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)

Human embryonic neutrophils (N) in the liver (from 8.5 mm crown-rump length) are alkaline phosphatase (AP) negative during the first trimester of pregnancy. Early bone marrow granulocytes (from eleventh to sixteenth weeks of gestation) behave similarly. Only a small percentage of slightly AP positive cells could be found. Occasional cells with strong NAP reaction appear in the second trimester. NAP positivity greatly increases in the third trimester and term-babies have a somewhat higher than normal NAP activity in circulating blood. Unlike NAP reaction, naphthol-AS-D-chloroacetate esterase and peroxidase reactions are positive even in the earliest (AP negative) neutrophils.
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PMID:Ontogeny of human neutrophil granulocyte alkaline phosphatase. 64 70

We examined steady-state levels of mRNA for alkaline phosphatase in neutrophils (NAP) treated with granulocyte colony-stimulating factor (G-CSF). The amount of mRNA for NAP was shown to increase after 6 hours of culture with G-CSF when no increase in NAP activity was yet observed, and the transcript was the greatest after 20-24 h of culture with G-CSF. Treatment of neutrophils with both G-CSF and retinoic acid augmented the amount of mRNA for NAP over the amount obtained by G-CSF alone, which was most marked at 24 h. These results show that both G-CSF-mediated NAP induction and its potentiation by retinoic acid are due to the increased levels of mRNA for NAP.
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PMID:Regulation of mRNA levels of alkaline phosphatase gene in neutrophilic granulocytes by granulocyte colony-stimulating factor and retinoic acid. 170 51

A photoreactive derivative of a sulfur-free bovine parathyroid hormone (PTH) analogue, [Nle8,N-epsilon-(4-azido-2-nitrophenyl)Lys13,Nle18,Tyr34]bovine PTH-(1-34)-NH2 (NAP-NlePTH), was purified from the products of the reaction of [Nle8,Nle18,Tyr34]bovine PTH-(1-34)-NH2 (NlePTH) with 4-fluoro-3-nitro-phenylazide and was used to identify binding components of the PTH receptor in clonal rat osteosarcoma cells (ROS 17/2.8). The purified analogue, NAP-NlePTH, is a fully active agonist in three different ROS 17/2.8 cell bioassays: 1) specific binding to saturable PTH receptors; 2) stimulation of cyclic AMP accumulation; and 3) inhibition of cellular alkaline phosphatase activity; this analogue gave dose response curves parallel to and 25-33% as potent as its parent molecule, NlePTH. Radioiodinated NAP-NlePTH (125I-labeled NAP-NlePTH) retained maximal receptor-binding potency. Radioligand saturation studies in intact cells showed that the Kd of PTH receptors for the photoligand was slightly less than that for 125I-labeled NlePTH (2.8 and 0.8 nM, respectively), but that the Bmax was essentially identical for both radioligands (8 fmol/10(5) cells). Photoaffinity labeling of ROS 17/2.8 cells revealed several 125I-labeled macromolecular components by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. One predominant 125I-labeled band, having an apparent Mr of 80,000 daltons (including Mr = 4,347 ligand; hereafter referred to as the Mr = 80,000 protein), was consistently demonstrated in both reducing and nonreducing conditions. Its labeling was completely inhibited by coincubation with NlePTH (10 nM) at 26-fold molar excess to the photoligand, but not by biologically inactive PTH fragments or unrelated hormone. Labeling of several other macromolecular components persisted in the presence of NlePTH (1 microM). Only the labeling of the Mr = 80,000 protein showed saturation kinetics for photoaffinity labeling; the dose of 125I-labeled NAP-NlePTH (0.8 nM) to half-saturate labeling of the Mr = 80,000 protein was close to the Kd (2.8 nM) of specific binding of the photoligand to receptors in intact ROS 17/2.8 cells. Pretreatment of the cells with NlePTH and dexamethasone led to the predicted proportional decrease or increase, respectively, in labeling of the Mr = 80,000 protein. Our data, using a highly purified photoactive derivative of PTH, having carefully defined chemical and biological properties, show a plasma membrane component of Mr = 80,000 in ROS 17/2.8 cells that possesses the affinity, binding capacity, and physiological characteristics of the PTH receptor.
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PMID:Photoaffinity labeling of parathyroid hormone receptors in clonal rat osteosarcoma cells. 283 Dec 8

