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)

Electron microscopic observations showed that the fungal metabolite brefeldin A caused disassembly of the Golgi complex in human choriocarcinoma cells and accumulation of alkaline phosphatase (ALP) in the endoplasmic reticulum (ER) and nuclear envelope, where ALP was not apparently detectable in control cells. Pulse/chase experiments with [35S]methionine demonstrated that in the control cells, ALP synthesized as a 63-kDa precursor form was rapidly converted to a 66-kDa form, by processing of its N-linked oligosaccharides from the high-mannose type to the complex type, which was expressed on the cell surface after 30 min of chase. In contrast, in the brefeldin-A-treated cells the precursor was gradually converted to a 65-kDa form, slightly smaller than the control mature form, which was not expressed on the cell surface even after a prolonged time of chase. Kinetics of the ALP processing in the brefeldin-A-treated cells demonstrated that the precursor was initially converted to an intermediate form, partially sensitive to endo-beta-N-acetylglucosaminidase H (endo H), then to an endo-H-resistant 65-kDa form. In addition, this form was found to be sensitive to neuraminidase digestion, though its sialylation was not so complete as that of the control mature form. Taken together, these results suggest that under disassembly of the Golgi complex caused by brefeldin A, oligosaccharide-processing enzymes including sialyltransferase, an enzyme in the trans Golgi cisterna(e) and/or the trans Golgi network, might be redistributed into the ER and involved in processing of the oligosaccharides of ALP accumulating there.
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PMID:Intracellular accumulation and oligosaccharide processing of alkaline phosphatase under disassembly of the Golgi complex caused by brefeldin A. 226 2

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

Investigation of mild, inherited increased serum alkaline phosphatase activity partially combined with Gilbert's syndrome in one family showed, apart from a normal liver fraction, an intestinal isoenzyme pattern and an extra band in the agar electrophoresis. Analysis by agarose electrophoresis before and after incubation of neuraminidase showed that the extra fraction was an intestinal variant isoenzyme. The precise genetic background of the two disorders in this family could not be determined from the available data. Abnormal activities of (regular) intestinal alkaline phosphatase isoenzyme caused the increase in serum alkaline phosphatase in the absence of disease.
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PMID:Familial increased serum intestinal alkaline phosphatase: a new variant associated with Gilbert's syndrome. 231 88

Intestinal and serum leucine aminopeptidase (LAP) and alkaline phosphatase (AKP) were characterized by electrophoresis for eight inbred strains of laboratory mice. Intestinal LAP and AKP of adult mice were expressed concordantly within strains, as banded or diffuse, and concordantly for rate of migration within strains that had diffuse isozymes. All strains, except DD/S, had a single band of serum LAP and a single, diffuse zone of serum AKP. DD/S had a double band of serum LAP as well as isozymes of intestinal LAP and AKP unlike those of other strains. All strains displayed similar, neuraminidase-sensitive isozymes of intestinal LAP and of AKP prior to weaning, but after weaning there was marked sensitivity to neuraminidase only in DD/S. In interstrain crosses, banded/diffuse, migration rate, and neuraminidase sensitivity were inherited as independent autosomal traits, with indications of variable penetrance and genetic interaction.
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PMID:Intestinal leucine aminopeptidase and alkaline phosphatase: genetic regulation and development in mice. 239 81

The gross anatomy, histology and histochemistry of the ferret prostate is described. The structure and course of the prostatic urethra and the ductus deferentes are also described. The prostate is the only accessory reproductive gland present in the ferret. The prostate consists of tubuloalveolar glands surrounded by fibromuscular connective tissue. Histochemical studies showed that the glandular parenchyma contained large amounts of sialidase-labile sialomucin as well as acid phosphatase and small quantities of alkaline phosphatase and proteins. The findings in this study are discussed in relation to similar studies in other animals and man.
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PMID:Morphology and histochemistry of the ferret prostate. 242 64

Hydrophilic gel permeation chromatography of 14-36 wk human amniotic fluid on Fractogel columns divides the total alkaline phosphatase (AP) activity in a higher and a lower mol wt zones. Differential inhibition testing, isoelectric focusing, cellulose acetate, agarose and polyacrylamide gel electrophoreses before and after neuraminidase treatment show the higher mol wt zone to be homogeneous and to be made of the higher mol wt foetal intestinal isoenzyme form whereas the lower mol wt zone represents an unresolved mixture of hepatic, placental and lower mol wt foetal intestinal isoenzymes. In the early stages of pregnancy, the activity associated with the higher mol wt zone outweighs by far that of the lower mol wt zone; however from the 24 th week one notes a steady increase in the relative magnitude of this second zone until at the end of the gestation period both zones assume near equal importance albeit within a lower total AP activity. Satisfactory quantitation of the higher mol wt foetal intestinal isoenzyme form in one ml amniotic fluid can be attained after a 3-h chromatography run using p-nitrophenylphosphate as substrate.
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PMID:Alkaline phosphatase activities in human amniotic fluid, chromatographic separation of the foetal intestinal component. 246 54

