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)

Crystalline human alkaline phosphatase from placenta and intestine was isolated by butanol extraction, acetone precipitation, a heat step (for the placental enzyme), ammonium sulfate precipitation, anion exchange chromatography, gel filtration and crystallisation with ammonium sulfate. Rabbit antibodies showed a partial cross-reaction between both enzymes in double diffusion, quantitative precipitation experiments and in serial precipitin curves. There was no reaction with human alkaline phosphatases from liver, kidney and bone. Three phenotypes of placental alkaline phosphatase with different electrophoretical mobility exhibited identical immunological reactions with their respective antisera. Monospecific antisera were obtained by absorption with crystalline intestinal or placental alkaline phosphatase. These monospecific antisera against the placental or the intestinal alkaline phosphatase can be used for an immunological determination of these two alkaline phosphatases without contamination by other alkaline phosphatases in human serum.
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PMID:Immunological relationship between human placental and intestinal alkaline phosphatase. 120 18

Growth plate cartilage from rachitic rats was studied to assess the role of extra-cellular matrix vesicles in the reinstitution of calcification during healing. The concentration and distribution of matrix vesicles was found to be normal in rachitic growth plate, and although the rachitic cartilage matrix was largely uncalcified, an occasional vesicle did contain internal mineral. Matrix vesicles served as initial loci for mineralization when healing was brought about either by in vivo injection of phosphate or in vitro incubation of growth plates in a metastable calcifying solution. During in vitro calcification a distinct line of mineralization developed in the upper growth plate which was shown by electron microscopy to reflect mineralization by the vesicles. The appearance of this vesicle-associated calcification line was inhibited by preheating or repeated freezing and thawing, and by 30 minutes preincubation in deoxycholate, ethane-1-hydroxy-1,1-diphosphonate, or beryllium sulfate. Our results suggest that vesicle calcification is dependent on the structural and enzymatic integrity of the vesicle membrane. Enzymes that may well play a role in vesicle calcification are phosphatases (e. g., alkaline phosphatase, pyrophosphatase and ATPase), which are known to be concentrated in vesicle membranes.
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PMID:Calcification of rachitic cartilage to study matrix vesicle function. 124 48

Four out of 18 human liver alkaline phosphatase (AP) preparations reacted with anti-liver and anti-intestinal AP. The liver AP that reacted with anti-intestinal AP, designated as intestine-like AP, was precipitated at 50% ammonium sulfate whereas the major liver AP precipitated at 66% saturation. Gel filtration showed that liver AP, intestine-like AP and intestinal AP contained AP with apparent molecular weights of 130,000 daltons; the intestine-like AP contained a second but smaller component of 70,000-80,000 daltons. AP extracted from intestine also contained this smaller component; its electrophoretic mobility was that of an a2-globulin, whereas that of the intestine-like AP had a mobility of beta-globulin. The similarity of the intestine-like AP to the AP variant found in hepatomas is stressed.
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PMID:The alkaline phosphatases of human liver: an immunochemical study. 124 90

The alkaline phosphatase from KB cells was purified, characterized, and compared to placental alkaline phosphatase, which it resembles immunologically. Two nonidentical nonomeric subunits of the KB phosphatase were found. The two subunits, which have apparent molecular weights of 64,000 and 72,000, can be separated on polyacrylamide gels containing sodium dodecyl sulfate. The Mr = 64,000 KB subunit appears to be identical in protein structure to the monomer of placental alkaline phosphatase. The Mr = 72,000 KB subunit, while differing in the NH2-terminal amino acid, appears also to be very similar to the placental alkaline phosphatase monomer. Both KB phosphatase subunits bind (32P)phosphate, and bind to Sepharose-bound anti-placental alkaline phosphatase. Native KB phosphatase is identical to the placental isozyme in isoelectric point, pH optimum, and inhibition by amino acids, and has a very similar peptide map. The data presented support the hypothesis that the Mr = 64,000 KB phosphatase subunit may the the same gene product as the monomer of placental alkaline phosphatase. This paper strengthens the evidence that the gene for this fetal protein, normally repressed in all cells but placenta, is derepressed in the KB cell line. In addition, this paper presents the first structural evidence that there are two different subunit proteins comprising the placental-like alkaline phosphatase from a human tumor cell line.
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PMID:Characterization of KB cell alkaline phosphatase. Evidence of similarity to placental alkaline phosphatase. 126 37

