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)

Serum enzyme determinations are now well-established diagnostic tools in so-called "placental insufficiency". A good predictability of oxytocinases (P-CAP-placental oxytocinase and T-CAP-tissue oxytocinase) and a doubtful one of those of phosphatases (AP-alkaline phosphatase, HSAP-heat stable alkaline phosphatase) has been shown in high-risk pregnancies. The purpose of this study was to determine the prognostic value of the above cited enzymes in the so-called "pregnancy at neuroendocrinological risk", i.e. pregnancy in women with a prepregnancy history of hormonal disorders. It was shown that the outcome and results of such pregnancies are poorer that those of normal pregnancies. The series studied comprised 364 pregnant patients with pregnancy at neuroendocrinological risk that were being monitored by means of serum assays of the four enzymes. An attempt was made to assess each of these enzyme activities both in single (at least one value below 2.5 percentile calculated for healthy subjects) and serial determinations (two consecutive results decreasing or remaining at the same level). Normal and abnormal enzyme results were compared with normal and abnormal conditions of the newborn. The results presented showed that P-CAP (Tab. I) and T-CAP (Tab. II) levels were useful in prenatal diagnosis of fetal impairment in heneral, in addition to perinatal mortality and low values of the APGAR score. Neither the single nor serial assays of AT (Tab. III) and HSAP (Tab. IV) were valuable in predicting birth of an impaired neonate. Sensitivity of the test, i.e. percentage of women with abnormal enzyme assays among those patients who gave birth to impaired neonates, and specificity of the test, i.e. the percentage of women delivered of impaired neonates among all women with abnormal enzyme assays, of the four enzymes were compared. Sensitvity and specificity of P-CAP and T-CAP were higher than those for AP and HSAP. Moreover, sensitivity for all four enzymes was higher in serial assays, and specificity was higher in single assays. The results of the present analysis demonstrated the prognostic value of oxytocinase assays also in the pregnancy at neuroendocrinological risk. Assays of P-CAP and T-CAP were of equal significance, notwithstanding reports of a greater usefulness of P-CAP. Assays of CAP were helpful particularly in the conditions on which neuroendocrinological gestosis exerts a direct influence, i.e. in low Apgar score and perinatal mortality. On the other hand, serum alkaline phosphatases proved useless in endocrine pathology of pregnancy and HSAP was not superior to AP. About one half of future mothers of impaired neonates had enzyme results outside the range of the assays under consideration. This could be explained by the fact that these enzymes activities reflect placental function and are not directly related to fetal metabolism. Because of that they should be supplemented by other diagnostic methods being used in a clinic of high-risk pregnancy.
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PMID:Comparative prognostic value of serum placental and tissue oxytocinase, alkaline phosphatase and its heat-stable fraction in pregnancy at neuroendocrinological risk. 101 Oct 62

The phenotype of Escherichia coli appR pleiotropic mutants has been compared with that of mutants in the katF gene, which lies in the same region and controls expression of catalase HPII (katE) and exonuclease III (xth). All the described characters of appR mutants--reduced pH 2.5 acid phosphatase level, overexpression of alkaline phosphatase and ability of crp or cya mutants to utilize some CAP + cAMP-dependent carbon sources--were reproduced by a katF:: Tn10 insertion. In all cases, the wild-type phenotype was restored by the presence of a plasmid-borne katF+ gene. Conversely, spontaneous appR mutants were hypersensitive to H2O2 to the same degree as katF mutants. We conclude that the appR gene is identical to katF, which encodes a putative new sigma factor (Mulvey and Loewen, 1989).
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PMID:Are appR and katF the same Escherichia coli gene encoding a new sigma transcription initiation factor? 164 76

A previously described chondrocyte alkaline phosphatase induction factor (CAP-IF) for chicken epiphyseal growth plate chondrocytes has been purified to SDS-PAGE homogeneity from fetal bovine serum by ammonium sulfate precipitation and by dye-ligand affinity (Affi-Gel Blue and Reactive Green-19 agarose) and hydroxyapatite column chromatographies. As determined by immunoprecipitation of [35S]methionine-labeled cellular proteins after 3 day treatment, this highly purified CAP-IF increases the level of AP and certain other membrane proteins 2- to 3-fold over control values. The pure protein of apparent 64.5 kDa molecular weight has been identified as fetuin by N-terminal amino acid sequencing. This was confirmed by the finding that high alkaline phosphatase (AP)-inducing activity is present in fetuin prepared by the Spiro method. However, fetuins prepared by the Pedersen or Deutsch procedures are inactive. At least half of the CAP-IF activity of fetuin was irreversibly destroyed by treatment with EDTA and addition of Zn2+ did not reactivate the EDTA-treated fetuin. Ascorbate synergistically enhanced the effect of fetuin on chondrocyte AP activity by over 8-fold during 3 day exposure. Because of the very high homology between fetuin and the A-chain of alpha 2-HS glycoprotein, we also tested and found that alpha 2HS glycoproteins from human serum and bovine bone are both strong AP inducers. Our findings suggest that the AP-inducing activity resides in a labile, cystatin/Zn(2+)-binding domain common to these related serum glycoproteins. These proteins appear to play a role in enhancing AP expression in normal growth plate cartilage differentiation.
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PMID:Fetuin and alpha-2HS glycoprotein induce alkaline phosphatase in epiphyseal growth plate chondrocytes. 172 Oct 70

