detected after cultivation of Streptomyces aureofaciens B96 under submerged conditions. These DNases are nutritionally regulated and high content of amino acid nitrogen in cultivation medium repress their production. By varying cultivation conditions, there remained only two extracellular nuclease activities. The major one, extracellular endodeoxyribonuclease SaD I, was purified to homogeneity by ammonium sulfate precipitation, adsorption on Spheron, chromatography on Superose-12P followed by FPLC on MonoQ and final purification on HiTrapQ. The molecular weight of the purified SaD I determined by SDS-PAGE was 31 kDa. The DNase hydrolyses endonucleolytically both double-stranded and single-stranded circular and linear DNA. It does not cleave RNA and does not exhibit phosphodiesterase nor phosphomonoesterase activity. It requires a divalent cation (Zn2+, Co2+, Mn2+, Mg2+) and its activity optimum is at neutral pH (pH 7.2). The optimal temperature for DNA cleavage was 40 degrees C. Activity was strongly inhibited in the presence of phosphate, Hg2+, chelating agents or iodoacetate, but it was stimulated by addition of dimethyl sulphoxide.
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PMID:An extracellular endodeoxyribonuclease from Streptomyces aureofaciens. 1565 86

Epidemiological studies have indicated incidences of 32.9% and 27.8% for rickets and osteomalacia, respectively, in Bactrian camels (Camelus bactrianus), but there is an increased incidence under drought conditions, sometimes reaching 75%. We have found that concentrations of phosphorus and copper in forage and soil samples in a drought affected area were significantly lower than in a control area or normal reference values (P < 0.01) ; the mean Ca:P ratio in the forages was 50:1. The phosphorus content of blood and hair from affected camels was significantly less than that in controls (P < 0.01) and concentrations of copper in the liver and kidney were significantly lower in affected camels than control animals (P < 0.01); the concentrations of triiodothyronine (T(3)), thyroxine (T(4)) and parathyroid hormone (PTH) in the serum from affected animals were significantly higher than those from healthy controls (P < 0.01); serum inorganic phosphorus and ceruloplasmin levels were lower than those in the controls (P < 0.01 or P < 0.05); the concentrations of serum alpha-globulin and beta-globulin were significantly higher in the affected camels than in the healthy controls (P < 0.01). The pathological changes seen in camels affected with rickets included porous, brittle, light, osteoporotic bones that were susceptible to fractures and had less resistance to cutting and sawing. Wrist joints were enlarged with an apparent bowing of the long bones in forelimb and with typical broadening of the epiphyses. In adult female camels, many enlarged scars were often seen in ribs indicating earlier fractures. The disease could be cured with supplementary bone meal, phosphate or mineral mixtures and in field investigations clinical signs disappeared within 15 days. Over the same period, the concentrations of phosphorus and alkaline phosphatase in blood returned to normal. The disease may be effectively prevented by use of mineral blocks (block salt licks) or dosing orally with copper, selenium and cobalt soluble glass boluses. We conclude that rickets and osteomalacia are mainly caused by phosphorus and copper deficiencies in the pasture.
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PMID:Studies on rickets and osteomalacia in Bactrian camels (Camelus bactrianus). 1584 87

