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)

Alkaline phosphatase was extracted from human gastric carcinoma cells (KMK-2) under long-term culture, and its biochemical and biological properties were investigated. The enzyme was extremely heat labile and was inhibited significantly by L-homoarginine, but only slightly by L-phenylalanine, so that it was classified as a liver-type alkaline phosphatase. Comparative studies with liver and early placental alkaline phosphatases revealed that the enzymes all showed a similar extent of inhibition by amino acids, heat stability, immunological character, molecular, and other biochemical properties. However, KMK-2 alkaline phosphatase was more similar to early placental enzyme in electrophoretic and gel filtration pattern. This liver-type alkaline phosphatase was found ultrastructurally on microvilli of KMK-2 cells, but not on the lateral structurally on microvilli of KMK-2 cells, but not on the lateral surface with interdigitating folds. Prednisolone markedly decreased the content of the present isozyme. Although the present phenotype was stable during long-term culture in regard to the isozyme properties, the original cancer cells from which the cell line had been derived were L-phenylalanine sensitive and moderately L-homoarginine sensitive. This indicated that phenotypic change occurred on cultivation of cancer cells in vitro.
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PMID:Characterization of liver-type alkaline phosphatase from human gastric carcinoma cells (KMK-2) in vitro. 49

The cellular localization and isoenzyme pattern of alkaline phosphatase in five cell lines derived from human bladder carcinomas (T24, RT4, RT112, J82, EJ) shown not to be HeLa cells has been established. RT112 cells had a high level of alkaline phosphatase. RT4 had a moderate amount of alkaline phosphatase but in the other three lines, levels were extremely low. Prednisolone caused a small (2 to 3-fold) increase in total alkaline phosphatase in T24 and RT112 lines only. Electrophoretic separation of isoenzymes showed that RT112 and RT4 cells (derived from more highly differentiated tumor types) had three heat stable bands equivalent to placental alkaline phosphatase and three slower bands of a modified placental type. Prednisolone increased only the former. In T24 cells the enzyme resembled the liver-type alkaline phosphatase in electrophoretic mobility and sensitivity to heat denaturation. Cytochemical studies confirmed the presence of cell surface-associated extramembraneous placental type enzyme in RT112 cells. All five cell lines had small deposits of intramembraneous alkaline phosphatase in the plasma membrane and deposits associated tith the mitochondrial membranes and the endoplasmic reticulum that were not completely inhibited by phenylalanine or Levamisole.
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PMID:Alkaline phosphatase activity in human bladder tumor cell lines. 87 May 58

HeLa TCRC-1, is a monophenotypic cell line for the production of the carcinoplacental Regan isoenzyme of alkaline phosphatase. It has been previously reported that, when this cell line is grown in immunosuppressed rats, there is an alteration of phenotypic expression in that an isoenzyme that is referred to as oncoamnion (FL) becomes the dominant enzyme form. This report describes the isoenzyme regulation after these cells are returned to culture for at least three months. These cells in culture demonstrate a density-dependent alteration in isoenzyme profiles. The Regan isoenzyme is the dominant isoenzyme form in new, sparsely populated cultures, while the oncoamnion isoenzyme predominates in the later high-density stages of growth. Prednisolone induction of enzyme activity is found to be most effective in the early stages of growth, and the previously reported specificity of hormone action on isoenzymes produced by cancer cells is maintained. Enzyme induction is restricted to the Regan isoenzyme, while hormone-mediated diminution in enzyme activity is confined to the oncoamnion (FL) isoenzyme.
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PMID:Evidence for altered gene regulation in HeLa cells returned to culture after growing in immunosuppressed rats. 97 60