A factor, termed neutrophil alkaline phosphatase-inducing factor (NAP-IF), that has the capacity to increase the NAP activity of granulocytes was characterized by using two samples: cystic fluid (CF) and conditioned medium of a tumor cell line (T3M5). The molecular weight of NAP-IF was shown to be between 13,000 and 45,000, and its isoelectric point was between 5.5 and 6.2. It was sensitive to heat and proteolytic enzymes, but was resistant to DNase and RNase, suggesting that NAP-IF is an acidic protein or glycoprotein. These characteristics of NAP-IF seem to be similar to those of granulocyte-macrophage colony-stimulating factor (GM-CSF) that is also present in the CF. NAP-IF rich fractions obtained by isoelectric focusing from CF were also found to be rich in a subclass of GM-CSF: granulocyte-CSF (G-CSF). Furthermore, a high correlation was noted between the activities of G-CSF and NAP-IF (gamma = 0.798, P less than 0.005). These results suggest that the two activities, i.e., G-CSF and NAP-IF, may be attributable to an identical macromolecule.
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PMID:Characterization of neutrophil alkaline phosphatase-inducing factor (NAP-IF). 387 40

Neutrophil alkaline phosphatase activity was estimated in 194 patients; 59 cases of chronic myeloid leukaemia (CML), 42 cases of polycythaemia vera (PV), 24 cases of primary myelofibrosis, 7 cases of idiopathic thrombocythaemia, 6 cases of leukaemoid reaction, 19 cases of secondary polycythaemia (PS) and 37 cases of the primary myelodysplastic syndrome (MDS). According to NAP activities the groups proved to be separate entities (p less than 0.00025). The incidence of decreased NAP score in the CML group was 85% and differed significantly from the other groups as a whole, as well as separately (p less than 0.001). The MDS group, the only group besides CML that showed decreased scores, also differed significantly from the others (p less than 0.001). The PS group, nearly always showing normal scores, differed significantly from the PV group (p less than 0.0052). A method evaluating single cell NAP activity proved superior to the score method in discriminating between the different groups. Thus, the incidence of decreased activity in the CML group was 93% compared with 85% by the score method and the incidences of increased activity in the PV, MP, IT, and LR groups were 79% to 100% compared with 25% to 67% by the score method. The latter difference was statistically significant (p = 0.029).
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PMID:Evaluation of neutrophil alkaline phosphatase (NAP) activity in untreated myeloproliferative syndromes and in leukaemoid reactions. 404 68

We measured the concentration of granulocyte-committed progenitor cells (CFU-c) and the alkaline phosphatase activity of neutrophils harvested from colonies cultured from the peripheral blood of 30 patients with high-count chronic granulocytic leukaemia (CGL) in the chronic phase. Neutrophils in colonies cultured from marrow of normal donors or patients with acute myeloid leukaemia in remission served as controls. CFU-c numbers in CGL peripheral blood were on average 3 times higher than in normal marrow (130.1 +/- 126.2 (SD) versus 43.0 +/- 25.2 per 1 X 10(5) cells plated, respectively). The mean NAP scores in cultured CGL neutrophils were substantially higher than control values (89.9 +/- 48.0 versus 55.9 +/- 33.0 units, respectively). There was a tendency for peak values of NA in culture to be reached at earlier points in CGL cultures with high CFU-c numbers (i.e. high proliferative rates) than in those with lower CFU-c numbers (lower proliferative rates). Our data accord with the concept that low NA levels in CGL in vivo result from modulating influences external to the neutrophil.
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PMID:Alkaline phosphatase activity of chronic granulocytic leukaemia neutrophils in agar culture. 692 68

Using postmitotic granulocytes (PMGs) with low neutrophil alkaline phosphatase activity (NAP activity), factor(s) having the capacity to increase their NAP activity were examined in vitro. A high activity of the factor was demonstrated in the cystic fluid of a human squamous cell carcinoma, which is known to produce a large amount of granulocyte-macrophage colony-stimulating factor (GM-CSF). The NAP-stimulating factor increased NAP values both in PMGs from normal bone marrow and PMGs from patients with chronic myeloid leukemia (CML), and NAP values in cells treated with the factor approached or rose above those of normal peripheral granulocytes after 48 hr of culture. The effect of the factor was specific in that the factor caused stimulation only in granulocytic series. These findings may indicate that increases in NAP activity reflect maturation or granulocytes and that low NAP activity of neutrophils derived from patients with CML is due to the immaturity of these cells. The relationship between the factor responsible for the increase in NAP activity and GM-CSF is also discussed.
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PMID:Factor(s) responsible for the increase in alkaline phosphatase activity of postmitotic granulocytes from normal individuals and patients with chronic myeloid leukemia. 697 95