Escherichia coli alkaline phosphatase exhibits maximal activity when Zn(2+) fills the M1 and M2 metal sites and Mg(2+) fills the M3 metal site. When other metals replace the zinc and magnesium, the catalytic efficiency is reduced by more than 5000-fold. Alkaline phosphatases from organisms such as Thermotoga maritima and Bacillus subtilis require cobalt for maximal activity and function poorly with zinc and magnesium. Previous studies have shown that the D153H alkaline phosphatase exhibited very little activity in the presence of cobalt, while the K328W and especially the D153H/K328W mutant enzymes can use cobalt for catalysis. To understand the structural basis for the altered metal specificity and the ability of the D153H/K328W enzyme to utilize cobalt for catalysis, we determined the structures of the inactive wild-type E. coli enzyme with cobalt (WT_Co) and the structure of the active D153H/K328W enzyme with cobalt (HW_Co). The structural data reveal differences in the metal coordination and in the strength of the interaction with the product phosphate (P(i)). Since release of P(i) is the slow step in the mechanism at alkaline pH, the enhanced binding of P(i) in the WT_Co structure explains the observed decrease in activity, while the weakened binding of P(i) in the HW_Co structure explains the observed increase in activity. These alterations in P(i) affinity are directly related to alterations in the coordination of the metals in the active site of the enzyme.
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PMID:Metal specificity is correlated with two crucial active site residues in Escherichia coli alkaline phosphatase. 1593 27

A thermostable alkaline phosphatase with high specific activity and thermal resistance was purified from a novel species of Thermus sp. named as Thermus yunnanensis sp. nov. The enzyme contains a single peptide with a molecular mass of about 52 kDa on SDS-PAGE analysis and appears to be a homodimer in solution with the molecular mass of 104 kDa. The optimal pH and temperature for its activities are pH 8.0-10.0 and 70-80 degrees C, respectively. The catalytic activities of the enzyme are metal ion dependent, and Mg2+, Zn2+ and Co2+ are the main activators. Among these, Co2+ is the most active stimulator and has unique activation effect at high temperature. Metal binding analysis showed the binding of Mg2+ at the metal binding site was easy to loss in the thermoinactivation, and Co2+ was apt to bind at that site and kept the favorable configuration of catalysis, which would result high activation in the incubation with Co2+ at high temperature. According to this study, a model was proposed for the explanation of the activation and the results of actual experiments demonstrated the validity of the model.
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PMID:Characterization of a thermostable alkaline phosphatase from a novel species Thermus yunnanensis sp. nov. and investigation of its cobalt activation at high temperature. 1595 49

Seventy-three, 10-week-old, newly weaned Omani goats of three different breeds, namely Dhofari (D), Batinah (B) and Jebel Akhdar (JA) were randomly divided into a control (n=38) and a treated group (n=35) for an experimental period of 10 months. Goats in both groups were fed 150 g/day per head of a pelleted concentrate, based on body weight and their requirements and Rhodes grass hay ad libitum, containing 0.12 and 0.10 mg/kg DM cobalt, respectively. Goats in the treated group also received bi-monthly subcutaneous injections of 2000 microg hydroxycobalamin. In contrast to the treated goats, the control animals of all breeds experienced a severe decrease in their serum vitamin B(12) levels, developed pale mucous membranes, appeared scruffy and two breeds (D and B) had significantly lower weight gains from month 5. Untreated kids of all breeds had significant decreases in their red blood cell counts and erythrocyte indices after approximately four months. Controls developed low total serum protein levels whilst activities of alkaline phosphatase and aspartate aminotransferase significantly increased. Although it is widely assumed that goats are more resistant to cobalt deficiency than sheep this is apparently not true for Omani goats. Based on experimental data from previously reported studies and those from the present study it can be concluded that the reduction in weight gains in D and B goats is related to their lower digestibility coefficients for dry matter, crude protein and energy while the increase in alkaline phosphatase and aspartate aminotransferase are associated with developing hepatic lipidosis.
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PMID:Effects of low concentrations of dietary cobalt on liveweight gains, haematology, serum vitamin B(12) and biochemistry of Omani goats. 1632 57

