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)

In rats exposed for 12 weeks to the mixture of nitric oxides (0.34--2.81 mg/m3) and chlorine (0.61--1.50 mg/m3) the following changes were found: increased methemoglobin concentration (MetHb), increased partial pressure, increased total carbon dioxide concentration (pCO2 TCO2), increased current dicarbonate concentration (AB), and increased buffer bases (BB). In addition, asparagine transferase activity (aspAT), alanine aminotransferase (A1AT), alkaline phosphatase (AP) and hepatic isoenzyme of lactic dehydrogenase (LDH5) in serum were found to be increased. Histopathological examination revealed: inflammatory lesions and edema of pulmonary parenchyma, alveolar emphysema and edema of connective tissue of palpetra derm with mastocytes. Chronic exposure to low concentrations of nitric oxides and chlorine induces, apart from local lesions in conjunctivae, pulmonary lesions leading to respiratory acidosis compensated by metabolic alkalosis, or liberation of indicatory enzymes through impaired cells.
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PMID:[Chemical hazards connected with electrochemical machining. I. Toxicity of nitric oxides and chlorine lesions in rats' parenchymatous organs]. 50 41

The effect of intraperitoneally administered penicillic acid, a mycotoxin produced by several species of Penicillium and Aspergillus, on female dogs of mixed breeding was determined by serum tests, by observation of clinical signs and survival times, and by evaluation of gross and microscopic lesions. Combination studies employing penicillic acid and a second mycotoxin, rubratoxin B, also were undertaken. Post mortem examination disclosed hemorrhaging of the serosal surfaces of the abdomen of dogs receiving penicillic acid. The most significant histologic change observed in penicillic-acid-treated dogs was congestion and dilatation of hepatic sinusoids. Extensive hepatic changes of the liver were noted only in the dog receiving 20 mg/kg penicillic acid. There was no evidence of parenchymal necrosis in any of the liver samples examined from animals given penicillic acid. A predominently peripheral lobular depletion of glycogen in parenchymal cytoplasm also was seen in liver sections from animals exposed to penicillic acid. Although slight decreases in lactic dehydrogenase were observed, no trends were detected in the several blood enzymes and serum constituents examined that could be specifically related to penicillic acid intoxification. Glutamic-oxaloacetic transaminase, lactic dehydrogenase and alkaline phosphatase activities and survival time varied in relation to duration of exposure and total dose of rubratoxin B administered. The lesions in animals injected with 1.0 mg/kg rubratoxin B consisted of mild hepatic necrosis and degenerative changes in renal tubular epithelium. An additive effect due to the combined administration of penicillic acid and rubratoxin B was observed only by an elevation in serum sodium and chlorine levels.
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PMID:Acute toxicity of penicillic acid and rubratoxin B in dogs. 58 Jun 98

Twelve blood serum parameters: sodium, potassium, chlorine, total protein, cholesterol, glucose, urea nitrogen, creatinine, bilirubin, alkaline phosphatase, alanine and aspartate aminotransferases activities were measured in 488 normal subjects (male), residents of Leningrad, by the Technicon (USA) microanalyzer. Relationships between the estimated reference values and the distribution patterns of the referent blood parameters (variability, symmetric pattern) were analyzed. The authors compare the reference values of the Leningrad population with those obtained by this microanalyzer in the USA.
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PMID:[Characteristics of the distribution and reference values of 12 biochemical indices of the blood serum]. 171 39

We have carried out an experimental model of urinary diversion and dis-diversion on male Wistar rats in order to study the complications that are produced after diversion, as well as to see whether the alterations continue unchanged, or increase, or diminish after dis-diversion. The following experimental design was used: a control group made up of 48 animals an a problem group of 200 animals all submitted to vesicosigmoidostomy of which 100 were designed to be subsequently dis-diverted. The sacrificed animals (n = 112) were studied for somatic, biochemical and histological parameters. Statistical comparison of the problem group with the controls showed significant differences for the somatic and biochemical parameters, especially in the form of weight-size retardation, increase of urea, creatinine, calcium, phosphorus, uric acid, cholesterol, transaminase, alkaline phosphatase, sodium and chlorine and decrease in albumin and total proteins. After dis-diversion there is an improvement of some of these parameters without reaching total normalization. This leads us to think that either the lesions are irreversible, or more time after dis-diversion is needed for there to be reversibility. We also describe the histological lesions found at the level of the vesicointestinal anastomosis, and the mortality of our series which is higher than that presented by females, a fact inducing us to think that factors exist in the male which increase the mortality.
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PMID:[Urinary de-diversion after diversion with chronic bladder contamination. An experimental study in male rats]. 206

