Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:P15088 (mast cell)
 14,925 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Rat mast cells purified on a Percoll gradient were challenged with compound 48/80 and protein kinase C activity in the cell pellets and the amount of histamine release into the supernatant was assayed by measuring the incorporation of 32P from [gamma 32P]ATP (adenosine triphosphate) into lysine-rich histone and by the fluorometric technique, respectively. In another series of experiments, rat mast cell granules were isolated in a gradient from sonicated rat mast cells and diphosphoinositide kinase activity was assayed by measuring the incorporation of 32P from [gamma 32P]ATP into triphosphoinositide on oxalic acid-impregnated silica gel plates after the extraction of lipids in acidic condition. Azelastine (A-5610, E-0659) inhibited the histamine release from the cells in parallel with the tendency to inhibit the increased protein kinase C activity in the activated mast cells. Azelastine also inhibited the diphosphoinositide kinase activity in the granules. These inhibitory effects of azelastine on the phosphorylation enzymes in rat mast cells may be involved in the inhibitory mechanism of the mediator release from the cells.
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PMID:Inhibitory effects of azelastine on protein kinase C and diphosphoinositide kinase in rat mast cells. 197 Jul 35

Rat mast cell granules were obtained by homogenization of highly purified rat mast cells and isolated in a Percoll gradient. Diphosphoinositide (DPI) synthesis in rat mast cell granules was assayed by measuring the incorporation of 32P from [gamma 32P] ATP into DPI in the absence of exogenous phosphatidylinositol (PI). Lipids were isolated with methanol/chloroform/HCl and were separated by thin-layer chromatography on oxalic acid impregnated silica gel plates. DPI areas were identified by staining with iodine, scraped and measured for 32P radioactivity. The addition of polyamines, spermine and spermidine, to the granules caused an increase of DPI synthesis, which can be catalyzed by PI kinase. This effect of polyamines in the DPI synthesis was in a dose-dependent manner and maximal effects were observed at 1 mM spermine and 10 mM spermidine, respectively.
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PMID:Polyamines stimulate the phosphorylation of phosphatidylinositol in rat mast cell granules. 216 49

Rat mast cell granules were obtained by homogenization of highly purified rat mast cells and isolated in a Percoll gradient. DPI synthesis in rat mast cell granules was assayed by measuring the incorporation of 32P from [gamma 32P] ATP into DPI in the absence of exogenous phosphatidylinositol (PI). Lipids were isolated with methanol/chloroform/HC1 and were separated by thin-layer chromatography on oxalic acid impregnated silica gel plates. DPI areas were identified by staining with iodine, scraped and measured for 32P radioactivity. The addition of PMA to the granules caused an increase of DPI synthesis, which can be catalysed by PI kinase. Neither an inactive phorbol ester, 4-alpha-phorbol-12, 13-didecanoate, nor dimethyl sulfoxide (DMSO) used as a solvent for PMA had any effect. The effect of PMA in the DPI synthesis was dose-dependent and maximal effects were observed at 10-100 ng/ml. Dose-response curves of the effects of PMA in DPI synthesis in the granules corresponded to those of other biochemical effects of PMA in rat mast cells, such as mediator release mediated through the activation of protein kinase C. These results suggest that PMA may directly affect PI kinase or indirectly regulate its activity in rat mast cell granules.
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PMID:[Effect of phorbol myristate acetate (PMA) on diphosphoinositide (DPI) synthesis in rat mast cell granules]. 254 22

Rat mast cell granules were obtained by homogenization of highly purified rat mast cells and isolated in a Percoll gradient. Diphosphoinositide (DPI) synthesis in rat mast cell granules was assayed by measuring the incorporation of 32P from [gamma 32] ATP into DPI in the absence of exogenous phosphatidylinositol (PI). Lipids were isolated with methanol/chloroform/HCl and were separated by thin-layer chromatography on oxalic acid impregnated silica gel plates. DPI areas were identified by staining with iodine, scraped and measured for 32P radioactivity. The addition of polyamines, spermine and spermidine to the granules caused an increase in DPI synthesis, which can be catalyzed by PI kinase. This effect of polyamines on DPI synthesis in the rat mast cell granules was dose-dependent and maximal effects were observed at 1 mM spermine and 10 mM spermidine respectively. When the effect of 1 mM spermine on 32P incorporation into DPI in rat mast cell granules was investigated serially, 32P incorporation into DPI in rat mast cell granules incubated with spermine for 15 min was enhanced significantly (p less than 0.05) compared with that in the granules in the absence of spermine.
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PMID:[Polyamines stimulate the phosphorylation of phosphatidylinositol in rat mast cell granules]. 255 94

Rat mast cell granules were obtained by homogenization of highly purified rat mast cells and isolated in a Percoll gradient. Diphosphoinositide (DPI) synthesis in rat mast cell granules was assayed by measuring the incorporation of 32P from [gamma 32P]ATP into DPI in the absence of exogenous phosphatidylinositol (PI). Lipids were isolated with methanol/chloroform/HCl and were separated by thin-layer chromatography on oxalic acid impregnated silica gel plates. DPI areas were identified by staining with iodine, scraped and measured for 32P radioactivity. The addition of phorbol myristate acetate (PMA) to the granules caused an increase of 32P incorporation from [gamma 32P]ATP in the DPI fraction, which can be catalyzed by PI kinase. This effect of PMA in the DPI synthesis was dose dependent and maximal effects were observed at 10 ng/ml.
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PMID:Phorbol myristate acetate stimulates formation of diphosphoinositide in rat mast cell granules. 255 39

Rat mast cell granules were obtained by sonication of highly purified rat mast cells and isolated in a Percoll gradient. Phosphorylation of endogenous phosphatidylinositol in rat mast cell granules, which is catalyzed by phosphatidylinositol kinase in the granules, was assayed by measuring the incorporation of 32P from [gamma 32P]ATP into phosphatidylinositol 4-phosphate. Lipids were isolated with methanol/chloroform/HCl and were separated by thin-layer chromatography on oxalic acid impregnated silica gel plates. Phosphatidylinositol 4-phosphate areas were identified by staining with iodine, scraped and measured for 32P radioactivity. The phosphorylation reaction was inhibited by 50-500 microM adenosine, ADP and 500 microM AMP in a concentration-dependent manner. Among several anti-allergic drugs investigated. 100-1000 microM theophylline and 10-100 microM azelastine inhibited the phosphorylation reaction, but disodium cromoglycate and ketotifen had little effect.
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PMID:Inhibitory effect of adenine nucleotides and anti-allergic drugs on phosphorylation of phosphatidylinositol in rat mast cell granules. 257 58