Low oxygen tension is a potent differentiation inducer of numerous cell types and an effective stimulus of many gene expressions. Here, we described that under 8% O(2), bone marrow stromal cells (MSCs) exhibited proliferative and morphologic changes. The level of differentiated antigen H-2Dd and the number of G(2)/S/M phase cells increased evidently under 8% O(2) condition. Also, the proportion of wide, flattened, and epithelial-like cells (which were alkaline phosphatase staining positive) in MSCs increased significantly. When cultured in adipogenic medium, there was a 5- to 6-fold increase in the number of lipid droplets under hypoxic conditions compared with that in normoxic culture. We also demonstrated the existence of MSC differentiation under hypoxic conditions by electron microscopy. Expression of Oct4 was inhibited under 8% O(2) condition, but after adipocyte differentiation in normoxic culture and hypoxia-mimicking agents cobalt chloride (CoCl(2)) and deferoxamine mesylate (DFX) treatments, Oct4 was still expressed in MSCs. These results indicate hypoxia accelerates MSC differentiation and hypoxia and hypoxia-mimicking agents exert different effects on MSC differentiation.
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PMID:Proliferation and differentiation of bone marrow stromal cells under hypoxic conditions. 1681 46

Endoplasmic reticulum (ER) stress-responsive alkaline phosphatase (ES-TRAP) serves as a sensitive indicator for ER stress. In response to heavy metals including cadmium, nickel and cobalt, hepatocytes and renal tubular cells expressing ES-TRAP exhibited ER stress and decreased ES-TRAP activity. In ES-TRAP transgenic mice, acute exposure to cadmium showed rapid, transient decreases in the activity of serum ES-TRAP. It was inversely correlated with the induction of endogenous ER stress markers in the liver and kidney. Our result provides first evidence for the acute, reversible induction of ER stress in vivo after exposure to heavy metal.
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PMID:Rapid, transient induction of ER stress in the liver and kidney after acute exposure to heavy metal: evidence from transgenic sensor mice. 1747 59

Nicotianamine (NA) is a nonprotein amino acid that inhibits the angiotensin I-converting enzyme (ACE) in the renin-angiotensin system (RAS). The purpose of this study is to prove that NA contributes to the suppression of hypertension by preferential inhibition of ACE. On comparison with EDTA-a chelator-we found that the inhibition pattern of NA for ACE is that of mixed inhibition and that NA exhibits weak chelation effects for zinc, copper, and cobalt ions. Therefore, we investigated whether NA inhibited zinc-containing enzymes other than ACE in vitro. The results revealed that NA does not inhibit leucine aminopeptidase or alkaline phosphatase in rat serum. On the other hand, NA demonstrated specific inhibitory effects for rat serum ACE and aortic ACE. These results suggest that the preferential inhibition of circulatory and tissue ACE by NA can contribute to the suppression of hypertension.
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PMID:Nicotianamine preferentially inhibits Angiotensin I-converting enzyme. 1793 38

A gene (tap) encoding a thermostable alkaline phosphatase from the thermophilic bacterium Thermus thermophilus XM was cloned and sequenced. It is 1506 bp long and encodes a protein of 501 amino acid residues with a calculated molecular mass of 54.7 kDa. Comparison of the deduced amino acid sequence with other alkaline phosphatases showed that the regions in the vicinity of the phosphorylation site and metal binding sites are highly conserved. The recombinant thermostable alkaline phosphatase was expressed as a His6-tagged fusion protein in Escherichia coli and its enzymatic properties were characterized after purification. The pH and temperature optima for the recombinant thermostable alkaline phosphatases activity were pH 12 and 75 degrees C. As expected, the enzyme displayed high thermostability, retaining more than 50% activity after incubating for 6 h at 80 degrees C. Its catalytic function was accelerated in the presence of 0.1 mM Co2+, Fe2+, Mg2+, or Mn2+ but was strongly inhibited by 2.0 mM Fe2+. Under optimal conditions, the Michaelis constant (K(m)) for cleavage of p-nitrophenyl-phosphate was 0.034 mM. Although it has much in common with other alkaline phosphatases, the recombinant thermostable alkaline phosphatase possesses some unique features, such as high optimal pH and good thermostability.
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PMID:Expression and characterization of recombinant thermostable alkaline phosphatase from a novel thermophilic bacterium Thermus thermophilus XM. 1798 75


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