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)

Six hundred nineteen strains of nonfermenting gram-negative rods were tested for alkaline phosphatase, benzyl-arginine arylamidase, pyrrolidonyl arylamidase, ethylene glycol acidification, and susceptibility to desferrioxamine and colistin. The results were highly discriminant. Therefore, the proposed tests may be helpful for the identification of this group of organisms.
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PMID:Biochemical and susceptibility tests useful for identification of nonfermenting gram-negative rods. 1188 Apr 47

Ecto- and exoenzymes that metabolize extracellular adenosine diphosphate (ADP), the major promoter of platelet activation and recruitment, are of potential clinical importance because they can metabolically prevent excessive thrombus growth. An ecto-ADPase (CD39, NTPDase1) has been identified on endothelial cells. We demonstrate that ADP and adenosine triphosphate (ATP) are rapidly metabolized to adenosine monophosphate (AMP) in sheep plasma at pH 7.4. This hydrolysis is sensitive to P(1), P(5)-di-(adenosine-5') pentaphosphate (Ap(5)A), and ethylene glycol bis (beta-aminoethyl ether) - N, N, N(-), N(-) tetra-acetate (EGTA) but insensitive to tetramisole (an alkaline phosphatase inhibitor). A specific phosphodiesterase substrate, p -nitrophenol-5'-thymidine monophosphate (TMP) (p -Nph-5'-TMP), was readily hydrolyzed in sheep plasma at a rate of approximately 0.25 nmol/min/mg protein, and this hydrolysis was inhibited by ADP, ATP, and Ap(5)A. Furthermore, 200-fold purified p -Nph-5'-TMP-hydrolyzing activity also hydrolyzed ATP and ADP directly to AMP. When ADP was preincubated in plasma, its ability to induce platelet aggregation was inhibited in a time-dependent manner. This effect was abolished by Ap(5)A. The inhibitory effects on platelet aggregation correlated with hydrolysis of the ADP in plasma. These data suggest that the endogenous soluble plasma phosphohydrolase metabolizes ATP and ADP by means of cleavage of the alpha-beta-phosphodiester bond of nucleoside 5'-phosphate derivatives. This novel biochemical activity inhibits platelet reactivity through hydrolysis of extracellular nucleotides released by activated platelets during (patho)physiological processes, serving a homeostatic and antithrombotic function in vivo.
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PMID:Role of a novel soluble nucleotide phospho-hydrolase from sheep plasma in inhibition of platelet reactivity: hemostasis, thrombosis, and vascular biology. 1191 50

We investigated the modulation of critical transcriptional steps of C2C12 myoblast/osteoblast transdifferentiation triggered by the bone morphogenetic protein 2 (BMP2) signaling protein, in response to epigenetic inhibition of the endocytotic internalization of exogenous BMP2. BMP2 endocytosis was inhibited chemically with polyethylene glycol-50 (PEG-Chol) and cyclodextrin and mechanically by mild hyposmotic treatment. BMP2-dependent nuclear translocation of the mother against Dpp (Smad1) transcription factor was ten times faster if BMP2 endocytosis was inhibited. Smad1-dependent expression of the JunB gene, the first transcriptional step in myoblast dedifferentiation, was increased by a factor of three to four. JunB-dependent levels of myogenin repression, one of the critical markers of terminal myoblastic differentiation, was amplified by a factor of three. Smad1-dependent levels of alkaline phosphatase expression, one of the C2C12 osteoblast differentiation markers, were 3.5 to 5 times higher. The same behavior was observed for osteopontin, the other C2C12 osteoblast differentiation marker. These results suggest that the cell genome could "sense" tissue mechanical deformations by mechanical inhibition of signaling protein endocytosis, thereby translating mechanical strains into transcription events involved in cell differentiation.
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PMID:C2C12 myoblast/osteoblast transdifferentiation steps enhanced by epigenetic inhibition of BMP2 endocytosis. 1205 92

Degradable poly(ethylene glycol) (PEG) hydrogels with varying mass loss profiles were investigated to assess their applicability as delivery vehicles for osteoinductive growth factors in bone tissue engineering. Protein release is readily controlled by changes in both the structure (i.e., macromer concentration) and chemistry (i.e., number of degradable units) of the starting macromer. In vitro studies indicate an increase in total protein levels, alkaline phosphatase, and mineralization by osteoblasts cultured in the presence of osteoinductive growth factors compared to cells cultured with standard media. When growth factors are delivered from a 25 wt% hydrogel, a significant increase in both alkaline phosphatase and mineralization was seen after 3 weeks of culture over growth factor delivery in a bolus fashion. Additionally, gene expression levels of both osteocalcin and type I collagen were higher at early timepoints when growth factors were released from hydrogels. These results indicate that growth factors remain active after photoencapsulation, that the sustained delivery of growth factors alters various markers of osteoblastic differentiation, and that these networks could be useful as delivery vehicles for growth factors in bone tissue engineering. Finally, ectopic bone formation was present in subcutaneous rat tissue after implantation of hydrogel networks loaded with osteoinductive growth factors.
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PMID:Delivery of osteoinductive growth factors from degradable PEG hydrogels influences osteoblast differentiation and mineralization. 1222 Aug 38

An otherwise unexplained, persistently elevated plasma alkaline phosphatase concentration in a 71-year-old woman was found to be attributable to the presence of macro-alkaline phosphatase using polyethylene glycol precipitation. Gel filtration showed two high MW peaks with masses of about 330 kDa and 560 kDa. The alkaline phosphatase (ALP) complex was characterized by immunoelectrophoresis as a complex with IgG with kappa light chains.
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PMID:Macro-alkaline phosphatase due to IgG kappa complex: demonstration with polyethylene glycol precipitation and immunofixation. 1222 63

