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)

FL-amnion cells have mainly two alkaline phosphatase (AP) isozymes, of which the faster migrating one (FL-APF) on 5% polyacrylamide gel electrophoresis has proved to be identical to the Kasahara isozyme, a tumor-associated AP of intestinal type. But the other slower migrating one (FL-APs) remains to be characterized. Immunological and enzymic examination of purified FL-APs revealed that it is a hybrid form of AP consisting of one subunit with a molecular weight of 66,200 coming from the same subunit as that of FL-APF and another one with a molecular weight of 58,000 from placental AP subunit with modified glycosylation.
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PMID:A hybrid form of alkaline phosphatase produced in FL-amnion cells. 165 55

Two types of alkaline phosphatase (AP) isozymes in rabbit kidney, a major intestinal-like type and a minor tissue-unspecific type, have been identified. The former enzyme was purified from rabbit kidney by immunoaffinity chromatography using monoclonal anti-human intestinal AP antibody. The purified enzyme yielded a single protein band on sodium dodecyl sulfate-polyacrylamide gel electrophoresis, and the apparent molecular size of its monomer subunit was found to be 72,000. Three amino acid residues within the first 16 N-terminal amino acid residues were different in purified AP and human intestinal AP. Although the rabbit enzyme possessed some peptide bands identical to those of human adult intestinal AP after Staphylococcus aureus V8 protease digestion, the enzyme did not react with monoclonal antibody against human adult intestinal AP alone, whereas it did react with monoclonal antibody against both human adult and fetal intestinal APs. The affinity of the enzyme for concanavalin A was identical to that of the fetal intestinal AP, but different from that of the adult enzyme. These results indicate that the antigenicity and certain properties of purified rabbit AP are more like those of human fetal intestinal AP or Kasahara isozyme, so-called intestinal-like AP, than like human adult intestinal AP.
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PMID:Purification and partial characterization of intestinal-like alkaline phosphatase in rabbit kidney. 198 15

A variety of perturbations of calcium metabolism are reported to occur in the spontaneously hypertensive rat (SHR) compared to its genetic control the Wistar-Kyoto rat (WKY), including significant dysfunction of calcium handling by the proximal renal tubule of the SHR, resulting in impaired active calcium transport in the gut and an apparent renal calcium leak. We explored the intestinal and renal epithelia of 12- to 14-week-old SHR and WKY using electron microscopy. Biochemical comparisons of these transport epithelia included measurements of three vitamin D dependent cellular proteins and one structural protein: alkaline phosphatase, intestinal CaBP9K, renal CaBP28K, and villin expression. Electron microscopy demonstrated a patchy loss in microvilli in the SHR, accounting for approximately 10 to 15% of the total microvillar surface. In the kidney, morphological abnormalities were observed only in the proximal renal tubule. Again, there was patchy loss of microvilli from the brush border membrane. In SHR duodenal alkaline phosphatase activity was significantly reduced compared to the WKY (0.145 +/- 0.002 v 0.186 +/- 0.002 integrated extinction/min/micron 3 X 10(3) brush border (P less than .001). Duodenal CaBP9K and renal CaBP28K were significantly reduced in SHR compared to WKY. There were no differences in villin expression. These data are consistent with the previously characterized disturbances of active calcium transport in the intestine and inappropriate renal calcium leak in the SHR. While a possible link between these disturbances and hypertension remains to be determined, this study provides supportive evidence for a primary disturbance in cell calcium handling and transporting epithelia in this form of genetic hypertension.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Epithelial abnormalities in intestine and kidney of the spontaneously hypertensive rat. 222 67

Asparagine-linked oligosaccharides were quantitatively released by hydrazinolysis from an alkaline phosphatase, Kasahara isozyme, which was purified from FL amnion cells. Almost all of the oligosaccharides (98%) were acidic components, all of which can be converted to neutral oligosaccharides upon sialidase digestion. Structural analysis of the oligosaccharides by sequential exoglycosidase digestion in combination with methylation analysis revealed that the alkaline phosphatase of FL cells contains sialylated mono-, bi-, tri-, and tetraantennary complex type sugar chains with the Gal beta 1----4GlcNAc beta 1---- outer chains. Some of the tetraantennary sugar chains contain a single Gal beta 1----4GlcNAc beta 1----3Gal beta 1----4GlcNAc beta 1---- outer chain on their Man alpha 1----6 arm. Both fucosylated and nonfucosylated trimannosyl cores were found in the sugar chains. However, it is of interest that the core portion of monoantennary oligosaccharide was not fucosylated and that of the tetraantennary oligosaccharide with a tetrasaccharide outer chain was completely fucosylated.
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PMID:Structures of the asparagine-linked oligosaccharides of an alkaline phosphatase, kasahara isozyme, purified from FL amnion cells. 229 56

