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 effects of bile-duct ligation on hepatic and intestinal (jejunum) alkaline phosphatase activities were studied using rats and guinea pigs. In ligated rats, the enzyme activity was increased 4.1-fold in the liver after 24 h and 2.8-fold in the intestine after 12 h. In guinea pigs, the hepatic and intestinal enzyme activities were increased 2.3-fold and 1.5-fold after 100 and 24 h, respectively. The intestinal activity was induced sooner after ligation than hepatic activity. The induction of alkaline phosphatase was inhibited by prior treatment of animals with amanitin, an inhibitor of RNA polymerase activity. This result indicates that the induction is associated with de novo enzyme synthesis. The content of cyclic AMP in liver and intestine increased immediately after ligation. The increase in alkaline phosphatase activities was also inhibited by pretreatment with chlorpromazine, an inhibitor of adenylate cyclase activity. Hence, cellular cyclic AMP may be implicated in playing a role in the induction of alkaline phosphatase by bile-duct ligation.
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PMID:A possible mechanism for the changes in hepatic and intestinal alkaline phosphatase activities in bile-duct-ligated rats or guinea pigs. 661 80

A method for an analytical isolation of plasma membranes from columnar cells (colonocytes) of the proximal colon of the guinea pig is described. Isolation of the colonocytes was performed by a mild EDTA-chelation method. After homogenization, two subsequent sucrose gradient centrifugations (isokinetic and isopycnic) yielded a plasma-membrane fraction which was enriched 12-fold in (Na+ + K+)-ATPase activity and 8-fold in adenylate cyclase activity. It is suggested that the purified membrane fraction consists mainly of basolateral membranes of the colonocytes. Due to the lack of suitable marker enzymes, no evidence for enrichment of the brush-border membranes was obtained. Histochemical studies demonstrated that alkaline phosphatase is absent from the luminal membrane of the surface epithelial cells of the proximal colon of the guinea pig.
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PMID:Isolation of basolateral membranes from columnar cells of the proximal colon of the guinea pig. 662 41

Rat brain cortex, caudate nucleus and cerebellum contain one or more factors that confer Vasoactive Intestinal Polypeptide (VIP)-, dopamine (DA)- and norepinephrine (NE)-sensitivity to adenylate cyclase in the absence of added GTP. These factors also stimulate the basal activity of the enzyme. The activity is found in a 100 000 X g supernatant; has an apparent molecular weight greater than 450 000 daltons; is inactivated by pronase, alkaline phosphatase and ammonium sulphate, and partially degraded by trypsin; and is stable to heat and acidic treatment. The effect of the factors is additive with that of guanosine-5'-triphosphate (GTP), and is not abolished by guanosine 5'-0-(2-thiodiphosphate) (GDP-beta-S). These results suggest that stimulation of adenylate cyclase by VIP, and most likely by DA and NE, can be modulated by soluble proteins.
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PMID:Properties of cytosolic proteins that confer vasoactive intestinal polypeptide-sensitivity to rat brain adenylate cyclase. 664 95