A case of polymyositis associated with chronic active hepatitis was reported. A 53-year-old man, who had no previous history of blood transfusion nor hepatitis, noticed proximal dominant muscle weakness on January 29, 1985. He was admitted to Kyoto National Hospital on February 7, and laboratory studies disclosed the elevation of serum enzyme levels; creatine kinase (CK) 9845 IU/L (normal 54-263), glutamate oxaloacetate transaminase (GOT) 834 IU/L (9-31), glutamate pyruvate transaminase (GPT) 491 IU/L (4-34), lactate dehydrogenase (LDH) 2135 IU/L (248-464). Also serum gamma globulin was high (1.8 g/dl) and LE-like cell was found. The diagnosis of polymyositis was made and prednisolone therapy (60 mg/day) was started on February 23. The elevated serum enzymes decreased gradually, but severe muscle weakness persisted for about one month. On April 3, he was admitted to our hospital. Physical examination revealed moderate proximal dominant muscle weakness without skin eruption, jaundice or hepatosplenomegaly. The serum enzymes were still high; CK 1826, GOT 173, GPT 232 (GOT less than GPT), LDH 1548. However, alkaline phosphatase (ALP) and bilirubin were normal. Hepatitis B surface antigen (HBsAg) was not detected. Antinuclear antibody was positive. The electromyogram study showed myopathic change, and the muscle biopsy demonstrated myopathic change and cell infiltration, compatible with polymyositis. These results suggested liver dysfunction associated with polymyositis. Prednisolone therapy was continued and muscle weakness decreased. From December, 1985, serum enzymes (CK, GOT, GPT, LDH) elevated again and muscle weakness also slightly increased. Anti-smooth muscle antibody was positive. It was suggested that both polymyositis and liver dysfunction deteriorated.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:[A case of polymyositis associated with chronic active hepatitis]. 218 64

A randomized, double-blind, 1-year pilot study of prednisolone treatment for primary biliary cirrhosis was undertaken. Nineteen patients received 30 mg prednisolone per day initially, with a maintenance dose of 10 mg per day. Seventeen patients received placebo. The groups were matched for age, menopausal status, hepatic histological stage and bilirubin. Treatment was well tolerated without dropouts. Two patients receiving prednisolone developed diabetes, one a duodenal ulcer and one depression. One patient receiving placebo died for liver failure after 3 months. Cholestatic symptoms (itch and fatigue) improved on prednisolone. There was significant (prednisolone vs. placebo) improvement in transaminase (p = 0.0214), alkaline phosphatase (p = 0.0032), procollagen III peptide (p = 0.0103), immunoglobulin G (p = 0.0012) and liver histology (p = 0.016); these changes were greatest among noncirrhotic patients. No patient developed skeletal symptoms. Fifty-seven per cent had abnormal triolein breath tests prior to treatment, and 65% had abnormally low calcium absorption tests. Calcium absorption increased significantly in the treated group vs. placebo at 2 weeks (p less than 0.02), but not at 1 year. Femoral photon absorptiometry fell in the prednisolone group after 1 year (-3.5% vs. placebo +0.5%, p less than 0.05), as did trabecular bone volume (-6% vs. -2.8%, p less than 0.005) and resorption surface (-11% vs. +2%, p less than 0.02) on serial bone biopsy. Prednisolone seems to exert a favorable hepatic effect in primary biliary cirrhosis but at the expense of increased bone loss to approximately twice the expected rate. Prednisolone treatment merits further assessment in primary biliary cirrhosis over a longer period, with attention to selection of patients most likely to benefit and continuing observation of bone mass to better establish the "cost/benefit" ratio.
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PMID:A pilot, double-blind, controlled 1-year trial of prednisolone treatment in primary biliary cirrhosis: hepatic improvement but greater bone loss. 277 3

Human urinary bladder carcinoma cells (JTC-32) retain a low alkaline phosphatase activity. Prednisolone or a hypertonic concentration of NaCl caused a moderate increase in the activity (10- to 15-fold of control), but dibutyryl cAMP or butyrate did not. Examination of the combined effect of these four agents revealed that they acted synergistically in any combination. When the cells were incubated with the four agents together, the enzyme activity increased 60- to 250-fold. Serum also contributed to this synergistic increase. These agents slightly inhibited cell growth and protein synthesis. The enzyme induction was completely inhibited by cycloheximide or actinomycin D. The synergistic effect of the four agents on the enzyme activity was also observed in other strains of carcinoma cells, human urinary bladder carcinoma cells (JTC-30) and monkey hepatocarcinoma cells (NCLP-6E). Thus, it is concluded that the coexistence of the four agents provides general and superior conditions for the induction of alkaline phosphatase in cultured carcinoma cells.
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PMID:Induction of alkaline phosphatase activity by synergistic action of dibutyryl cyclic adenosine monophosphate, prednisolone, butyrate and sodium chloride in cultured cells. 283 93

