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 release of plasma-membrane-bound enzymes by phosphatidylinositol-specific phospholipase C obtained from Bacillus thuringiensis was investigated. Among the ectoenzymes of plasma membrane tested, alkaline phosphodiesterase I was released markedly from rat kidney cortex slices, in addition to alkaline phosphatase and 5'-nucleotidase. Other membrane-bound enzymes; alanine aminopeptidase, leucine aminopeptidase, dipeptidyl peptidase, leucine aminopeptidase, dipeptidyl peptidase IV, esterase and gamma-glutamyl transpeptidase could not be liberated from the treated slices. Alkaline phosphodiesterase I was released linearly from rat kidney slices with the concentration of phosphatidylinositol-specific phospholipase C, but little enzyme was released from rat liver slices. Alkaline phosphodiesterase I separated from kidney tissue with n-butanol still retained phosphatidylinositol and was transformed into a lower molecular weight form by phosphatidylinositol-specific phospholipase C. This suggests an important function for phosphatidylinositol in the binding of alkaline phosphodiesterase I to the plasma membrane of rat kidney cells. The alkaline phosphodiesterase I released from rat kidney had a molecular weight of about 240,000 and an isoelectric point (pI) of 5.4. The enzyme hydrolyzed the phosphodiester linkage of p-nitrophenyl-thymidine 5'-monophosphate at pH 8.9 and had a Km value of 0.3 mM. The enzyme was activated by Mg2+ and Ca2+, but was inhibited by EDTA. Strong inhibition took place on the addition of adenosine 5'-phosphosulfate or the nucleotide pyrophosphates, i.e., UDP-galactose and alpha, beta-methylene ATP.
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PMID:Release of alkaline phosphodiesterase I from rat kidney plasma membrane produced by the phosphatidylinositol-specific phospholipase C of Bacillus thuringiensis. 609 28

Human lymphocytes were isolated from defibrinated blood by Ficoll-Hypaque centrifugation with erythrocyte hypotonic lysis. Homogenates of mixed lymphocytes were subjected to analytical subcellular fractionation by sucrose gradient centrifugation in a Beaufay automatic zonal rotor. The principal organelles were characterized by their marker enzymes: cytosol (lactate dehydrogenase), plasma membrane (5'-nucleotidase), endoplasmic reticulum (neutral alpha-glucosidase), mitochondria (malate dehydrogenase), lysosomes (N-acetyl-beta-glucosaminidase), peroxisomes (catalase). gamma-Glutamyl transferase was exclusively localized to the plasma membrane. Leucine amino-peptidase, especially when assayed in the presence of Co2+, was also partially localized to the plasma membrane. Experiments with diazotized sulphanilic acid, a non-permeant enzyme inhibitor, showed that these plasma membrane enzymes are present on the cell surface. No detectable alkaline phosphatase was found in the lymphocytes. Acid phosphatase and beta-glucuronidase were localized to lysosomes and there was some evidence for lysosomal heterogeneity. Leucine amino peptidase, optimal at pH 8.0, showed a partial localization to intracellular vesicles, possibly lysosomes, especially when assayed in the presence of EDTA. These studies provide a technique for determining the intracellular distribution of hitherto unassigned lymphocyte constituents and serve as a basis for investigating the cell pathology of lymphocytic disorders.
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PMID:Enzyme analysis and subcellular fractionation of human peripheral blood lymphocytes with special reference to the localization of putative plasma membrane enzymes. 614 55

The levels of ornithine carbamyl transferase, acid phosphatase, alkaline phosphatase, leucine amino peptidase, creatine kinase, amylase, glutamic oxalacetic transaminase, glutamic pyruvic transaminase, lactate deshydrogenase, hydroxybutyrate deshydrogenase, glutamate deshydrogenase and malate deshydrogenase were determined in the plasma of Rainbow Trout and Tench submitted to water temperature increases. In the Rainbow Trout a thermal shock from 12 to 21 degrees, increases activities of some enzymes while temperature increase up to pre-mortem stage causes very important changes in enzymatic levels. In the Tench a thermal shock from 12 to 28 degrees causes more changes of enzymatic activities than a shock from 12 to 25 degrees. In Tench acclimated to 25 degrees, various enzyme levels are increased in comparison with 12 degrees control animals. A high potassium level in water causes complex changes in enzyme levels. The most sensitive enzymes to thermal disturbance are GOT and GPt transaminases which increase whatever the aggression form, amylase when thermal disturbance is moderate, alkaline phosphatase and malate deshydrogenase in case of strong thermal stress. The study of these enzymes is recommended for watching the state of fishes living in artificially heated waters.
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PMID:[Activities of twelve enzymes in the blood plasma of rainbow trout and tench subjected to various forms of thermal disturbance]. 616 76

