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)

In active odontoblasts from the rat incisor, used as a model system for biologic calcification, two distinguishable enzyme activities capable of degrading adenosine monophosphate (ATP) exist. Once can be inhibited ny 1-tetramisole, (+/-)-2,3,5,6,-tetrahydro-6-phenylimidazo (2.1B) THIAZOLE HYDROCHLORIDE (Levamisol) and (+/-)-6(m-bromophenyl)-5.6-dehydroimidazo (2.1-b) thiazole oxalate (R823) and is probably identical with nonspecific alkaline phosphatase (EC 3.1.3.1). The activity of the other enzyme, named Ca2+-ATPase, is dependent on the presence of Ca2+ or Mg2+ and is activated by these ions. The pH optimum of Ca2+-ATPase is 9.8. The Ca2+-ATPase is unaffected by Levamisole, R 8231, ouabain, ruthenium red, Na+ and K+ ions. Maximal activity was found against ATP, whereas adenosine diphosphate, guanosine triphosphate, inosine triphosphate and adensoine monophosphate were hydrolysed at lower rate. It may be speculated that the Ca2+-ATPase is concerned with the transmembranous transport of Ca2+ ions to the mineralization front.
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PMID:A comparison of ATP-degrading enzyme activities in rat incisor odontoblasts. 0 54

The localization of alkaline phosphatases in dentinogenically active rat incisor odontoblasts was studied by means of subcellular fractionation and electron microscopical histochemistry. Subcellular fractionation revealed the predominant phosphatase activity to be present in the microsome fraction and to a lesser extent in the mitochondrial fraction. Adenosine triphosphate degrading enzyme activity was determined in the presence or absence of (+/-)-6(m-bromophenyl)-5, 6-dihydroimidazo(le) (2,1-b) thiazole oxalate (R 8231). Before the histochemical study, the effects on phosphatase activities by aldehyde fixation were studied by biochemical assay. A method of fixation for optimal preservation of phosphatase activity is presented. Phosphatase electron microscopic histochemistry was performed by using ATP as a substrate and with or without addition of the inhibitor R 82319 Precipitates were seen in the membranes of vesicles present in the odontoblast process and the Golgi region. When there were signs of insufficient fixation, precipitates were also seen in the outer membranes of mitochondria. No phosphatase activity was seen in the cell membrane. ATP degrading enzyme activities mediated by nonspecific alkaline phosphatase (APase) and Ca2+ -adenosine triphosphatase thus have the same morphological localization. This close association is consistent with earlier biochemical studies.
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PMID:Ultrastructural localization of alkaline phosphatases in rat incisor odontoblasts. 2 17

Ca2+-ATPase activity was solubilized, partly purified, and separated from nonspecific alkaline phosphatase activity (APase1) of dentinogenically active rat incisor odontoblasts. Attempts were made to extract the enzymes by various agents, such as Triton X-100, deoxycholate, butanol, EDTA, and buffers of decreasing ionic strength. Solubilization by butanol followed by extraction with low concentrations of EDTA proved to be most effective. Purification and separation were done by molecular sieve chromatography. Ca2+-ATPase showed no activity against p-nitrophenyl phosphate (p-NPP) or inorganic pyrophosphate (PPi) and was unaffected by R 8231 [+/-)-6(m-bromophenyl)-5,6-dihydroimidazo(2,1-b)thiazole oxalate]. It was activated by Ca2+ and Mg2+ ions in equimolar concentrations with the substrate. The enzyme was rapidly inactivated in the solubilized state. An apparent molecular weight of about 18,000 was obtained from molecular sieve data. APase, showing activity against ATP, PPi, and p-NPP, was virtually totally inhibited by R 8231. It was activated by Mg2+ ions but slightly reduced in activity by Ca2+ ions. It had an apparent mol. wt. of 79,000. The results provide direct evidence for earlier suggestions of the existence in hard tissue forming cells of two phosphatases active at alkaline pH.
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PMID:Separation of odontoblast Ca2+-ATPase and alkaline phosphatase. 15 25