The in vitro intestinal ring uptake of prednisolone (11 beta,17,21-trihydroxypregna-1,4-diene-3,20-dione), prednisolone 21-succinate, and prednisolone 21-phosphate was compared in rings prepared from rat jejunum and colon. An HPLC assay was developed to determine whether the drug or intact prodrug was taken up by the tissue. In jejunum and colon, the uptake of prednisolone was limited by its solubility (0.84 mM, 37 degrees C). The freely soluble succinate and phosphate esters were well absorbed in the jejunum. The only species detected in jejunal tissue after incubation with prednisolone 21-phosphate was prednisolone, indicating hydrolysis prior to absorption. This implication was verified by light microscopy. Incubation of tissue from the jejunum with prednisolone 21-succinate resulted in uptake of a mixture of prodrug and parent drug, with the latter form predominating. Prednisolone 21-succinate was also absorbed well in the colon, where the predominant species taken up by the tissue was the intact ester. The half-life of the succinate ester in the tissue was approximately 1 h postincubation, implicating enzyme mediation. Uptake of the phosphate ester by the colon was less than 20% of that observed in the jejunum, with the species absorbed still being primarily the parent alcohol. Light microscopy techniques confirmed that prednisolone 21-phosphate and hydrocortisone 21-phosphate are good substrates for brush border membrane alkaline phosphatase in the jejunum, and that lack of this enzyme in colon tissue was most likely responsible for poor uptake in the colon.
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PMID:Uptake of prodrugs by rat intestinal mucosal cells: mechanism and pharmaceutical implications. 379 23

In order to characterize newly established human urinary bladder carcinoma cell lines (JTC-29, JTC-30, JTC-31, JTC-32, JTC-33 and JTC-34) by Kakuya et al. [In Vitro, 19, 591-599 (1983)], we investigated alkaline phosphatase in these cell lines. Relatively high alkaline phosphatase activity was found in JTC-29 and JTC-32 cells, but the enzyme activity in the other cell lines was very low. Prednisolone induced alkaline phosphatase activity even at 0.005 micrograms/ml (14 nM) and the effect was maximal at 0.05 micrograms/ml. NaCl also induced alkaline phosphatase activity at 50 mM. A further increase in the activity was observed at 0.1 M NaCl, but at 0.2 M all cells came off from plastic culture dishes without an increase in the enzyme activity during the incubation for 24 h at 37 degrees C. Both actinomycin D and cycloheximide abolished the increases in the enzyme activity with prednisolone or NaCl. The Lineweaver-Burk plot showed that the increases in the enzyme activity are due to the increases in Vmax, but not in Km. Alkaline phosphatase in JTC-32 cells and prednisolone-treated JTC-32 cells was heat stable and 100% of the initial enzyme activity remained after 30 min of incubation at 56 degrees C. However, the enzyme in JTC-29 cells was heat labile and its activity was reduced to less than 50% after 20 min of incubation at 56 degrees C. L-Phenylalanine was the strongest inhibitor for the enzyme reactions in JTC-32 cell homogenates among L-phenylalanine, L-leucine and L-homoarginine, whereas L-homoarginine was the strongest for the enzyme reactions in JTC-29 cell homogenates.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Characterization of alkaline phosphatase in human urinary bladder carcinoma cell lines and enzyme regulation with prednisolone or sodium chloride. 393 23

The alkaline phosphatase (AP) and gamma-glutamyl-transpeptidase (GGT) activities and the effect of steroid treatment were studied in human bile and serum following choledochotomy. Activity of the two enzymes in the bile changed in parallel. Following the operation the enzyme activities initially decreased, but after 3 days they showed a progressive increase and reached their maximum on day 6. It appears that the bile is a major route for the elimination of both enzymes from the damaged liver. 60 mg Prednisolone on the day of operation and 2 days after surgical intervention prevented the initial decline in enzyme activity and significantly increased the excretion of enzymes. The possible pathogenesis of enzymatic changes after choledochotomy is discussed.
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PMID:Bile enzyme activities following choledochotomy and the effect of steroid treatment. 614 63

Agglutinability by concanavalin A was measured with HeLa65 cells grown with prednisolone or sodium butyrate, 2 compounds that increase the activity of the carcinoplacental form of alkaline phosphatase, an enzyme localized in membranes. Prednisolone enhanced concanavalin A agglutination approximately 3-fold while sodium butyrate had no effect.
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PMID:Effects of prednisolone and butyrate on agglutinability of HeLa cells by concanavalin A. 686 73


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