The two most commonly used biochemical markers of bone turnover are the serum alkaline phosphatase and the urinary excretion of peptide-bound hydroxyproline, both of which are increased in Paget's disease. Serum alkaline phosphatase is assumed to be derived from osteoblasts during the process of bone formation, whereas small peptides containing hydroxyproline are excreted in the urine following the degradation of bone collagen. The alkaline phosphatase is probably the more useful measurement for diagnosis and for following response to treatment, whereas hydroxyproline, although very sensitive, presents technical difficulties in collection and measurement. Several other biochemical changes in Paget's disease indicate abnormal bone metabolism. These include increased urinary excretion of hydroxylysine and its glycosides derived from collagen, as well as the release into the circulation and subsequent urinary excretion of fragments of pro-collagen indicative of increased collagen formation. Proteins specific to bone, such as osteocalcin, are increased in serum, bone, such as osteocalcin, are increased in serum, as are various enzymes possibly derived from bone cells, including acid phosphatase and proline imino-peptidase. Treatment of Paget's disease results in a fall in urinary hydroxyproline before alkaline phosphatase. This indicates that drug treatment, whether with diphosphonates, calcitonin or mithramycin, has a primary action to inhibit bone resorption, with a subsequent adaptive reduction in bone formation rate.
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PMID:Biochemical markers of bone turnover in Paget's disease. 622 Jan 91

Activity of lysosomal hydrolases, cathepsins A and D, acid phosphatase, was induced in inflamed rat hypodermic tissue. Simultaneously, cytoplasmic enzymes leucine amino-peptidase and alkaline phosphatase were activated in the tissue. At the same time, activity of thiol-dependent enzymes/cathepsins B and C/ was decreased in all preparations studied. The data obtained suggest that both lysosomal and membrane-bound hydrolases participated in development of inflammation. Besides, proliferation of the hypodermic tissue appears to effect, by means of mediator and metabolite systems, on activity of intracellular enzymes in other tissues studied, which were not related directly to the impairment.
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PMID:[Activity of various intracellular hydrolases in experimental inflammation]. 627 Sep 5

Bone cells released from perinatal rat calvaria by digestion with clostridial peptidase were separated into two distinct populations (designated types B and C) by equilibrium density centrifugation on a two-step gradient of Percoll. They were extensively characterized by light and electron microscopy and for behaviour in culture, acid and alkaline phosphatase activity, collagen synthesis, collagenase secretion and adenylate cyclase response to parathyroid hormone (PTH) and calcitonin. Type C cells were predominantly large with up to seven nuclei and an unusual cytoplasmic appearance in cytocentrifuge preparations. They did not proliferate in culture and we have established culture conditions which prevented their overgrowth by contaminating proliferative cells. In culture these cells had low alkaline and high acid phosphatase and high aryl sulphatase activity, and synthesized little collagen. In contrast type B cells were mostly smaller and many had irregular cytoplasmic projections. In culture they became polygonal in shape, proliferated rapidly, and reached confluence in 4-5 days. These were low in aryl sulphatase and acid phosphatase, high in alkaline phosphatase activity, and synthesized labelled collagen actively with [3H]proline and ascorbic acid included in the culture medium. The two cell population were found to differ in culture in two important further respects. First, the type C cells showed an adenylate cyclase response to calcitonin but not to PTH, while the converse was true for type B cells; this was so over at least a 20-fold range of isobutylmethyl xanthine concentration. Secondly, type C cells in culture secreted an active collagenolytic enzyme. Type B cells secreted much lower levels of a predominantly latent collagenase which required activation by mersalyl. Co-culture of type C and type B cells led to a marked reduction in the content of active collagenase in the culture medium.
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PMID:Separation of two bone cell populations from fetal rat calvaria and a study of their responses to parathyroid hormone and calcitonin. 631 50