The physiological and genetic controls operating on phosphate-regulated promoters were studied in greater detail. This was done by defining the control for three phosphate-regulated genes: phoA, psiE, and psiO. Each is highly inducible by phosphate starvation. Individually, these phosphate-starvation-inducible, psi, genes at the same time show common and differing features in their molecular control. The phoA gene, encoding alkaline phosphatase, is specifically induced by phosphate starvation. It is negatively controlled by phoR as well as by the phosphate-specific transport (PST) system in Escherichia coli. phoA induction is positively controlled by the phoB, M, and R products; it is unaffected by the cAMP and CAP system. The psiE and psiO genes were studied by using strains with lacZ fused to their respective promoters. psiE-lacZ is induced by phosphate-, carbon- or nitrogen-limited growth. Genetically, psiE-lacZ induction is partially phoB and phoR-dependent. However, its expression is phoM-independent. This implies that phoB/phoR coupled control differs from phoB/phoM coupled control. Repression of psiE-lacZ is substantially altered in only some PST mutants, such as phoT. In addition, psiE-lacZ is negatively controlled by the cAMP and CAP system. psiO-lacZ is induced by phosphate-, carbon- or nitrogen-limited growth or by anaerobiosis. Its expression is unaffected by any pho mutation that has been previously described. A cell density-dependent induction of psiO-lacZ is observed in lon mutants. Also, psiO-lacZ is negatively controlled by the cAMP-CAP system. In summary, these results demonstrate that co-ordinately regulated promoters can have some common regulatory elements while, at the same time, not sharing other controlling factors.
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PMID:Overlapping and separate controls on the phosphate regulon in Escherichia coli K12. 630 24

Three sets of interrelated specimens containing alkaline phosphatase (ALP) were analyzed: CAP 1977 Enzyme Survey serum, human serum supplemental with calf intestinal ALP, and human serum with increased human liver ALP. Five quite distinct ALP methods were used. In addition, fresh serum from volunteer blood donors and serum from patients with increased serum ALP activities were examined by each of these five methods. Conversion factors for the five different methods based on results from calf-intestine-supplemented interrelated specimens could not be used to interconvert results for fresh human serum. However, the interrelated specimens with increased human liver ALP made interconversion of results for fresh human serum possible.
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PMID:Intralaboratory survey of alkaline phosphatase methods. 728 42

The Kallestad technique for measurement of total IgE is based on a "sandwich" technique that uses a solid phase (wells in a sensitised microplate) as a separator. The samples that contain the IgE and monoclonal anti-IgE antibodies (AcM anti-IgE) are incubated in the wells sensitised with goat anti-mouse IgE. The AcM anti-IgE binds the IgG and the complex is then bound to the wells by the anti-mouse IgG. After washing, anti IgE marked with alkaline phosphatase is added and this binds to the previously linked IgE. The intensity of colouration is directly proportional to the concentration of IgE in the sample and is measured by spectrophotometry. The Kallestad technique has very great sensitivity (> 1 KUI/L) for a serum sample of 20 microliter. The measurement is quick, with 2 h incubation. There was good intra-assay reproducibility for values 2 to 1100 KUI/L with CV of 7.6. This good reproducibility was also found in inter-assays for values between 2 and 10 KUI/L. The Kallestad technique was evaluated firstly against the CAP RIA System of Pharmacia and secondly, for values against the kit RIA Ultra. For a population labelled "all comers" with values between 2 to 1100 KUI/L the statistical analysis showed no significant difference between the two techniques. The statistical analysis of the study of low values, made with the RIA Ultra kit showed that there was a significant difference between the two techniques. Exchange of standards between the two methods showed a certain over-evaluation of the values of Pharmacia whilst measurements with the Kallestad standards showed a relative under-evaluation. It should be noted that the comparison has been made between a RIA (Pharmacia) technique and one of EIA (Kallestad).
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PMID:[Total serum IgE levels. Comparative study of the Kallestad and Pharmacia techniques]. 770 27

The collapsin and semaphorin family of extracellular proteins contributes to axonal path finding by repulsing axons and collapsing growth cones. To explore the mechanism of collapsin-1 action, we expressed and purified a truncated collapsin-1-alkaline phosphatase fusion protein (CAP-4). This protein retains biological activity as a DRG growth cone collapsing agent and saturably binds to DRG neurons with low nanomolar affinity. Specific CAP-4 binding sites are present on DRG neurons, sympathetic neurons, and motoneurons, but not on retinal, cortical, or brainstem neurons. Outside the nervous system, high levels of CAP-4 binding sites are present in the mesenchyme surrounding major blood vessels and developing bone and in lung. These sites provide a substrate for the collapsin-1-dependent patterning of non-neuronal tissues perturbed in sema III (-/-) mice. The staining patterns for mouse semaphorin D/III and chick collapsin-1 fusion proteins are indistinguishable from one another but quite separate from that for semaphorin B and M-semaphorin F fusion proteins. These data imply that a family of high-affinity semaphorin binding sites similar in complexity to the semaphorin ligand family exists.
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PMID:Neuronal and non-neuronal collapsin-1 binding sites in developing chick are distinct from other semaphorin binding sites. 936 65