Exposure for 20 min of stationary phase cells of Salmonella typhimurium to a combined triple stress system (TSS) treatment comprising hypochlorite derived 5 ppm free available chlorine in solution acidified with 1% succinate (pH 2.5) and at a chill shock temperature of 5 degrees C resulted in symptoms of injury. Cells became sensitive to 40 micrograms/ml lysozyme, 50 micrograms/ml actinomycin D and 100 micrograms/ml ribonuclease B, to which control cells were resistant. Metabolic injury was indicated by reduction in colony forming ability of stressed cells on minimal salts glucose agar M9 medium. There was no detectable leakage loss of 260-280 nm-absorbing materials. This was also confirmed by assay of the cellular RNA material components. Loss of alkaline phosphatase activity was observed in the stressed cells. The intensity of induced cellular damage as measured by lysozyme sensitivity was greatest in the cells exposed to the complete TSS, followed by those stressed in 1% succinate at 5 degrees C, then 5 ppm chlorine at 5 degrees C and the singular chill shock stress at 5 degrees C, respectively. The magnitudes of cellular damage, however, were suggestive of synergistic interactions among the component stress factors of the TSS. The findings obtained indicated impairment of the structural integrity and functional capabilities of the permeability barriers and the inactivation of certain periplasmic enzymes. The resultant cumulative cellular damage from the TSS exposure may therefore enhance greater sensitivity of treated cells to subsequent stress factors.
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PMID:Mechanisms of triple stress-mediated damage in stationary phase cells of Salmonella typhimurium exposed to succinate-acidified hypochlorite system at 5 degrees C. 242

Transport of taurocholate into the hepatocyte against unfavorable chemical and electrical gradients occurs via a sodium-dependent, carrier-mediated transport system. Although this cotransporter has been characterized in the rodent, it has not been demonstrated in man. Therefore, we utilized human liver, obtained via multiorgan donation but not used for transplantation, to prepare basolateral (sinusoidal) liver plasma membrane vesicles by a Percoll gradient method. Na+,K+-ATPase, a marker enzyme for the basolateral domain, was enriched 28.9-fold in the final membrane fraction compared with homogenate, whereas the bile canalicular membrane enzymes Mg++-ATPase and alkaline phosphatase were enriched only 3.4- and 6.4-fold, respectively. Marker enzyme activities for endoplasmic reticulum, lysosomes and mitochondria were not enriched compared with homogenate. Integrity of the membrane vesicles was confirmed by the demonstration of Na+-dependent concentrative uptake of the amino acid L-alanine (estimated intravesicular volume of 0.59 microliter per mg protein). An inwardly directed 100 mM Na+ gradient stimulated the initial rate of 2.5 microM taurocholate uptake and energized a transient 2-fold accumulation of the bile acid above equilibrium ("overshoot"). In contrast, uptake was slower and no overshoot occurred with a K+ gradient. A negative intravesicular potential, created by altering accompanying anions or by valinomycin-induced K+ diffusion potentials, did not enhance taurocholate uptake, suggesting an electroneutral cotransport mechanism. Chloride as the accompanying anion stimulated the initial rate of uptake compared with anions of lesser or greater lipid permeability. Na+-dependent taurocholate (4 microM) uptake was significantly inhibited by 250 microM cholate, taurocholate, glycocholate, taurochenodeoxycholate and bromsulfophthalein.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Taurocholate transport by basolateral plasma membrane vesicles isolated from human liver. 277 5

Substitution reactions with biologic nucleophiles appear to govern the antitumor and toxic properties of platinum complexes. In this paper we have characterized the reactions of several platinum antitumor agents with sulfur-containing amino acids, peptides, proteins, and nonbiologic nucleophiles. The rate constants for the reactions of trans-diamminedichloroplatinum(II) (trans-DDP), cis-diamminedichloroplatinum(II) (DDP), diammine (1,1-cyclobutanedicarboxylato)platinum(II) (CBDCA) and cis-diisopropylamine-cis-dichloro-trans-dihydroxy platinum(IV) (CHIP) with cysteine (Cys), methionine (Met), and glutathione (GSH) were determined at 37 degrees. A reactivity ratio of 1:1.5:22:6500 was determined for the reaction of GSH with CHIP, CBDCA, DDP, and trans-DDP respectively. The rate constant for the binding of DDP to DNA, 7.4 X 10(-5) sec-1, decreased to 5.9 X 10(-5) sec-1 and 1.7 X 10(-5) sec-1 in the presence of 0.5 and 5 mM GSH respectively. The products formed in the reaction of GSH with trans-DDP, DDP, and CBDCA were also examined. Under conditions of high platinum concentration (2-3 mM), CBDCA and DDP form large molecular weight species with GSH as indicated by 1H-NMR and ultrafiltration experiments. The complex [Pt(GSH)2 X 3H2O]n was isolated from the reaction of 3 mM DDP with 6 mM GSH. The product formed in the reaction of 3 mM trans-DDP with 6 mM GSH was not macromolecular in nature, and 1H-NMR spectra revealed that platinum was bound to the Cys sulfhydryl group. Rate constants were determined for the reactions of these platinum complexes with diethyldithiocarbamate (DDTC) and thiosulfate, two agents known to reduce platinum-mediated nephrotoxicity. DDTC, but not thiosulfate, was shown to rapidly chelate platinum from [Pt(GSH)2 X 3H2O]n. The effects of DDP, CBDCA, and CHIP on the sulfhydryl-dependent rat renal proximal tubule membrane enzymes alkaline phosphatase (AP), gamma-glutamyltranspeptidase (GGTP), leucine aminopeptidase (LAP), and the Na+/K+- and Mg2+-adenosine-5'-triphosphatases (ATPases) were also investigated in vitro. The ability of platinum complexes to inhibit these enzymes parallels their reactivity with other nucleophiles. DDTC and thiourea were shown to restore activity to platinum-inhibited enzymes. Chloride ion was found to reduce platinum-mediated enzyme inhibition in an unpredictable manner, the greatest effect being observed with LAP and GGTP and the least with the ATPases. None of these renal enzymes was directly inhibited by DDP in vivo.
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PMID:Characterization of the reactions of platinum antitumor agents with biologic and nonbiologic sulfur-containing nucleophiles. 295 56

