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)

A short treatment of dog renal brush-border membrane vesicles (BBMV) with sodium cholate, followed by dialysis of the detergent, reorients the polarity of H(+)-ATPase in the membrane and exposes its ATP binding sites to the extravesicular space, as previously shown with pig BBMV. In cholate-pretreated vesicles, the H(+)-ATPase remains fully active, but is inserted under the reversed polarity in sealed vesicles. A large spontaneous N-ethylmaleimide-sensitive ATPase activity is thus observed, as well as a steep intravesicular acidification upon external ATP addition, two findings absent in native vesicles. The ability of nitrate plus ATP to dissociate the hydrolytic subunits ot the proton pump in cholate-pretreated vesicles, but not in native vesicles, demonstrates that most of the ATP binding subunits are accessible to ATP following cholate treatment. The sensitivity of the cytoplasmic domain of the H(+)-ATP activity to trypsin also confirms the reorientation of the enzyme in cholate-pretreated vesicles. The H(+)-ATPase and alkaline phosphatase remain largely associated with the membranes after the treatment with cholate, but gamma-glutamyltranspeptidase, aminopeptidase N, and neutral endopeptidase are largely solubilized. Upon dialysis of cholate, all these enzymes are in part reinserted in the membrane according to their original polarity. The reorientation process is however specific for the H(+)-ATPase. Cholate treatment does not increase the formation of inside-out vesicles. Thus the treatment with cholate really reorients the polarity of the H(+)-ATPase in vesicles and allows for study of the proton pumping capacity of vacuolar H(+)-ATPase of proximal tubules.
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PMID:Effect of cholate on H(+)-ATPase and other proteins of dog renal brush-border membrane. 812 55

To examine the postnatal development of equine small intestine, biopsy specimens of jejunal mucosa from 8 ponies, between 6 and 28 weeks old, were subjected to analytical subcellular fractionation and assay of organelle marker enzymes. Fractionation revealed a reduction in the particulate brush border component of beta-galactosidase (lactase) activity between 6 and 28 weeks, and a corresponding increase in soluble activity, although the reduction in mean specific activity was not significant. There also was a decrease in the proportion of brush border to soluble aminopeptidase N activity, a relative loss of brush border gamma-glutamyltransferase activity, and a considerable decrease in the specific activity of alkaline phosphatase throughout the gradient fractions. In contrast, there were marked increases in activities of alpha-glucosidase (maltase) and sucrase in the older ponies, accompanied by considerable changes in the intracellular distribution of particulate alpha-glucosidase activity, which was predominantly associated with endoplasmic reticulum at 6 weeks, whereas the large increase in activity observed by 28 weeks was clearly associated with the brush border. The modal density of brush borders also increased with age, suggestive of an increase in the glycoprotein-to-lipid ratio of the microvillar membrane. In contrast to these brush border changes, there was relatively little alteration in the activities or density distributions of marker enzymes for endoplasmic reticulum, basolateral membranes, mitochondria, or lysosomes. These findings indicate that maturation of equine intestinal epithelium during the first few months of life results in major changes in the properties and enzyme composition of enterocyte brush borders.
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PMID:Subcellular biochemical changes during the development of the small intestine of pony foals. 853 83

The heterogenous expression of brush border membrane hydrolases by the human enterocyte-like Caco-2 cell line during morphological and functional differentiation in vitro was investigated at the cellular level. Indirect immunofluorescence revealed that the heterogeneous ("mosaic") expression of sucrase-isomaltase, lactase, aminopeptidase N, and alkaline phosphatase was, in fact, transient in nature. The labeling indexes for each hydrolase gradually increased during culture at postconfluence in order to reach a maximum (> or = 90%) after 30 days, concomitant with an upregulation of their respective protein expression levels. In contrast, dipeptidylpeptidase IV labeling remained relatively constant. Backscattered electron imaging analysis in midstage (12 days postconfluence) monolayers demonstrated a lack of correlation between brush border membrane development and expression of each enzyme studied. Moreover, double immunostaining revealed that none of the other four hydrolases correlated directly with sucrase-isomaltase expression. Finally, immunodetection for the proliferation-associated antigen KI-67 revealed a transient mosaic pattern of proliferation which was inversely related to Caco-2 cell differentiation. These data indicate that enterocytic differentiation-related (as well as proliferation-related) gene expression in Caco-2 cells is regulated but uncoordinated at the cellular level, suggesting that an overall control mechanism is lacking.
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PMID:Uncoordinated, transient mosaic patterns of intestinal hydrolase expression in differentiating human enterocytes. 855 68