Chondroitin sulfate localization in mouse epiphyseal cartilage was studied using CS-56 monoclonal antibody immunospecific for the glycosaminoglycan portion of the molecule. For light and fluorescence microscopy, decalcified specimens were embedded in paraffin, Lowicryl, or were frozen and cryostat-sectioned, and the antigen-antibody reaction was demonstrated by treating sections with IgM-peroxidase, IgM-alkaline phosphatase, or IgM-fluorescein conjugates. For electron microscopy, decalcified and undecalcified specimens were embedded in Lowicryl; ultrathin sections from undecalcified specimens were decalcified by flotation on EDTA; sections from both types of specimens were treated with IgM-immunogold conjugate for demonstration of CS-56 reaction. Before immunoreaction, part of all decalcified sections were digested with Streptomyces or testicular hyaluronidase. Control sections were treated with either mouse and goat non-immune serum, or mouse monoclonal antiserum to human dendritic reticulum cells. Both light and electron microscopy show CS-56 reaction with cytoplasmic components of maturing and hypertrophic chondrocytes. Under the light microscope, immunoreaction was not visible in calcified matrix, and was visible in uncalcified matrix only after hyaluronidase digestion. Under the electron microscope, it was evident both in uncalcified and calcified matrix, although the latter showed few immunogold particles, usually placed on areas which appeared incompletely calcified. Gold particles were chiefly distributed at the periphery of calcification nodules and fully calcified matrix. These results show that CS-56, besides reacting with cytoplasm of maturing and hypertrophic chondrocytes, binds to crystal ghosts and other components of cartilage matrix, immunoreactivity decreasing as calcification increases. This suggests that chondroitin sulfate molecules are either degraded during calcification, or segregated into macromolecular complexes, or both degraded and segregated. The second possibility is supported by the increase of immunosensitivity induced by hyaluronidase digestion.
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PMID:Immunohistochemical investigation on the presence of chondroitin sulfate in calcification nodules of epiphyseal cartilage. 128 29

Prostaglandins are locally produced in a number of tissues in response to a variety of stimuli, including local growth factors and systemic hormones. The present investigation characterizes prostaglandin effects on growth plate chondrocytes. Since cyclic adenosine monophosphate (cAMP) may act as a prostaglandin-stimulated second messenger, the effects of prostaglandins A1, D2, E1, E2, F2 alpha, and I2 (10(-10)-10(-6) M) on cAMP levels and thymidine incorporation were evaluated. The stimulation of cAMP and thymidine incorporation by the various prostaglandin metabolites were dose dependent and highly correlated (r = 0.99, p less than 0.001). The magnitude of the effect varied but was maximal at 10(-6) M for each of the prostaglandins. Prostaglandins of the E series (E1 and E2) were the most potent, causing significant effects at 10(-10) M and with maximal 12- and 13-fold increases in DNA synthesis after a 24 h exposure. Prostaglandins D2 and A1 maximally stimulated thymidine incorporation by 4.7- and 3.1-fold but caused significant increases only at 10(-8) M. Prostaglandins F2 alpha and I2 were the least stimulatory, producing small but significant increases in thymidine incorporation at 10(-6) M (30 and 100% stimulations). A causal relationship between cAMP and thymidine incorporation was further verified by the ability of dibutyryl-cAMP to increase DNA synthesis. Long-term chondrocyte cultures treated continuously with PGE2 demonstrated an increase in cell number, confirming the proliferative effect. Indomethacin did not alter the potent dose-dependent stimulations of chondrocyte DNA synthesis by TGF-beta 1, basic FGF, or PTH, indicating that these known mitogens act independently of prostaglandin metabolism. PGE2 was further examined for its effects of matrix synthesis. PGE2 inhibited collagen synthesis with a maximal 42% decrease but did not alter noncollagen protein synthesis. In contrast, PGE2 maximally increased sulfate incorporation by 35% and caused a small dose-dependent inhibition in alkaline phosphatase activity. Thus, prostaglandins alter DNA and matrix synthesis in growth plate chondrocytes and may have an important role in chondrocyte metabolism in the growth plate, fracture callus, and other areas of endochondral ossification.
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PMID:Influence of prostaglandins on DNA and matrix synthesis in growth plate chondrocytes. 131 4

The present study investigated the effects of a number of oxoanion compounds on in vitro ovulation of goldfish follicles and ovarian second messenger activities. Significant levels of ovulation were induced by 0.1 mM sodium chromate, 0.1 mM sodium metavanadate, 10 mM sodium molybdate, 0.1 mM sodium orthovanadate, 5 mM sodium selenate, 0.5 mM sodium tungstate, and 0.1 mM vanadyl sulfate. At levels that significantly stimulated ovulation, metavanadate, molybdate, orthovanadate, tungstate, and vanadyl sulfate also stimulated follicular phosphatidylinositol cycling and inhibited ovarian alkaline phosphatase activity. Moreover, the ovulation induced by these oxoanions was not inhibited by indomethacin (10 micrograms/ml), while ovulation induced by selenate and chromate was. In contrast, only vanadium-containing compounds significantly stimulated prostaglandin (PG) synthesis, and, in fact, selenate significantly inhibited PG production. Finally, only sodium molybdate- and vanadium-containing compounds appeared to increase follicular adenosine 3',5'-cyclic monophosphate content. While all oxoanions stimulated in vitro ovulation, they had differential effects on certain signal transduction pathways when tested at concentrations that stimulated in vitro ovulation. From the results, two basic groups could be delineated, one containing tungstate-, molybdate-, and vanadium-containing compounds and the other selenate and chromate. Thus the mechanism by which ovulation is induced by chromate and selenate may be different from that of vanadium-containing compounds, molybdate, and tungstate.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Oxoanions stimulate in vitro ovulation and signal transduction pathways in goldfish (Carassius auratus) follicles. 133 98