A method has been developed for routine high yield separation of canalicular (cLPM) from basolateral (blLPM) liver plasma membrane vesicles of rat liver. Using a combination of rate zonal floatation (TZ-28 zonal rotor, Sorvall) and high speed centrifugation through discontinuous sucrose gradients, 9-16 mg of cLPM and 15-28 mg of blLPM protein can be isolated in 1 d. cLPM are free of the basolateral markers Na+/K+-ATPase and glucagon-stimulatable adenylate cyclase activities, but are highly enriched with respect to homogenate in the "canalicular marker" enzyme activities leucylnaphthylamidase (48-fold), gamma-glutamyl-transpeptidase (60-fold), 5'-nucleotidase (64-fold), alkaline phosphatase (71-fold), Mg++-ATPase (83-fold), and alkaline phosphodiesterase I (116-fold). In contrast, blLPM are 34-fold enriched in Na+/K+-ATPase activity, exhibit considerable glucagon-stimulatable adenylate cyclase activity, and demonstrate a 4- to 15-fold increase over homogenate in the various "canalicular markers." cLPM have a twofold higher content of sialic acids, cholesterol; and sphingomyelin compared with blLPM. At least three canalicular-(130,000, 100,000, and 58,000 mol wt) and several basolateral-specific protein bands have been detected after SDS PAGE of the two LPM subfractions. Specifically, the immunoglobin A-binding secretory component is restricted to blLPM as demonstrated by immunochemical techniques. These data indicate virtually complete separation of basolateral from canalicular LPM and demonstrate multiple functional and compositional polarity between the two surface domains of hepatocytes.
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PMID:Structural and functional polarity of canalicular and basolateral plasma membrane vesicles isolated in high yield from rat liver. 669 96

Incubation of S49 cell membranes at 0 degree C resulted in a loss of adenylate cyclase activity, but addition of ATP and ATP regenerating system prevented the decrease of the activity. A non-phosphorylating analogue of ATP, adenyl-5'-yl imidodiphosphate, was less effective than ATP. Treatment of solubilized adenylate cyclase with calf intestine alkaline phosphatase caused the decrease of the activity. Membranes from cyc- S49 mutant cells, which are devoid of guanine nucleotide-binding protein, yielded the same results as membranes from S49 cells, indicating that the catalytic component is involved in the alteration of the enzyme activity by these treatments. These results suggest that phosphorylation and dephosphorylation of the catalytic component may regulate adenylate cyclase activity.
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PMID:Alteration of adenylate cyclase activity by phosphorylation and dephosphorylation. 683 11

1. The addition of 50 000g cytosol preparations of isolated human platelets, cultured rat osteogenic sarcoma or cultured bone cells to particulate preparations of adenylate cyclase, from the same or unrelated tissues, caused marked enhancement of the hormone-stimulated enzyme activities. 2. The degree of enhancement obtained by addition of the cytosol preparations was similar to that observed on addition of GTP. 3. The enhancing activity of the three cytosol types was found to be sensitive to digestion by trypsin and alkaline phosphatase, partially heat-labile and partially inactivated by exposure to charcoal. 4. Gel filtration studies indicated an apparent molecular weight of 20 000--30 000. Further, the 20000-30000-mol.wt. fractions obtained by gel filtration could enhance the adenylate cyclase activity of particulate preparations derived from unrelated cell types. 5. The results suggest a common or similar adenylate-cyclase-enhancing factor or factors, protein in nature, present in the three cytosol types.
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PMID:Properties of a factor in cytosol that enhances hormones-stimulated adenylate cyclase activity. 693 Sep 68

Certain metabolic properties of hormonally responsive osteogenic sarcoma cells derived from a transplantable rat tumor have been compared with those of related normal rat bone cells. All studies were carried out on cells grown in monolayer culture. Normal rat bone cells derived by repeated collagenase/trypsin digestion of newborn rat calvaria. Bone cells selected for comparison were thought to be osteoblast-like, as judged by enrichment of alkaline phosphatase and adenylate cyclase responsiveness to parathyroid hormone and prostaglandin E2. The adenylate cyclases of the two cell strains were similarly stimulated by a range of prostanoids and their metabolites and analogs. Morphology showed the two cell strains to be similar; the only obvious difference was a multilayering of cells in the sarcoma cultures, while the normal cultures showed abundant extracellular fibril formation which was not seen in the tumor cells. Investigation of the cAMP-dependent protein kinase isoenzymes showed the presence of two forms in both cell types, one eluting at a low salt concentration and the other at a high salt concentration. There was approximately twice the amount of the first isoenzyme compared to the second isoenzyme. The results indicate the usefulness of the two cell strains to elucidate further the molecular mechanisms of action of parathyroid hormone and prostaglandins.
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PMID:Functional properties of hormonally responsive cultured normal and malignant rat osteoblastic cells. 693 60