Interleukin-8 (IL-8) such as LUCT (lung giant cell carcinoma-derived chemotactic protein), NAP (neutrophil activating protein) and MDNCF (monocyte-derived neutrophil chemotactic factor), and formylmethionyl-leucyl-phenylalanine (fMLP) are well-known chemoattractants for human polymorphonuclear leukocytes (PMNs) and are able to stimulate phosphorylation of 64-kd protein (p64) in these leukocytes. To elucidate the molecular mechanism of PMN activation with chemoattractants, we investigated the phosphorylation process of p64 in an intact cell. 32P-Labeled PMNs were stimulated with LUCT/IL-8, fMLP, leukotriene B4, or C5a, and phosphorylated proteins were analyzed by two-dimensional electrophoresis and autoradiography. A marked phosphorylation of p64 was observed after stimulation. A new spot of phosphorylated p64 (pp64) could be detected on the gel stained with Coomassie Brilliant Blue, indicating that the isoelectric point (pI) of p64 shifted from 5.3 to a more acidic pI by the phosphorylation forming pp64. The spot of pp64 was shown to be dephosphorylated to p64 by treatment with calf intestine alkaline phosphatase. Other proteins having molecular masses 82, 66, 58, 55 and 50 kd were also phosphorylated. The fMLP-stimulated phosphorylation was time-dependent and saturated within 5 min. Maximum stimulation was achieved with 10 nM fMLP. Phosphoamino acid analysis revealed phosphorylation of serine residues in pp64. Staurosporine (100 nM) and W-7 (100 microM) significantly inhibited the phosphorylation of p64, but H-7 slightly inhibited it. H-8 and herbimycin A did not effect phosphorylation. Phorbol myristate acetate was found to stimulate significantly. Protein kinase C did not stimulate the phosphorylation. These data suggest that protein kinase C and calmodulin-like protein are indirectly involved in the phosphorylation of p64 during chemoattractant-activation of PMN.
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PMID:Characterization of a 64-kd protein phosphorylated during chemotactic activation with IL-8 and fMLP of human polymorphonuclear leukocytes. I. Phosphorylation of a 64-kd protein and other proteins. 839 62

A kinetic parameter (the Vm/Km ratio), an index of neutrophil alkaline phosphatase catalytic efficiency, was studied in 36 women with normal pregnancies at 16-20 weeks' gestation. On each blood sample, determinations were achieved on enzyme extracted from maternal granulocytes by monitoring the phosphohydrolytic activity at 400 nm on a spectrophotometer equipped with software for computation of kinetic parameters. Infant sex was recorded at the delivery for all women included in this study. The recent introduction of NAP as a marker for some pathological pregnancies requires a better knowledge of the behaviour of that enzyme in physiological conditions. Data reported focus attention on fetal sex. It appears to be one of the factors involved in variations of kinetic parameters observed in maternal NAP. Sex-linked differences in placental maturation could explain these results.
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PMID:Fetal sex and variations in kinetic properties of neutrophil alkaline phosphatase during the second trimester of normal pregnancy. 957 25

Electrochemical biosensor for the detection of DNA hybridization using the reduction signal of alpha-naphthol is described. A pencil graphite electrode was used as a working electrode. Capture probes were covalently attached on to the pencil graphite electrode surface (PGE) at the 5' end amino group by using N-(dimethylamino)propyl-N'-ethylcarbodiimide hydrochloride (EDC) and N-hydroxysulfosuccinimide (NHS) as a coupling agent on to PGE. After capture probe immobilization on to PGE surface; probe was hybridized with complementary biotinylated oligonucleotide. Alkaline phosphatase labeled with extravidin (Ex-AP) binds to biotinylated hybrid via biotin-avidin interaction. alpha-Naphthyl phosphate (alpha-NAP) was added and the reaction between alkaline phosphatase (AP) and alpha-NAP was occurred consequently as a substrate of AP, alpha-NAP reduction signal was obtained from this reaction, at -0.100 V by using differential pulse voltammetry (DPV). Other experimental parameters were studied such as; optimizations of hybridization time, and the concentrations of capture probe, biotinylated oligonucleotide and enzyme.
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PMID:Electrochemical detection of enzyme labeled DNA based on disposable pencil graphite electrode. 1590 40


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