Natural killer (NK) cytotoxicity was assayed with P3-X63-Ag8-U1 (P3U-1) target cells which had been previously demonstrated to release endogenous alkaline phosphatase (AlP) on the attack of lymphocyte-activated killer cells). P3U-1 cells showed a definite sensitivity to the AlP-release test, but no response in the Cr-release test at all. The AlP-release was not inhibited by anti-perforin antibody, benzoate, phenyl-methyl-sulfonyl-fluoride, soybean trypsin inhibitor, Succinyl-Gly-Pro-Leu-Gly-Pro-amino-methyl-coumarin, or gamma-radiation to effector cells, but was inhibited by o-phenanthroline, anti-CD13 antibody, and anti-LFA-1 alpha antibody. The AlP-release from P3U-1, therefore, did not appear to be brought on by the NK cell-derived perforin, hydroxy-radical, granzymes or cytosolic proteases. The inhibition by o-phenanthroline and the antibody for CD13 (aminopeptidase N) or the adhesion factor in NK cells, however, indicated that the membrane of such cells with adhesion ligand to NK cells was probably susceptible to NK cell surface-associated metaloprotease in an adhesion dependent manner to the extent of some injury without complete perforation through the membrane.
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PMID:[An adhesion dependent injury of target cell membrane by NK cell surface associated metaloprotease]. 856 38

Brush border membrane vesicles from larvae of the tobacco hornworm, Manduca sexta, contain protein bands of 85 and 120 kDa which react directly with streptavidin conjugated to alkaline phosphatase. The binding could be prevented either by including 10 microM biotin in the reaction mixture or by prior incubation of the brush border membrane vesicles with an activated 60- to 65-kDa toxin from Bacillus thuringiensis HD-73. The ability of B. thuringiensis toxins to recognize biotin-containing proteins was confirmed by their binding to pyruvate carboxylase, a biotin-containing enzyme, as well as to biotinylated ovalbumin and biotinylated bovine serum albumin but not to their nonbiotinylated counterparts. Activated HD-73 toxin also inhibited the enzymatic activity of pyruvate carboxylase. The biotin binding site is likely contained in domain III of the toxin. Two highly conserved regions within domain III are similar in sequence to the biotin binding sites of avidin, streptavidin, and a biotin-specific monoclonal antibody. In particular, block 4 of the B. thuringiensis toxin contains the YAS biotin-specific motif. On the basis of its N-terminal amino acid sequence, the 120-kDa biotin-containing protein is totally distinct from the 120-kDa aminopeptidase N reported to be a receptor for Cry1Ac toxin.
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PMID:The Bacillus thuringiensis insecticidal toxin binds biotin-containing proteins. 870 86

The effect of the broad spectrum antibiotics cefaclor, cefadroxil, cephradine, cefatrizine, cephaloglycine and cefroxadine was examined on rat intestinal brush border enzymes, aminopeptidase N (E.C. 3.4.11-2), dipeptidyl peptidase IV (E.C. 3.4.14.5) and alkaline phosphatase (E.C. 1.3.1.3.). All the cephalosporins assayed -except cefaclor- inhibit the aminopeptidase N activity, in an uncompetitive manner. Cefatrizine showed the most important inhibitory effect (52.5%; p < 0.001). Cefaclor and cefadroxil have no effect on the activity of the dipeptidyl peptidase IV, while cephaloglycine and cephradine showed a non competitive type inhibition. In contrast, cefatrizine and cefroxadine showed a competitive inhibition for this enzyme. None of the cephalosporins assayed had any effect on alkaline phosphatase activity.
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PMID:Influence of cephalosporins on intestinal enzymatic activity. 877 83