32 healthy persons, 12 men and 20 women, 19 to 48 years of age, were examined in the three positions--recumbent, sitting and erect. Blood was taken by venepuncture after 15 minutes stay in the position. The analyses were carried out with the discrete analyzer "PA-1000", flame photometer, chlorine titrator "Radiometer" and osmometer "Knauer". The statistical assessment was performed by the pair analysis. The changing of the body position from recumbent to sitting and to erect leads to a significant increase of the concentrations of the total protein and albumin which cannot pass through the capillary endothelial barrier following the changes in the hydrostatic and filtration pressure. The capillary endothelial barrier is permeable for the low-molecular compounds whose concentrations change insignificantly. Cholesterol and triglycerides are an exception since they are bound to nonfilterable lipoprotein complexes. Reliable increase of creatinine is found only in the women examined. Calcium which in the serum is protein-bound also increases significantly. A significant increase is found also of the activity of the enzymes creatine kinase, alkaline phosphatase and gamma GTP. The changes of the activity of the enzymes AsAT, AlAT, LDH and hydroxybutyrate dehydrogenase are insignificant.
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PMID:[Effect of body position on substrates, enzymes and electrolytes in the serum of healthy subjects]. 321 28

Serum biochemistry was monitored in 50 patients with otosclerosis confirmed surgically. Age distribution was 25 to 50 years (mean:30 years), and the group included 8 men. Constants determined were serum sodium, potassium, chlorine, iron, phosphorus, aluminium, magnesium, copper and alkaline phosphatase. All patients were free from systemic or metabolic disease. Results failed to demonstrate variations in sodium, potassium, iron, and chlorine concentrations when compared with controls, with non-significant differences in copper, magnesium, phosphorus, aluminium and alkaline phosphatases. These findings were observed both in young patients in whom the otosclerotic process is in the active phase, and in older patients, this excluding correlations between duration of the disease and variations in concentrations of specific ions. The presence of aluminium in the active otosclerotic process is therefore due to local factors of which the mechanism is unknown at the present time.
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PMID:[Concentration of various bioelements in the serum of otosclerosis patients]. 400 18

Chloride binding to alkaline phosphatase from Escherichia coli has been monitored by 35Cl NMR for the native zinc enzyme and by 113Cd NMR for two Cd(II)-substituted species, phosphorylated Cd(II)6 alkaline phosphatase and unphosphorylated Cd(II)2 alkaline phosphatase. Of the three metal binding sites per enzyme monomer, A, B, and C, only the NMR signal of 113Cd(II) at the A sites shows sensitivity to the presence of Cl-, suggesting that Cl- coordination occurs at the A site metal ion. From the differences in the chemical shift changes produced in the A site 113Cd resonance for the covalent (E-P) form of the enzyme versus the noncovalent (E . P) form of the enzyme, it is concluded that the A site metal ion can assume a five-coordinate form. The E-P form of the enzyme has three histidyl nitrogens as ligands from the protein to the A site metal ion plus either two water molecules or two Cl- ions as additional monodentate ligands. In the E . P form, there is a phosphate oxygen as a monodentate ligand and either a water molecule or a Cl- ion as the additional monodentate ligand. The shifts of the 113Cd NMR signals of the unphosphorylated Cd(II)2 enzyme induced by Cl- are very similar to those induced in the E-P derivative of the same enzyme, supporting the conclusion that the phosphoseryl residue is not directly coordinated to any of the metal ions. Specific broadening of the 35Cl resonance from bulk Cl- is induced by Zn(II)4 alkaline phosphatase, while Zn(II)2 alkaline phosphatase is even more effective, suggesting an influence by occupancy of the B site on the interaction of monodentate ligands at the A site. A reduction in this quadrupolar broadening is observed upon phosphate binding at pH values where E . P is formed, but not at pH values where E-P is the major species, confirming a specific interaction of Cl- at the A site, the site to which phosphate is bound in E . P, but not in E-P. For the zinc enzyme, a significant decrease in phosphate binding affinity can be shown to occur at pH 8 where one monomer has a higher affinity than the other.
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PMID:Chloride binding to alkaline phosphatase. 113Cd and 35Cl NMR. 638 93


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