A method for isolating a plasma membrane-enriched fraction and other subcellular fractions from rat mesenteric arteries by the use of a discontinuous sucrose density gradient is decribed. Electron microscopy showed both plasma membrane and endoplasmic reticulum fractions to be composed of vesicles. 5'-Nucleotidase, alkaline phosphatase, ouabain-sensitive (Na+ + K+)-ATPase and K+-phosphatase, and phosphodiesterase I were concentrated in the plasma membrane fraction. The increase in ATP-dependent calcium uptake in the presence of oxalate was greater in the endoplasmic reticulum than in the plasma membrane fraction. The lack of inhibition of active calcium uptake by azide suggests that the plasma membrane-enriched fraction was relatively free of mitochondrial contamination. Calcium uptake by the plasma membrane or the endoplasmic reticulum fraction was not enhanced by high-energy compounds other than ATP, and was little affected by 100 mM KCl or NaCl in the Mg++-containing medium. Subcellular fractions isolated by this method will be useful for investigating the biochemistry of small blood vessels of the rat.
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PMID:Isolation and characterization of plasma membrane from rat mesenteric arteries. 18 63

The safety and effectiveness of sodium cellulose phosphate (SCP) in the treatment of calcium urolithiasis of absorptive hypercalciuria was explored. Eighteen patients with absorptive hypercalciuria with intestinal hyperabsorption of calcium, normal or suppressed parathyroid function, and active stone disease received 10 to 15 Gm SCP daily (2.5 to 5 Gm with meals) and 2 to 3 Gm magnesium gluconate daily (1 to 1.5 Gm twice daily orally separately from SCP) for eight to 54 months, while maintained on a moderate calcium and oxalate restriction. During treatment, serum calcium, immunoreactive parathyroid hormone, and urinary cyclic AMP remained within the normal range. Serum alkaline phosphatase and bone density (measured by photon absorptiometry) did not change significantly or remained within normal limits. Serum concentrations of magnesium, copper, zinc, and iron and blood hematocrit were not significantly altered by therapy. However, urinary calcium returned toward normal, and incidence of renal stone formation markedly decreased. The results suggest that SCP is a safe and an effective drug for absorptive hypercalciuria.
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PMID:Clinical pharmacology of sodium cellulose phosphate. 48 64

A series of tetramisole derivatives was synthesized and tested for inhibitory activity against alkaline phosphatase which was partially purified from a murine ascitic neoplasm resistant to 6-thiopurines (Sarcoma 180/TG). These agents included derivatives substituted with halogens, CH3, or NO2 groups at either the meta or para position of the phenyl ring of tetramisole and 2,3-dehydrotetramisole. The phenyl ring of tetramisole and 2,3-dehydrotetramisole was also replaced by a naphthyl ring, and the phenyl ring of 2,3-dehydrotetramisole was substituted by a thienyl ring system. The presence of both the thiazolidine and dihydroimidazole rings of tetramisole was found to be essential for enzyme inhibitory activity. Substitution of a naphthyl for the phenyl group and dehydrogenation at the 2,3 position of the thiazolidine ring were found to significantly enhance inhibitory activity for alkaline phosphatase. Tests employing (S)-(-)-6-(4-bromophenyl)-2,3,5,6-tetrahydroimidazo[2,1-b]thiazole oxalate in combination with 6-thioguanine demonstrated that the inhibitor of alkaline phosphatase was capable of increasing the toxicity of 6-thioguanine to Sarcoma 180/TG cells in tissue culture.
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PMID:Tetramisole analogues as inhibitors of alkaline phosphatase, an enzyme involved in the resistance of neoplastic cells to 6-thiopurines. 55 60