A combination of mild proteolytic digestion and selective growth stimulation has been used to isolate and propagate adult rat intestinal epithelial cells with a finite life span. Growth of these cells on a variety of matrices and on mesenchymal cells has resulted in the expression of brush border enzymes including sucrase-isomaltase, aminopeptidase N, and alkaline phosphatase. Examination of the cells at the electron microscopic level has revealed that although these cells express key brush border enzymes, they do not have a fully formed brush border. These findings suggest that the expression of brush border enzymes and structural proteins represent distinct stages of enterocyte differentiation that are under separate transcriptional and temporal control.
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PMID:Growth and propagation of normal rat intestinal epithelial cells. 890 24

Three GPI-anchored proteins, aminopeptidase N, alkaline phosphatase and alkaline phosphodiesterase I were released from the midgut brush border membrane of Bombyx mori by phosphatidylinositol-specific phopholipase C and the aminopeptidase N was purified to a homogeneous state. N-terminus and 6 internal sequences, one of which possessed part of zinc-binding motif, showed homology with those from other species. The zinc content in purified aminopeptidase N was estimated as approximately 0.72 mol/mol of the protein and 1,10-phenanthroline completely inhibited the enzyme activity, suggesting zinc requirement for the activity. The aminopeptidase N activity was inhibited not only by probestin and actinonin, but also strongly depressed by amastatin, while leuhistin and bestatin were less inhibitory. These suggest that the active site of aminopeptidase N might be structurally different from those of mammals. Calcium and magnesium ions stimulated the aminopeptidase N activity, but copper ion was rather inhibitory. Zinc ion showed bi-modal effect on the activity, i.e., stimulatory at low concentration, but inhibitory at higher than 100 microM. This inhibition was completely restored by EDTA. These results suggest that the aminopeptidase N possesses two zinc ion-binding sites with high and low affinity as essential and inhibitory one, as well as some regulatory metal-binding sites.
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PMID:Characterization of aminopeptidase N from the brush border membrane of the larvae midgut of silkworm, Bombyx mori as a zinc enzyme. 960 61

The objective of the present study was to examine whether cinnamic acid exerts antitumor activity against colon cancer cells in vitro. For this purpose we investigated the effect of cinnamic acid on cell proliferation and on the differentiation markers alkaline phosphatase, sucrase and aminopeptidase N in human colon adenocarcinoma cells (Caco-2). Cinnamic acid (2.5-8.0 mM) prolonged the doubling time and inhibited the DNA synthesis of growing cells. The antiproliferative effect occurred rapidly after 2 h of treatment with 8.0 mM cinnamic acid and reached nearly maximal values after 8 h of treatment. Sucrase and aminopeptidase N activities were stimulated under cinnamic acid treatment (4.0-8.0 mM), while alkaline phosphatase activity was inhibited in postconfluent cells (8.0 mM). Similar effects on enzyme activities were seen in non-proliferating cells. Cinnamic acid did not alter the adhesion to collagen matrix or cell viability. Intracellular cAMP levels were decreased significantly after 1 h of treatment with 8.0 mM cinnamic acid, suggesting that cinnamic acid induces its effects on enzyme activities partly by modulating the cAMP signaling pathway.
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PMID:Cinnamic acid inhibits proliferation and modulates brush border membrane enzyme activities in Caco-2 cells. 968 74

In this study we show that the aminopeptidase N of cerebral pericytes (pAPN) associated with the blood-brain barrier (BBB) is downregulated in pericytic cell cultures. This observation is in accordance with previous data describing comparable in vitro effects for BBB-specific enzymes of endothelial or pericytic origin, such as gamma-glutamyl transpeptidase or alkaline phosphatase. By polymerase chain reaction and in situ hybridization we were able to determine that the down-regulation of pAPN occurs at the posttranscriptional level. The mRNA of pAPN was found to be constitutively expressed even when the protein is no longer detectable. Culturing the pericytes in an endothelial cell-conditioned medium allowed pAPN to be reexpressed. However, the reexpression effect depended largely on the culturing conditions of the pericytes. Although purified pericytes deprived of endothelial cells did not reveal a reexpression effect, pericytes that were kept in contact with endothelial cells were able to acquire a pAPN-positive phenotype, indicating that endothelial cells constitute an essential requirement for the in vitro reexpression of pAPN. Astrocytes, however, were insufficient in exerting any reexpression effect.
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PMID:Regulation of a blood-brain barrier-specific enzyme expressed by cerebral pericytes (pericytic aminopeptidase N/pAPN) under cell culture conditions. 980 17


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