The incidence of allergy to airborne proteins derived from tree and grass pollen, feces of mites, spores of molds, and pet dander has been increasing over the last decades. Since precise diagnosis is a prerequisite for successful immunotherapy, there is a rising demand for rapid, reliable, and inexpensive screening methods such as dipstick assays. With the purified recombinant major birch-pollen allergen rBet v 1a as model protein, crystalline bacterial cell-surface layers (S-layers) were tested for their applicability as an immobilization matrix for dipstick development. For this purpose, S-layers were deposited on a mechanically stable microporous support, cross-linked with glutaraldehyde, and free carboxylic acid groups of the S-layer protein were activated with carbodiimide. In the present test system, rBet v 1a was immobilized via the monoclonal mouse antibody BIP 1, which, unlike the allergen, is too large to enter the pores of the S-layer lattice, and which therefore formed a closed monolayer on the outermost surface of the crystal lattice. Moreover, BIP 1 is known to modulate IgE binding to the allergen. After incubation of the dipsticks in serum, washing of the reaction zone under tap water, and binding of an anti-IgE alkaline phosphatase conjugate, 5-bromo-4-chloro-3-indolyl phosphate/nitro blue tetrazolium was used as substrate, forming an IgE concentration-dependent colored precipitate on the S-layer surface. The investigation of patient sera previously tested with the CAP system confirmed the specificity of the S-layer-based dipstick assay. Since the dipstick is easy to handle and the whole test procedure takes only 90 min, this test system should be applicable for rapid determination of specific IgE and for first screening in the doctor's practice.
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PMID:A novel dipstick developed for rapid Bet v 1-specific IgE detection: recombinant allergen immobilized via a monoclonal antibody to crystalline bacterial cell-surface layers. 972 28

A phage-displayed combinatorial peptide library was used to define the specificity of one of the three Src homology 3 (SH3) domains in a novel cytoskeletal protein, named CAP, for Cbl Associated Protein. The C-terminal SH3 domain was used to affinity select peptides with the consensus, PXPPXRXSSL, from a library of X6PXXPX6 peptides. Peptide sequences resembling this consensus were identified in two signal transduction proteins, c-Cbl and son-on-sevenless (Sos), previously shown to interact with the C-terminal SH3 domain of CAP. Genetic fusion of 16 and 14 amino acid segments of c-Cbl and Sos, respectively, to bacterial alkaline phosphatase confirmed that these segments were potential ligand sites for the C-terminal SH3 domain of CAP. Alanine-scanning mutagenesis of the c-Cbl peptide ligand confirmed that most of the residues, which were conserved among the peptide ligands selected from the combinatorial peptide library, contributed to binding to the C-terminal SH3 domain of CAP.
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PMID:Molecular recognition properties of the C-terminal Sh3 domain of the Cbl associated protein, Cap. 989 38

Collapsin-1/Sema III, a member of the semaphorin family, has been implicated in axonal pathfinding as a repulsive guidance cue. Cellular and molecular mechanisms by which collapsin-1 exerts its action are not fully understood. Collapsin-1 induces growth cone collapse via a pathway which may include neuropilin-1, a cellsurface collapsin-1 binding protein, as well as intracellular CRMP-62 and heterotrimeric G proteins. We previously identified a second action of collapsin-1, the facilitation of antero- and retrograde axoplasmic transport. This response occurs via a mechanism distinct from that causing growth cone collapse. To investigate the possible involvement of neuropilin-1 in the action of collapsin-1 on axoplasmic transport, we produced a soluble neuropilin-1 (sNP-1) lacking the transmembrane and intracellular region. sNP-1 progressively displaced the dose-response curve for collapsin-1 to induce growth cone collapse to higher concentrations. sNP-1 also inhibited collapsin-1-induced augmentation of both antero- and retrograde axoplasmic transport. Furthermore, an anti-neuropilin-1 antibody blocked the collapsin-induced axoplasmic transport. These results together indicate that neuropilin-1 mediates collapsin-1 action on axoplasmic transport. To visualize collapsin-1 binding to endogenous neuropilin-1, we used a truncated collapsin-1-alkaline phosphatase fusion protein (CAP-4). CAP-4 stains the growth cone, neurite, and cell body. However, local application of collapsin-1 to growth cone but to neither neurite nor cell body promotes axoplasmic transport. Thus, growth cone NP-1 mediates the facilitatory action of collapsin-1 on antero- and retrograde axoplasmic transport.
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PMID:Growth cone neuropilin-1 mediates collapsin-1/Sema III facilitation of antero- and retrograde axoplasmic transport. 1038 79


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