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)

Twenty-one cases (25 biopsies including 9 frozen biopsies) of Kaposi's sarcoma associated with the acquired immune deficiency syndrome (AIDS) were examined immunohistochemically, lectin-histochemically, and enzyme histochemically to ascertain the histogenesis of the lesion. The Kaposi's sarcomas were histologically subtyped according to a modified Schmid's classification (granulation tissue-like-, angiosarcoma-like- and spindle cell type). In almost all lesions, many atypical vasoforming cells and at least some spindle cells without definite evidence of vasoformation by conventional microscopy were positive for factor VIII-related antigen, BMA 120 (a new monoclonal antibody to an endothelial cell-specific antigen), Ulex europaeus I (UEA-I), alkaline phosphatase and ATPase. Linear reaction products for BMA 120 and UEA-I, suggesting the luminal surface of immature vascular channels, were sometimes recognized in the positive spindle cells. Electron micrographs confirmed endothelial characteristics, such as irregular and fragmented but distinct basal lamina and numerous pinocytotic vesicles, in both the UEA-I- and ATPase-positive spindle cells. Among spindle cells negative for the endothelial markers, there were many macrophages as a stromal reaction to tumor tissue, identified by monoclonal antibodies to macrophages (KiM 6, 7, 8 and EBM 11), acid phosphatase and alpha-naphthyl acetate esterase. The results of the immuno- and enzyme histochemical investigations did not correlate with the different histologic types of Kaposi's sarcoma. However, our results strongly suggest that tumor cells of Kaposi's sarcoma are derived from vascular endothelial cells rather than lymphatic endothelium.
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PMID:Histogenesis of Kaposi's sarcoma associated with AIDS: a histologic, immunohistochemical and enzyme histochemical study. 368 78

The major source of rat serum alkaline phosphatase (ALP) is well known to be from the intestinal enzyme, but it is still unclear whether it is from the duodenal or the ileal enzyme. The organic origin was investigated by means of two-dimensional electrophoresis. Major isoelectric points and molecular masses for activities of duodenal enzyme treated with both phosphatidylinositol-specific phospholipase C and neuraminidase were identified apparently with those of the major serum enzyme. In organ culture, the normal duodenal enzyme was released in the highest amounts to the culture medium. These results indicate that the major source of serum ALP in adult rats is basically from the duodenal enzyme. On the other hand, lectin affinity chromatography for ALPs showed that the ALP in the medium from culture duodenum and liver had the same complex-type sugar chain as with the ALP in the duodenal tissue. Although the duodenal ALP induced by glucosamine in vitro had the hybrid-type chain, sugar chains of the induced ALP in the culture medium were of the complex type, indicating that medial ALPs possessing the same sugar chain as the native duodenal enzyme, complex type, are mainly released from their tissues in normal conditions.
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PMID:Blood appearance of rat alkaline phosphatase originating from the duodenum in vitro. 369 1

Separation of alkaline phosphatase isoenzymes using affinity electrophoresis in agarose gel containing lectin is described. The bone and biliary isoenzymes precipitate during electrophoresis and are clearly separated from the liver isoenzyme. The liver, intestinal and placental alkaline phosphatases are essentially not affected by the lectin. The migration distances of the precipitating bone and biliary fractions vary with their alkaline phosphatase activity. The bone isoenzyme is more heterogeneous than the biliary isoenzyme with respect to interaction with lectin forming both insoluble and soluble complexes. Affinity electrophoresis in agarose gel containing lectin can be used for quantitation by densitometry of liver and bone isoenzymes in sera containing only these two fractions but must be combined with conventional electrophoresis, preferably in agar gel, if biliary, intestinal, or placental isoenzymes are also present.
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PMID:Affinity electrophoresis of human serum alkaline phosphatase isoenzymes in agarose gel containing lectin. 370 57

The present study was undertaken to provide further evidence for mechanisms proposed for the toxicity of ingested winged bean lectin in animals: to determine its effect on activities of some hydrolases localized in the brush border membrane of the small intestine. An adaptive increase in sucrase activity of rats given a high-sucrose diet (HSD) was restrained by the addition to HSD of a lectin fraction (WBLF) isolated from raw winged beans but not by that of heated WBLF or soybean trypsin inhibitor. Restraining effects of WBLF added to HSD on time-course changes in activities of sucrase, alkaline phosphatase and leucine aminopeptidase of rats after giving HSD were similar to those of concanavalin A, which had been observed in the previous study. These results substantiate that the mechanism of the toxicity of ingested winged bean lectin involves its binding to the luminal surface of the small intestine and in turn disturbing the functional formation of the brush border membrane.
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PMID:Effect of ingested winged bean lectin on gastrointestinal function in the rat. 371 4

With this electrophoretic method the liver, biliary, and bone isoenzymes of alkaline phosphatase are clearly separated on agarose gels. Wheat-germ lectin, incorporated in the gel matrix, binds the bone isoenzyme selectively, forming a precipitate near the origin. Neither liver nor biliary isoenzyme is affected. Activity staining with an indigogenic dye substrate reveals the liver isoenzyme migrating nearest the anode, followed by the biliary and bone isoenzymes. Results are generally similar to those of electrophoresis on cellulose acetate. However, the lectin-agarose gels better resolve the liver and bone isoenzymes, and heat treatment of samples is not required before electrophoresis.
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PMID:Alkaline phosphatase isoenzymes resolved by electrophoresis on lectin-containing agarose gel. 375 86