Human alkaline phosphatase isozymes--the tissue-unspecific, the intestinal, and the placental alkaline phosphatases--were determined in sera by use of isozyme-specific monoclonal antibodies. The clinical utility of serum determinations of alkaline phosphatase isozymes was evaluated in patients with diseases of the gastrointestinal tract and the liver. No elevations of the different serum isozymes were observed in the intestinal diseases investigated (active Crohn's disease and ulcerative colitis). For non-malignant diseases of the liver the alkaline phosphatase isozymes presented characteristic patterns. Patients with cirrhosis due to hepatocellular diseases had markedly elevated levels of intestinal alkaline phosphatase and moderate serum activities of tissue-unspecific and placental alkaline phosphatases. In patients with liver disease with cholestatic features tissue-unspecific and placental isozyme levels were high, but the intestinal isozyme remained normal, whereas primary biliary cirrhosis was associated with high levels of the tissue-unspecific enzyme and moderate elevations of intestinal and placental alkaline phosphatases. It can be concluded that, in addition to tissue-unspecific alkaline phosphatase, intestinal and placental isozymes contribute to the total alkaline phosphatase activity for patients with liver disease. The results suggest that specific methods for the identification of alkaline phosphatase isozymes could be of value.
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PMID:Alkaline phosphatase isozymes in non-malignant intestinal and hepatic diseases. 322 93

The microheterogeneity of Kasahara isozyme was investigated by affinity electrophoresis with Con A as the affinity ligand in combination with polyacrylamide gradient gel electrophoresis. On two-dimensional Con A-containing agarose gel electrophoresis, the Kasahara isozyme was separated into three molecular species. Kasahara isozyme electrophoresed as two distinct bands with enzyme activity on polyacrylamide gradient gel, but liver, intestinal or placental alkaline phosphatase showed only one distinct spot or band on both electrophoreses. One of the three molecular species of Kasahara isozyme separated by Con A-containing agarose gel electrophoresis was extracted from the gel and applied to the polyacrylamide gradient gel electrophoresis again, resulting in the same electrophoretic pattern as that of the original Kasahara isozyme. These findings indicated that the Kasahara isozyme consists of at least four molecular species. The same analysis was conducted with alkaline phosphatase of the HuH-6 cl-5 cell line, which has been reported to release an alkaline phosphatase closely resembling the Kasahara isozyme, and the results were compared with those obtained with the Kasahara isozyme.
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PMID:Microheterogeneity of Kasahara isozyme. 375 65

A cloning method utilizing the enzyme histochemical procedure was applied to isolate variant HeLa subclones which produce different alkaline phosphatase isozymes. Phosphate was used to distinguish between Kasahara isozyme and Regan isozyme. The use of filter paper made it possible to determine the localization of the Kasahara isozyme-positive colonies. By this method, two variant clones, HeLa S3-10 KP and HeLa S3-10 KN, were isolated. Kasahara isozyme was induced in the former by increased cell density, but not in the latter.
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PMID:Application of the enzyme histochemical method for the isolation of HeLa variant inducibly producing the Kasahara isozyme of alkaline phosphatase. 722 19

HeLa S3 cells have been found to possess heat-stable alkaline phosphatase. However, the present electrophoretic study indicated that this cell line also contained a heat-labile isozyme as a minor component with the major heat-stable (Regan) isozyme. Histochemical demonstration of these two isozymes was also made through heat treatment and inhibition tests. By the single cell cloning of HeLa S3 cells, two subclones, HeLa S3-5 with heat-labile Kasahara isozyme and HeLa S3-10 with Regan isozyme, were established. All 18 subclones from this HeLa S3-5 possessed the same type of heat-labile alkaline phosphatase. These two isozymes were expressed in two cell lines, respectively, during long term culture. The present study suggests that certain cell populations of HeLa S3 have changed their phenotype to Kasahara isozyme due to alteration of a regulatory gene during long term cell culture.
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PMID:Alkaline phosphatase from two HeLa S3 subclones: one producing Regan and the other, Kasahara isozyme. 727 5

The phoD gene encoding the membrane-bound alkaline phosphatase (ALPI) from Zymomonas mobilis CP4 was cloned and sequenced. Both the translated sequence and the properties of the recombinant enzyme were unusual. Z. mobilis ALPI was monomeric (M(r) 62,926) and hydrolysed nucleotides more effectively than sugar phosphates. The translated sequence contained a single hydrophobic segment near the N-terminus which may serve as a membrane-anchor in Z. mobilis, although the recombinant enzyme was recovered in the cytoplasmic fraction of Escherichia coli. The predicted amino acid sequence for ALPI did not align well with other ALPs or other known genes. However, some similarity to E. coli ALP was noted in the metal-binding and phosphate-binding regions. Two other regions were identified with similarity to the active sites of pyruvate kinase and mammalian 5'-nucleotide phosphodiesterase (also membrane-bound), respectively. It is likely that Z. mobilis phoD represents a new class of alkaline phosphatase genes which has not been described previously.
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PMID:Cloning, sequencing and characterization of the alkaline phosphatase gene (phoD) from Zymomonas mobilis. 787 72

Multilocus linkage analysis has suggested that the Waardenburg syndrome type 1 (WS1) locus is flanked by placental alkaline phosphatase (ALPP) and fibronectin 1 (FN1). We used fluorescence in situ hybridization (FISH) to map ALPI (intestinal alkaline phosphatase) to 2q36.3-q37.1 and FN1 to 2q34. FISH also showed that a WS1 patient with a de novo interstitial deletion of 2q35-q36.1 retained both API and FN1 on the deleted chromosome. The human PAX3 gene has been shown previously to be mutated in at least two WS1 patients. We mapped a PCR product from the PAX3 gene to 2q35 and found it was absent in the deleted chromosome. Thus, our FISH mapping results confirm the conclusions from previous linkage analysis and support the conclusion that mutation of the PAX3 gene can cause Waardenburg syndrome.
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PMID:In situ hybridization applied to Waardenburg syndrome. 844 34


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