A 33-y-old male developed severe acidosis, renal failure, and profound neutrophilia after ingesting ethylene glycol. Workup for his neutrophilia excluded infectious and malignant causes. An elevated leukocyte alkaline phosphatase (LAP) level confirmed a leukemoid response, and the neutrophila resolved. Although several leukemoid reactions have been published due to therapeutic agents these reports are often incomplete or inaccurate; this is the first case of leukemoid response to a toxin. Leukemoid response is distinguishable from leukemia by the absence of clonally derived cells, although this is not easily apparent in extreme neutrophilia. Elevated LAP is useful in identifying leukemoid reaction from leukemia in cases of extreme neutrophila. If a patient develops extreme neutrophila in association with drug or toxin exposure, a leukemoid reaction should be considered and an LAP obtained.
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PMID:Leukemoid response in ethylene glycol intoxication. 1236 Nov 22

Dimyristoylphosphatidylethanolamine (DC(14:0)PE) and the dioleoyl analogue (DC(18:1cis)PE) were mixed with alpha-biotinylamido-omega-N-succinimidoxycarbonyl-poly(ethylene glycol) (NHS-PEG-biotin) and quantitatively converted to alpha-biotinylamido-omega-(dimyristoylphosphatidylethanolamino-carbonyl)polyethylene glycol (DC(14:0)PE-PEG-biotin) and the dioleoyl analogue DC(18:1cis)PE-PEG-biotin, respectively. As shown by thin-layer chromatography and 1H NMR spectroscopy, PEGylation of both phosphatidylethanolamine types went to completion if the reaction was performed in organic solvent in the presence of triethylamine. The resulting derivatives were successfully incorporated into both classical phospholipid vesicles and a phospholipid bilayer surrounding nanometer-sized magnetite cores. In the latter case, the so-called activated Stealth(1) magnetoliposomes were produced which very efficiently immobilized streptavidinylated alkaline phosphatase.
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PMID:Biotinylated Stealth magnetoliposomes. 1242 77

Biodegradable polymers, such as poly(lactic acid) (PLA) and poly(lactic-coglycolic acid) (PLGA), are attractive materials for tissue engineering because of their degradative and mechanical properties, which permit scaffolds to be tailored to the individual requirements of different tissues. Although these materials support tissue development, their chemical properties offer no control of cell adhesion or function because their surfaces become immediately masked by adsorbing serum proteins when the materials come into contact with body fluids. Furthermore, adhesion proteins undergo conformational changes and a decrease in bioactivity when adsorbed to hydrophobic materials, such as PLA. To overcome these limitations, we modified the properties of PLA by synthesizing a diblock copolymer with poly(ethylene glycol) (PEG), which is known to reduce the amount of adsorbed proteins and to modify their conformation. By altering the PEG content of these diblock copolymers we were able to control the adsorption of adhesion proteins and, because cell adhesion takes place only in the presence of serum proteins, to control cell adhesion and cell shape. Marrow stromal cell differentiation to the osteoblastic phenotype was strongly improved on PEG-PLA compared with PLA, PLGA and tissue culture polystyrene and led to a 2-fold increase in alkaline phosphatase activity and mineralization.
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PMID:Poly(D,L-lactic acid)-poly(ethylene glycol)-monomethyl ether diblock copolymers control adhesion and osteoblastic differentiation of marrow stromal cells. 1262 56

Technologies allowing direct detection of specific RNA/DNA sequences occasionally serve as an alternative to amplification methods for gene expression studies. In these direct methods the hybridization of probes takes place in complex mixtures, thus specificity and sensitivity still limit the use of current technologies. To address these challenges, we developed a new technique called the nucleic acid capture assay, involving a direct multi-capture system. This approach combines a 3'-ethylene glycol scaffolding with the incorporation of 2'-methoxy deoxyribonucleotides in the capture sequences. In our design, all nucleotides other than those complementary to the target mRNA have been replaced by an inert linker, resulting in significant reductions in non-specific binding. We also provide a versatile method to detect the presence of captured targets by using specific labeled probes with alkaline phosphatase-conjugated anti-label antibodies. This direct, flexible and reliable technique for gene expression analysis is well suited for high-throughput screening and has potential for DNA microarray applications.
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PMID:Nucleic acid capture assay, a new method for direct quantitation of nucleic acids. 1262 24

A simple method for preparation of brush border membranes (BBM) from rat kidney using polyethylene glycol (PEG) precipitation has been described. This method avoids the use of cations for the preparation, which might alter membrane lipid composition. These preparations were assessed for enrichment of marker enzymes, contamination by subcellular structures, lipid composition and transport function. An enrichment of 11.8910-fold of alkaline phosphatase, 13.9500-fold of amino peptidase and 13.6500-fold of gamma-glutamyl transpeptidase and an approximate yield of 60% were seen in the final membrane preparation as compared to the homogenate. There was very little contamination of basolateral membranes, peroxisomes, microsomes or lysosomes in the final membrane preparation. Analysis of sugars indicated high content of fucose and sailic acid as compared to hexoses. Isolated membranes appeared as vesicles as seen by electron microscopy. Lipid analysis indicated the presence of various neutral and phospholipids with a high content of sphingomyelin along with a cholesterol/phospholipid ratio of 0.4850. The isolated membrane vesicles were able to transport glucose. This study has shown a simple method of renal brush border membrane preparation, which is comparatively pure and functionally active.
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PMID:A simple method of rat renal brush border membrane preparation using polyethylene glycol precipitation. 1275 61


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