The effect of vincristine treatment on the morphofunctional status of the small intestine was studied morphologically in 80 Wistar rats. The drug was found to possess a general toxic effect. Diarrhea was matched by the arrest of crypt cell-proliferation at metaphase, lysis, a decreased disaccharidase activity and increased levels of cytoplasmic alkaline phosphatase and dipeptidyl(amino)peptidase-IV in enterocytes of the villi. Exudation and degenerated cell organellae prevailed in intramural nervous ganglion cells, smooth muscle cells of intestinal tunica muscularis and vessels and in endothelium. The said changes were transitory in epithelium, but never regressed in nervous structures. At later stages (6-12 months after vincristine, but never regressed in endothelium. The later stages (6-12 months after vincristine treatment), secondary dystrophic changes developed in the small intestine wall, being predominantly confined to neuromuscular and vascular elements.
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PMID:[The effect of vincristine on the morpho-functional state of the rat small intestine]. 648 90

Extracellular matrix vesicles from bovine fetal alveolar bone and from a dog osteosarcoma were isolated by differential centrifugation and then fractionated on a discontinuous sucrose density gradient. The fractions were examined by electron microscopy and were analyzed for protein, alkaline phosphatase, aminotripeptidase, and four different beta-naphthylamidase activities. The low-density peak of enzyme activities was shown by electron microscopy to be much more homogeneous than the crude matrix vesicle fraction. Two major peaks of protein and enzyme activities were present, one in the high and one in the low density layers. There was good correlation between the activities of alkaline phosphatase and the various peptidases in the fractions from the sucrose density gradient. These results indicate a coexistence of peptidase and alkaline phosphatase in matrix vesicles. On the other hand, there was generally no correlation between the peptidase and alkaline phosphatase activities in vesicular specimens from bovine liver obtained in the same way. Most of the peptidase activity and about half of the alkaline phosphatase activity were solubilized from bone matrix vesicles by detergents. The extracted alkaline phosphatase and alanyl beta-naphthylamidase activities were separated from each other on a DEAE-cellulose column.
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PMID:Neutral peptidase activities in matrix vesicles from bovine fetal alveolar bone and dog osteosarcoma. 665 55

The subcellular biochemical features of a naturally occurring enteropathy in the dog associated with bacterial overgrowth have been examined. Affected animals comprised a group of 10 German Shepherd dogs with raised serum folate and reduced vitamin B12 concentrations, mild steatorrhoea, reduced xylose absorption, and normal exocrine pancreatic function. Culture of duodenal juice showed bacterial overgrowth with mixed flora, most frequently including enterococci and Escherichia coli. Examination of peroral jejunal biopsies revealed predominantly minimal histological but distinct biochemical abnormalities in the mucosa. The specific activity of alkaline phosphatase was decreased, isopycnic density gradient centrifugation showing a marked loss particularly of the brush border component of enzyme activity. In contrast, gamma-glutamyl transferase activity was enhanced in brush border fragments of slightly increased modal density, but there were no changes in the activities of the carbohydrases, zinc-resistant alpha-glucosidase, maltase, sucrase, and lactase or of the peptidase, leucyl-2-naphthylamidase. Activities of lysosomal enzymes were increased and there was evidence for enhanced lysosomal fragility and mitochondrial disruption. The activities and density gradient distributions of marker enzymes for basal-lateral membranes, endoplasmic reticulum and peroxisomes were essentially unaltered. These findings show that bacterial colonisation of the proximal small intestine may be associated with specific alterations in microvillus membrane proteins and provide biochemical evidence for intracellular damage to the enterocytes.
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PMID:Biochemical changes in the jejunal mucosa of dogs with a naturally occurring enteropathy associated with bacterial overgrowth. 674 19

The histological, enzymatic, and electrolyte changes induced by a toxigenic strain of E. coli (0128B12) were studied in the rabbit. After 4 hours of contact with the bacteria, one-third of the goblet cells of the intestinal epithelium were totally degranulated, indicating an increase in the destruction of mucus and hence a weakening of mucosal protection through action of bacterial enzymes. The good histological conservation of the ileal mucosa at the end of the study period was confirmed by the stability of the disaccharidase of the glycocalyx and of the luminal surface membrane enzymes, alkaline phosphatase and leucine amino-peptidase. The observed water, sodium and bicarbonate losses were principally due to the action of the bacterial toxins on the ionic pumps of the epithelial cells.
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PMID:Infectious diarrhoeas: weakening of mucosa protection induced in rabbit ileal loops by a pathogenic Escherichia coli. 675 57


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