Intestinal-like alkaline phosphatase was found to be expressed in the intestinal 407 cell line. This enzyme was identified by use of monoclonal antibodies specific for human placental (H7 and HPMS-1) and intestinal alkaline phosphatase (2HIMS-1 and 2HIMS-3) separately. Purification of this isozyme by use of two different monoclonal antibody immunoaffinity chromatographies demonstrates a single protein band on SDS-polyacrylamide gel electrophoresis indicating that this enzyme is not formed as a heterodimer. The apparent monomer subunit molecular weight and the dimer molecular weight of this isozyme were determined to 70000 and 160000, respectively. The enzyme is a homodimer according to molecular weight determinations. Furthermore, this isozyme is neuraminidase sensitive and comparatively heat stable, properties also characteristic for the placental enzyme. Our data suggest that the intestinal-like alkaline phosphatase in the intestinal 407 cell line displays properties intermediate of the intestinal and placental isozymes which may reflect the existence and reexpression of a new primitive isozyme.
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PMID:Evidence for the expression of a primitive intestinal-like alkaline phosphatase in the intestinal 407 cell line. 246 Jan 3

1. The Virginia opossum (Didelphis virginiana) possessed an arylsulfatase which had a relative molecular weight of 130 +/- 12 kDa, displayed anomalous kinetics, hydrolysed AA2S, and exhibited other properties of arylsulfatase A. No arylsulfatase B was found. 2. The arylsulfatase present in the gray short-tailed opossum (Monodelphis domestica) had a relative molecular weight of 56 +/- 4 kDa, exhibited linear kinetics, was inhibited by chloride, and possessed other characteristics of arylsulfatase B. No arylsulfatase A was found. 3. Arylsulfatases from both species occurred as multiple isozymes which were unaffected by neuraminidase or alkaline phosphatase treatment.
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PMID:Comparative biochemistry of hepatic arylsulfatases from north and south American opossums. 257 50

Monoclonal antibodies, 17B1 and 17Q2, which are specific for large molecular weight mucous glycoproteins of airway epithelium, have been used to develop an ELISA method to quantitate the tracheal mucins of humans and rhesus monkeys. The assay is a double-sandwich system that does not depend on either the binding of mucous antigens to the microtiter plate or the use of a second antibody. The assay protocol includes (1) coating the microtiter well with purified IgG of 17B1 or 17Q2, (2) incubating the wells with mucous samples, (3) binding of alkaline phosphatase-conjugated IgG to the wells, and (4) developing the color with phosphate substrate. This ELISA method is very sensitive for human and rhesus monkey tracheal mucins. Quantitation is not affected by the presence of various proteoglycans (keratan sulfate, hyaluronate, heparin, heparan sulfate, and chondroitin sulfate). However, the quantitation is affected by the treatment of antigen with periodic acid and endo-beta-galactosidase. Other enzymes (e.g., neuraminidase, hyaluronidase, chondroitinase, heparitinase, heparinase, fucosidase, keratanase) have no effect on the antigenicity of substrate. The quantitation is linear, with a concentration from 0.2 to 4 ng protein/sample. The ELISA method developed in this study should be useful for quantitating the mucin content of various biologic fluids, such as sputum, bronchoalveolar lavage, and media from cultures following various pharmacologic and physiologic manipulations.
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PMID:An ELISA method for the quantitation of tracheal mucins from human and nonhuman primates. 262 58

Specific monoclonal antibodies raised against human intestinal and human tissue-unspecific alkaline phosphatase (AP) were developed and were used to study the expression of these two isoenzymes in human renal tissue and their release into urine. Approximately 25% of the total AP content of renal tissue at the transition between cortex and medulla was of the intestinal type; the remainder was of the tissue-unspecific type (liver, bone, kidney AP). Immunoperoxidase staining using specific monoclonal antibodies against liver and intestinal AP revealed that the tissue-unspecific AP isoenzyme is present through-out the different segments of the proximal tubule, whereas intestinal-type AP is found exclusively in tubuloepithelial cells of the S3-segment of the proximal tubule. The intestinal-type enzyme obtained from the kidney had a similar heat stability and Km value, and similar immunologic and inhibitory (L-p-bromotetramisole; L-phenylalanine) characteristics compared to adult intestinal and fetal intestinal AP. Its electrophoretic mobility in agarose gel was intermediate between that of adult intestinal and fetal intestinal AP; after neuraminidase treatment it became indistinguishable from the adult intestinal isoenzyme. The intestinal-type AP found in the urine was not sensitive to neuraminidase and had a molecular weight significantly lower than the urinary tissue-unspecific AP isoenzyme. In conclusion, intestinal AP in the kidney is a specific marker for the brush border of the S3 segment of the proximal tubule, and this finding opens new perspectives in the cell biology of this particular part of the nephron.
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PMID:Segment-specific localization of intestinal-type alkaline phosphatase in human kidney. 268 32


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