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)

The effects of prostaglandins (PGs) on the induction of alkaline phosphatase (ALP) were investigated in osteoblastic clone MC3T3-E1 cells cultured in serum-free medium. Prostaglandin E2 (PGE2) stimulated ALP activity in the cells in a dose-dependent fashion with a maximal effect which was about twice that in the control cells at concentrations of 100-500 ng/ml. Actinomycin D and cycloheximide inhibited the stimulative effect of PGE2 on ALP activity in the cells. PGE2-induced and native ALPs in the cells were of the same type as that in adult mouse calvaria, being heat-labile, L-homoarginine- and levamisole-sensitive, and L-phenylalanine-insensitive. Isobutyl methylxanthine (IBMX), a cAMP phosphodiesterase inhibitor, stimulated the inductive effect of PGE2 on ALP activity at 0.1 mM, at which concentration IBMX alone had little effect on the activity. PGE2 also increased the intracellular cAMP content in a dose-dependent fashion with a maximal effect at 100 ng/ml. PGE1, PGF1 alpha, and PGF2 alpha (primary PGs like PGE2) increased the activity. Our present results suggest that PGs stimulate the differentiation of osteoblasts and are involved in bone formation in vivo, as well as in bone resorption.
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PMID:Inductive effects of prostaglandins on alkaline phosphatase in osteoblastic cells, clone MC3T3-E1. 258 42

During early sexual development in Dictyostelium discoideum cell and pronuclear fusion are negatively regulated by an endogenous autoinhibitor. Here, the autoinhibitor was partially purified from the culture medium and found to inhibit both cell and pronuclear fusion while augmenting gamete numbers. These developmental effects suggested that calmodulin might be an intracellular target for the autoinhibitor. In support of this data, the partially purified autoinhibitor inhibited the calmodulin-dependent activation of phosphodiesterase in a dose-dependent manner, but had no effect on either a calmodulin-insensitive form of phosphodiesterase or the calmodulin-independent enzymes acid and alkaline phosphatase. Thus, the autoinhibitor of sexual development in Dictyostelium discoideum appears to regulate cell and pronuclear fusion at least in part by a direct effect on calmodulin.
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PMID:The autoinhibitor of cell fusion in Dictyostelium inhibits calmodulin. 259 Jan 96

Bungarus candidus venom exhibited high hyaluronidase, acetylcholinesterase and phospholipase A activities; low proteinase, 5'-nucleotidase, alkaline phosphomonoesterase and phosphodiesterase activities and moderately high L-amino acid oxidase activity. SP-Sephadex C-50 ion exchange chromatographic fractionation of the venom and Sephadex G-50 chromatography of the major lethal venom fractions indicate that the venom contains at least two highly lethal, basic phospholipases A with LD50 (i.v.) values of 0.02 micrograms/g (F6A) and 0.18 micrograms/g (F4A), respectively; as well as two polypeptide toxins with LD50 (i.v.) values of 0.17 micrograms/g and 0.83 micrograms/g, respectively. The major lethal toxin is the basic lethal phospholipase A, F6A, which accounts for approximately 13% of the venom protein and has a mol. wt of 21,000.
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PMID:The lethal and biochemical properties of Bungarus candidus (Malayan krait) venom and venom fractions. 279 37

Rat sciatic nerve cytosol contains a phosphodiesterase of the phospholipase C type that catalyzes the hydrolysis of inositol phospholipids, with preferences of phosphatidylinositol 4'-phosphate (PIP) greater than phosphatidylinositol (PI) much greater than phosphatidylinositol 4',5'-bisphosphate (PIP2), at a pH optimum of 5.5-6.0 and at maximum rates of 55, 13, and 0.7 nmol/min/mg protein, respectively. Analysis of reaction products by TLC and formate exchange chromatography shows that inositol 1,2-cyclic phosphate (83%) and diacylglycerol are the major products of PI hydrolysis. [32P]-PIP hydrolysis yields inositol bisphosphate, inositol phosphate, and inorganic phosphate, indicating the presence of phosphodiesterase, phosphomonoesterase, and/or inositol phosphate phosphatase activities in nerve cytosol. Phosphodiesterase activity is Ca2+-dependent and completely inhibited by EGTA, but phosphomonoesterase activity is independent of divalent cations or chelating agents. Phosphatidylcholine (PC) and lysophosphatidylcholine (lysoPC) inhibit PI hydrolysis. They stimulate PIP and PIP2 hydrolysis up to equimolar concentrations, but are inhibitory at higher concentrations. Both diacylglycerols and free fatty acids stimulate PI hydrolysis and counteract its inhibition by PC and lysoPC. PIP2 is a poor substrate for the cytosolic phospholipase C and strongly inhibits hydrolysis of PI. However, it enhances PIP hydrolysis up to an equimolar concentration.
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PMID:Inositol phospholipid hydrolysis by rat sciatic nerve phospholipase C. 282 95

Two regulatory mutants in orthophosphate-regulated cyclic phosphodiesterase (cPDase), cpd-3 and cpd-4, were isolated and mapped proximal to arg-1 on L.G. IC and distal to arg-12 on L.G. IIR, respectively. cpd-3 showed short aerial hyphae with dense formation of conidia. The morphology was very similar to that of cr-1, cpd-3 and cr-1 had reduced levels of cyclic 3',5'-AMP, adenylate cyclase and cPDases (CPDase I, II and III in low phosphate condition) but had elevated levels of cyclic 3',5'-GMP. Although cr-1 showed an enhanced level and enhanced activation of heat activated cyclic phosphodiesterase (ha-PDE), this enzyme was not activated in cpd-3. cpd-4, nuc-1 and nuc-2 produced neither cPDase I, II, III, alkaline phosphatase nor ribonuclease N1 in low phosphate media. These mutants did not produce aerial hyphae or conidia when grown in low phosphate liquid medium. Activation of ha-PDE occurred in cpd-4, but not in nuc-1 and nuc-2.
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PMID:Mutations affecting cyclic phosphodiesterases and adenylate cyclase in Neurospora. 283 77