To evaluate some of the early effects of methymercury chloride (MMC) male rats were given 10, 20 or 30 mg MMC/kg intraperitoneally. Urine was analysed for vanilmandelic acid (VMA), leucine aminopeptidase (LAP), alkaline phosphatase (AP), and creatinine, blood for glucose-6-phosphatase (G-6-P) and glucose, serum for glutamate-oxalate-transaminase (GOT) and urea. Except for LAP and AP excretion there is no effect of MMC on the parameters investigated. However, the effects on these 2 renal enzymes are to variable to permit their use as a test for MMC toxicity.
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PMID:Effect of methylmercury on some constituents of serum and urine. 71 3

In experimental investigations on Eimeria stiedai infected rabbits, serum enzymatic studies have been carried out in correlation with the examination of parasitological and pathological parameters. The rabbits were orally infected with a single dose of either 100,000 or 250,000 sporulated oocysts. Increase of the activity of the sorbit dehydrogenase (SDH), glutamate oxalate transaminase (GOT), glutamate pyruvate transaminase (GPT) and glutamate dehydrogenase (GlDH) could be found first between 3 and 10 days after infection indicating the beginning of the acute phase of liver coccidiosis. The increase of the conjugated bilirubin and of the gamma-glutamyl-transferase (gamma-GT) could be found not earlier than 10 days after infection and is to be explained as sign of disturbed efficiency of excretion. The various investigated parameters reached their peak of alteration about the end of the prepatent period and at the beginning of patency between 14 and 21 days after infection. The results emphasize the value and usefulness of serum enzymes, particularly the glutamate dehydrogenase (GlDH) and the gamma-glutamyl-transferase (gamma-GT) with about 30fold activity, as indicators in the course of Eimeria stiedai infection of rabbits. The enzymes returned to physiological values at the end of the experiment, 42 days after infection. Significant differences could not be detected within the infected groups. The activities of the alkaline phosphatase (AP), leucine aminopeptidase (LAP), choline esterase (ChE), lactate dehydrogenase (LDH) and isoenzym 1 (alpha-HBDH) showed only slight alterations and proved to be no significant parameters for the pathophysiological evaluation of the liver coccidiosis.
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PMID:[Alteration of enzyme activities in serum of Eimeria stiedai infected rabbits (author's transl)]. 73 5

Some biochemical and enzymatic constituents were determined in the small intestinal tract tissues of normal and sodium glycollate treated adult male rats. Alterations were observed with respect to certain lipids and carbohydrate fractions in the glycollate fed rats. DNA content was also elevated in this group. The functions of the cell membrane is likely to be affected as reflected in the levels of transport ATPases and orthophospho-hydrolases. The activities of the two marker enzymes in the intestinal brush border, namely alkaline phosphatase and leucylnaphthylamidase were reduced in the glycollate administered group. Administration of L(+)-tartrate, which is a mild laxative and has a regulatory influence on oxalate metabolism, lowered the activities of Na+, K(+)- and Ca(2+)-ATPases. There was a distinct lowering in the level of acid phosphatase in the tartrate treated rats.
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PMID:Effect of L(+)-tartrate on some biochemical and enzymatic parameters in normal and glycollate treated rats. 133 23

Biochemical studies were performed on 22 adult patients with idiopathic recurrent calcium oxalate renal stone disease and 23 healthy controls. It was found that urinary glutamic-oxaloacetic acid transaminase (UGOT) and urinary glutamic-pyruvic acid transaminase (UGPT) activity was low and lactate dehydrogenase (LDH) and gamma-glutamyl transferase (gamma-GT) activity was high in the urine of calcium oxalate stone formers. No significant changes were observed in the activity of glutamic-oxaloacetic acid transaminase, glutamic-pyruvic acid transaminase and gamma-GT in their blood but a significant reduction was found in both LDH and alkaline phosphatase activity. It was concluded that the activity of UGOT and UGPT is reduced in patients with kidney stones.
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PMID:Observations on calcium oxalate stone formers. 136 3


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