The responsiveness of human dental pulp (HDP) cells to parathyroid hormone (PTH) was investigated by measuring their cyclic AMP (cAMP) content, DNA synthesis, alkaline phosphatase activity, collagen synthesis, and glycosaminoglycan (GAG) synthesis. PTH dose-dependently increased the intracellular cAMP 1 min after the addition of PTH. Confluent HDP cells on day 14 expressed a high level of cAMP production after addition of 3 units/ml PTH. The hormone did not affect DNA synthesis by HDP cells. Alkaline phosphatase activity was suppressed by PTH to 81% of control (p < 0.01), and addition of dibutyryl cAMP to the medium mimicked the effect of PTH (79% of control, p < 0.01). The hormone inhibited collagen synthesis (15% decrease of [3H] proline incorporation, p < 0.01), and stimulated non-collagen protein synthesis (10% increase, p < 0.05). The increase of non-collagen protein by PTH was in accordance with the enhancement of GAG synthesis (17% increase of [35S]sulfate incorporation, p < 0.01). Dibutyryl cAMP caused further increase of GAG synthesis, to 155% of control (p < 0.01). Observations of the radiolabeled proteins on 10% sodium dodecyl sulfate-polyacrylamide gel electrophoresis after metabolic labeling with [14C]proline and [35S]sulfate revealed a similar tendency to the quantitative determinations in which PTH inhibited collagen synthesis and stimulated GAG synthesis. These findings suggest that HDP cells have some osteoblastic characteristics in terms of PTH responsiveness, and that this culture system is a useful model for studies of human dental pulp.
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PMID:Actions of parathyroid hormone on cultured human dental pulp cells. 133 58

Characterization of eleven monoclonal antibodies (MAbs), raised to isolated sodium dodecyl sulfate (SDS)-treated Alzheimer's neurofibrillary tangles (ANT), has revealed the presence of at least two different epitopes. MAbs were tested for reactivity to ubiquitin and paired helical filaments (PHF) isolated by three different procedures. The effect of protease and/or alkaline phosphatase pretreatment on the reactivity of the MAbs with isolated PHF was also examined. All MAbs that had reacted strongly in the ELISA with sonicated SDS-treated ANT also immune decorated isolated PHF to varying degrees. Two MAbs exhibited a high reactivity to PHF: 3-39 and 5-25. MAb 3-39 was found to recognize a protease sensitive epitope. In contrast MAb 5-25 was found to consistently decorate isolated PHF in all preparations and exhibited a strong reactivity to ubiquitin, and the epitope in isolated PHF was not protease sensitive. Thus structural PHF after protease treatment and detergent treatment contain an antigenic site that is present in ubiquitin.
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PMID:Immune electron microscopic characterization of monoclonal antibodies to Alzheimer neurofibrillary tangles. 137 80

The effect of simulated weightlessness on bone metabolism was investigated in skeletal unloading for 4 days. Skeletal unloading was designed using the model of hindlimb hang in rats. Skeletal unloading with hindlimb hang cased a significant decrease of alkaline phosphatase activity, deoxyribonucleic acid (DNA) content, and glucose consumption in the femoral diaphysis, but not in the calvaria. When femoral-diaphyseal tissues were cultured in the presence of insulin (10(-8) M), the hormone produced a significant increase of alkaline phosphatase activity and decrease of glucose consumption in the femoral-diaphyseal tissues obtained from normal rats. This hormonal effect was not seen in the femoral diaphysis, but in the calvaria, of rats with skeletal unloading. However, insulin effect was seen in the femoral diaphysis obtained at 3 days after the removal of skeletal unloading. Meanwhile, the presence of other bone-regulating factors (10(-8) M parathyroid hormone [1-34] and 10(-4) M zinc sulfate) revealed an appreciable effect on alkaline phosphatase activity in the femoral diaphysis from rats with skeletal unloading. These results suggest that gravitational stimulation can directly enhance a specific insulin sensitivity in the regulation of bone metabolism.
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PMID:Simulated weightlessness and bone metabolism: gravitational stimulation enhances insulin sensitivity. 143 99


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