Several clonal cell lines from a transplantable rat osteosarcoma, selected on the basis of parathyroid hormone (PTH)-sensitive adenylate cyclase, were established in culture. Bovine PTH-(1-84) (0.1 microM) stimulation of adenylate cyclase varied among clones from 8-fold to none. The level of PTH response was a stable property of each clonal line that was retained through numerous passages in vitro (nearly 3 yr in the oldest clone). Highly PTH-responsive lines had a cuboidal-eliptoid morphology and differed from the nonresponsive lines, which had a more fibroblastic appearance. PTH responsiveness correlated with several properties, presumably associated with the osteoblastic phenotype: elevated alkaline phosphatase activity, synthesis of the gamma-carboxyglutamic acid-containing bone protein, and production of mineralized tumors in host rats. PTH (1.0 nM; 24 h) reduced the alkaline phosphatase activity by 40% when tested in a responsive clone. The acid phosphatase activity of the various cell lines was uniformly low. These osteosarcoma-derived cell lines which are stable in vitro thus seem to reflect the phenotypic heterogeneity observed in the tumor in situ. They could be useful in studies of phenotypic expression, PTH action, and a possible relationship between the two.
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PMID:Parathyroid hormone-responsive clonal cell lines from rat osteosarcoma. 696 73

To show adenylate cyclase (AC) activity in rat calvaria, it is necessary first to decalcify the specimen. In hard tissues, several enzymes (adenosine triphosphatase (ATPase), alkaline phosphatase (APase), adenylate cyclase (AC) and perhaps pyrophosphatase (PPiase) are able to degrade adenosine triphosphate (ATP). The presence of sodium fluoride (NaF) in the incubation medium reduces the quantity of precipitate formed, compared to that observed using a NaF-free incubation medium. Levamisole, used under the same conditions, gives similar results. Possibly NaF inhibits pyrophosphohydrolase and/or phosphatases which mask the AC activity. Adenylylimidophosphate (AMP-PNP), which is a specific AC substrate, confirms the results obtained with ATP. AC activity is demonstrated cytochemically in the osteoblast and preosteoblast membranes, at the junction between two osteoblasts and along the cytoplasmic processes of the osteoblast which penetrate into the osteoid matrix. The osteocytes never show a precipitate, except those which present some osteoblastic features and then only on the membrane facing the osteogenic layer. An intracellular reaction is also evident and is discussed. Parathyroid hormone (PTH) does not reveal new sites of AC activity but increases the quantity of precipitate observed.
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PMID:An attempt at localizing adenylate cyclase in rat calvaria. Influence of sodium fluoride and parathyroid hormone. 700 93

Hepatocytes, endothelial and Kupffer cells were isolated from young adult (3 month) and old (24 month) rat livers and the activities of some plasma membrane, endoplasmic reticulum, mitochondrial, lysosomal and soluble enzymes compared using biochemical and electron microscope cytochemical techniques. Age-associated changes included: a decrease in glucose-6-phosphatase activity both in hepatocytes and sinus lining cells; and increase in alkaline phosphatase in endothelial cells but a decrease in hepatocytes; reduced basal and glucagon-induced adenyl cyclase in hepatocytes and endothelial cells and an increase in the number of hepatocytes with gamma-glutamyl transferase reaction. Cytochemistry showed that heterogeneity may also be characteristic of senescence particularly with regard to hepatocyte glucose-6-phosphatase which was absent in some cells, low in many cells but high in some and gamma-glutamyl transferase which was normally lacking from hepatocytes but localised as large deposits of reaction product on the plasma membranes of occasional cells isolated from old donors.
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PMID:Effects of age on rat liver enzymes. A study using isolated hepatocytes, endothelial and Kupffer cells. 706 Sep 52


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