Soluble and membrane-bound phosphatase and phosphodiesterase activities are present in preparations of 1,3-beta-D-glucan synthase from pea epicotyls. UDP-glucose phosphodiesterase and non-specific alkaline phosphatase could be partially inhibited by N-ethylmaleimide or iodoacetamide and partially removed from membranes by washing. Such treatments helped to prolong 1,3-beta-glucan synthase activity. Nevertheless, the 1,3-beta-D-glucan synthase activity in washed membranes still gradually decreased during incubation in buffer at 30 degrees C. The rate of decay was reduced by adding more specific phosphatase inhibitors, e.g. molybdate, vanadate or fluoride, or by addition of nucleotides, and much of the loss of 1,3-beta-D-glucan synthase activity during preincubation could be restored by addition of phosphatidylethanolamine to the assay mixtures. It is concluded that membrane phospholipid is an essential part of the environment of 1,3-beta-glucan synthase and must be maintained intact in order for the enzyme to remain fully active.
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PMID:Phosphatases and phosphodiesterases interfere with 1,3-beta-D-glucan synthase activity in pea epicotyl membrane preparations. 284 92

1. The L-amino acid oxidase, hyaluronidase, alkaline phosphomonoesterase, protease, phosphodiesterase, acetylcholinesterase, phospholipase A and 5'-nucleotidase activities of 47 samples of venoms from all the six species of cobra (Naja), including five subspecies of Naja naja, were examined. 2. The results demonstrated interspecific differences in the venom contents of phospholipase A, acetylcholinesterase, hyaluronidase and phosphodiesterase. These differences in venom enzyme contents can be used for the differentiation of species of the genus Naja. 3. Thus, our results revealed a correlation between the enzyme composition of venom and the taxonomic status of the snake at the species level for the genus Naja.
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PMID:A comparative study of cobra (Naja) venom enzymes. 285 66

The properties of the enzymes involved in Ca2+-stimulated breakdown of phosphatidylinositol 4'-phosphate (PIP), phosphatidylinositol 4',5'-bisphosphate (PIP2), and phosphatidic acid (PA) in rabbit erythrocyte ghosts were studied. At 25 degrees C, 1 to 180 microM Ca2+ rapidly stimulated the breakdown of PIP and PIP2, and maximal breakdown occurred within 10 minutes at all Ca2+ concentrations. The rate and the total amount of breakdown of PA, PIP, and PIP2 increased with Ca2+ concentration. MgCl2 inhibited the rate of Ca2+-stimulated breakdown of PIP and PIP2 at Ca2+ concentrations less than 10 microM, but did not have any appreciable effects at higher Ca2+ concentrations. MgCl2 also protected against Ca2+-stimulated breakdown of PA. In the presence and absence of 5 mM MgCl2, Ca2+ stimulated half-maximal breakdown of PIP and PIP2 at 2-3 microM under hypotonic and isotonic conditions. In the presence of 5 mM MgCl2, Ca2+-stimulated breakdown of PIP and PIP2 was associated with the release of Pi and inositol bisphosphate. In the absence of MgCl2, Ca2+ stimulated the release of 32P-labeled Pi, inositol bisphosphate, and inositol trisphosphate from labeled PIP, PIP2, and PA. Ca2+ increased phosphatidylinositol content and decreased PIP and PIP2 content in these membranes. The results of this investigation suggest that Ca2+ stimulates the breakdown of polyphosphoinositides by stimulating polyphosphoinositide phosphomonoesterase and phosphodiesterase activities in rabbit erythrocyte ghosts. These activities were activated by less than 3 microM Ca2+ in the presence of MgCl2 under hypotonic or isotonic conditions. These Ca2+-stimulated polyphosphoinositide phosphoesterase activities could therefore be active under physiological conditions in normal rabbit erythrocytes.
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PMID:Ca2+-stimulated phospholipid phosphoesterase activities in rabbit erythrocyte membranes. 298 4

Pure alkaline phosphatase of the calf intestine is able to hydrolyze phosphatidylinositol 4,5-diphosphate (TPI) to phosphatidylinositol and Pi and to dephosphorylate phosphatidic acid. This phosphomonoesterase activity shows a considerably high specific activity when an incubation medium at neutral pH containing 3 mM deoxycholate is used. The activity is inhibited by low concentrations of Ca2+. The enzyme has no detectable phosphodiesterase activity under the conditions tested.
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PMID:Alkaline phosphatase of the calf intestine hydrolyzes phospholipids. 298 37

Purified brush border membrane of Cotugnia digonopora showed the presence of a number of phosphohydrolases. Among these, alkaline phosphatase was extremely active. Other enzymes such as glucose-6-phosphatase, fructose-1,6-diphosphatase, cAMP-phosphodiesterase, 5'-nucleotidase and adenosine-triphosphatase were also active. Observations were made on the activities of various ATPases; whereas the enzyme was activated by Ca++ and Mg++ in an additive manner, its sensitivity to ouabain was negligible. Furthermore, in the presence of EDTA the enzyme activity was quite significant. The treatment of isolated brush border membrane with mebendazole, niclosamide and praziquantel in vitro did not alter the activity of these enzymes. However, treatment of intact worms drastically affected the integrity of the membrane.
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PMID:Enzymes of isolated brush border membrane of Cotugnia digonopora, and their insensitivity to anthelmintics in vitro. 299 11


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