We report an easy, rapid method for quantifying bone isoenzyme of alkaline phosphatase (EC 3.1.3.1., ALP) in serum. The original method described by Rosalki and Ying Foo (Clin Chem 1984;30:1182-6) was somewhat simplified. In contrast to their results, we found that bone ALP is precipitated quantitatively by wheat-germ lectin. To check the clinical plausibility of the method, we used samples from several comparison groups (blood donors, children, pregnant women, patients with neoplasms but without skeletal involvement) and a large number of patients suffering from bone diseases and diseases of the liver and biliary tree. Measured activities of bone ALP nearly always correlated with the clinical diagnosis. Only patients with hepatitis often had pathological bone activities not in accord with the other findings. Possible reasons for this observation are discussed.
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PMID:Quantification of bone alkaline phosphatase in serum by precipitation with wheat-germ lectin: a simplified method and its clinical plausibility. 375 20

We investigated the composition of the precipitate that forms when wheat-germ lectin derived from Triticum vulgaris is added to serum. A number of serum proteins are precipitated, representing about 2.5% of the total serum protein. This study demonstrates that the interaction of this lectin with the bone isoenzyme of alkaline phosphatase is not specific.
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PMID:Precipitation of serum proteins by the lectin from wheat-germ. 380 72

The apical membranes of rabbit gallbladder epithelial cells were isolated by treating the homogenate with Ca2+ or Mg2+ and centrifuging the suspension in Percoll gradient. In this way brush-border membranes were obtained with enrichment factors ranging between 10 and 20 and yields of 15-30%. A second method is described with which membranes were isolated, without any preliminary treatment, first by differential centrifugation, then with Percoll gradient; the final membrane enrichment was over 15, however the yield was very low (3%). Many possible enzymatic markers of the apical plasma membrane were investigated: L-gamma-glutamyltransferase, alkaline phosphatase, leucine aminopeptidase, sucrase. The first appears to be that of choice. Apical membrane fraction could be also evidenced by autofluorescence or by labeling with Lotus tetragonolobus lectin. Preliminary experiments showed that apical plasma membranes isolated in this way form vesicles.
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PMID:Isolation of apical plasma membrane in rabbit gallbladder epithelium by Percoll density gradient centrifugation. 381 91

Of 98 patients' specimens examined for alkaline phosphatase (EC 3.1.3.1) isoenzymes by electrophoresis on cellulose acetate membrane after incubation with neuraminidase, 50 showed only a single liver or bone isoenzyme staining band; in 15 of these, the tissue origin of the fraction could not be accurately identified from its electrophoretic location. In the remaining 48 specimens, both liver and bone fractions were identifiable, but in only 25 of these was the electrophoretic resolution sufficient to yield separate peaks on densitometry. In contrast, both liver and bone alkaline phosphatase isoenzymes were identified in 95 of the 98 specimens by affinity electrophoresis involving wheat-germ lectin, the detection of both fractions being in agreement with the results of sequential heat inactivation. The tissue origin of the enzyme bands was readily ascertainable from their consistent electrophoretic location in this medium, and in 89 of the specimens the isoenzyme fractions could be resolved into separate peaks on densitometry. We conclude that resolution of liver and bone alkaline phosphatase by incubation with neuraminidase followed by cellulose acetate electrophoresis is greatly inferior to that obtained by wheat-germ lectin affinity electrophoresis.
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PMID:Incubation with neuraminidase and affinity electrophoresis with wheat-germ lectin compared for separating and quantifying alkaline phosphatase isoenzymes in plasma. 383 70

The existence of HLA-DR/Ia-like antigen (Ia)-bearing cells of the mononuclear phagocyte system, macrophages (Mac), and/or interdigitating cells (IDC), in the normal kidney is controversial. If present, such cells may be important in renal transplant rejection. We performed enzyme histochemistry using alpha-naphthyl acetate/butyrate esterases (alpha NAE, alpha NBE), 5'-nucleotidase (5'N), acid phosphatase (AcP), alkaline phosphatase (AlkP), and ATPase (ATP) as well as immunoperoxidase staining for Ia and lectin binding (Ulex europaeus I; UEA) on plastic-embedded tissue sections of normal kidneys and rejected renal allografts. Plastic embedding provides clear visualization of histologic detail and allows specific identification of immunoperoxidase-stained cells. Mac and IDC (shown to be Ia+, alpha NAE+, AcP+, ATP+ in other sites) could not be demonstrated in normal renal interstitium. IDC and Mac were not generally identified in normal mesangium, although they could not be altogether distinguished from Ia+ endothelial cells. Focal mesangial staining for alpha NAE but not alpha NBE was present. Rejected kidneys showed increased numbers of alpha NAE+ cells in glomeruli. These cells were frequently Ia negative and often appeared to be blood monocytes present in capillary lumens. Peritubular capillaries and glomerular endothelium stained strongly for UEA, 5'N, and Ia. Our results suggest that previous reports of the presence of IDC in renal tissue on the basis of staining for Ia on frozen tissue may be due to staining of compressed or obliquely sectioned vascular structures that were not adequately visualized.
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PMID:Monocyte/macrophage derived cells in normal and transplanted human kidneys. 389 Nov 75


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