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Adenosine inhibits the rise in intracellular calcium and platelet aggregation produced by thrombin: evidence that both effects are coupled to adenylate cyclase.
Paul S, Feoktistov I, Hollister AS, Robertson D, Biaggioni I
(1990) Mol Pharmacol 37: 870-5
MeSH Terms: Adenosine, Adenosine-5'-(N-ethylcarboxamide), Adenylyl Cyclases, Caffeine, Calcium, Cytosol, Humans, Platelet Aggregation, Platelet Aggregation Inhibitors, Thrombin, Xanthines
Show Abstract · Added December 10, 2013
Platelet aggregation and secretion are associated with a rise in intracellular calcium concentration ([Ca2+]i). Adenosine has been postulated as an endogenous inhibitor of platelet aggregation. The antiaggregatory effects of adenosine are related to activation of adenylate cyclase. We studied the effect of adenosine on the rise in [Ca2+]i and platelet aggregation produced by thrombin. Human platelets were obtained from dextrose/citrate-treated plasma. [Ca2+]i was determined by fluorescence-dye techniques (fura-2). Adenosine inhibited the slope of the first phase of aggregation and the rise in [Ca2+]i produced by thrombin, in a dose-dependent manner. The dose that produced 50% inhibition of both aggregation and the rise in [Ca2+]i was approximately 500 nM. The effects of adenosine on [Ca2+]i were shared by its stable analogs, 5'-N-ethylcarboxamidoadenosine being approximately 10-fold more potent than (-)N6-phenylisopropyladenosine, suggesting that these effects were mediated through adenosine A2 receptors. Furthermore, caffeine antagonized the inhibitory effects of adenosine on platelet aggregation and [Ca2+]i. The effects of adenosine on [Ca2+]i appear to be mediated through a rise in intracellular cAMP, because they were prevented by the adenylate cyclase inhibitor 2',5'-dideoxyadenosine (1 mM) and were potentiated by phosphodiesterase inhibition with papaverine (1 microM). Adenosine also inhibits the rise in [Ca2+]i produced by thrombin in a calcium-free medium, suggesting that adenosine inhibits both calcium influx and the release of calcium from intracellular stores.
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11 MeSH Terms
Stimulation of casein kinase II by epidermal growth factor: relationship between the physiological activity of the kinase and the phosphorylation state of its beta subunit.
Ackerman P, Glover CV, Osheroff N
(1990) Proc Natl Acad Sci U S A 87: 821-5
MeSH Terms: Alkaline Phosphatase, Amino Acids, Casein Kinases, Cell Line, Cytosol, Epidermal Growth Factor, Humans, Kinetics, Macromolecular Substances, Molecular Weight, Phosphates, Phosphorylation, Protein Kinases, Tumor Cells, Cultured
Show Abstract · Added March 5, 2014
To determine relationships between the hormonal activation of casein kinase II and its phosphorylation state, epidermal growth factor (EGF)-treated and EGF-naive human A-431 carcinoma cells were cultured in the presence of [32P]orthophosphate. Immunoprecipitation experiments indicated that casein kinase II in the cytosol of EGF-treated cells contained approximately 3-fold more incorporated [32P]phosphate than did its counterpart in untreated cells. Levels of kinase phosphorylation paralleled levels of kinase activity over a wide range of EGF concentrations as well as over a time course of hormone action. Approximately 97% of the incorporated [32P]phosphate was found in the beta subunit of casein kinase II. Both activated and hormone-naive kinase contained radioactive phosphoserine and phosphothreonine but no phosphotyrosine. On the basis of proteolytic mapping experiments, EGF treatment of A-431 cells led to an increase in the average [32P]phosphate content (i.e., hyperphosphorylation) of casein kinase II beta subunit peptides which were modified prior to hormone treatment. Finally, the effect of alkaline phosphatase on the reaction kinetics of activated casein kinase II indicated that hormonal stimulation of the kinase resulted from the increase in its phosphorylation state.
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14 MeSH Terms
Localization of a reactive exofacial sulfhydryl on the glucose carrier of human erythrocytes.
May JM, Buchs A, Carter-Su C
(1990) Biochemistry 29: 10393-8
MeSH Terms: Binding Sites, Biological Transport, Bromosuccinimide, Cysteine, Cytochalasin B, Cytosol, Erythrocyte Membrane, Erythrocytes, Glucose, Humans, Maleimides, Monosaccharide Transport Proteins, Sulfhydryl Compounds, Thiocyanates, Trypsin
Show Abstract · Added December 10, 2013
Tryptic digestion studies of the human erythrocyte glucose carrier have shown that a reactive and transport-sensitive exofacial sulfhydryl is located in the carboxy-terminal half of the molecule, corresponding to Cys347, Cys421, or Cys429. In the present studies, the erythrocyte glucose carrier labeled on the exofacial sulfhydryl with bis(maleimidomethyl) ether-L-[35S]cysteine was chemically cleaved, either at tryptophans by N-bromosuccinimide or at nonalkylated cysteines by 2-nitro-5-thiocyanobenzoic acid. The resulting fragments were separated by linear gradient polyacrylamide gel electrophoresis, and the labeled fragments were identified by their apparent molecular weight, and by immunoblotting with antibodies to specific regions of the carrier protein. All of the labeled fragments were recognized by an antibody to the carboxy terminus of the carrier, but not by an antibody to a cytoplasmic loop on the C-terminal half of the carrier. The labeled exofacial sulfhydryl was assigned to Cys429, since this is the only residue of the three possibilities which is beyond the expected cleavage sites of the two reagents in the carrier sequence. These results concur with the predictions of hydropathy analysis and will be relevant for studies of how modification of this sulfhydryl affects carrier function, particularly since several other known carrier isoforms lack a corresponding cysteine.
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15 MeSH Terms
Metabolism of oleic acid in differentiating BFC-1 preadipose cells.
Abumrad NA, Forest C, Regen DM, Barnella US, Melki SA
(1991) Am J Physiol 261: E76-86
MeSH Terms: Adipose Tissue, Animals, Carrier Proteins, Cell Differentiation, Cell Division, Cell Line, Cytosol, Fatty Acid-Binding Protein 7, Fatty Acid-Binding Proteins, Glycerol, Kinetics, Lipolysis, Mice, Neoplasm Proteins, Nerve Tissue Proteins, Oleic Acid, Oleic Acids, Phospholipids, Triglycerides
Show Abstract · Added December 10, 2013
Incorporation of [3H]oleate and [14C]glucose into cellular lipids was studied in the preadipose cell line BFC-1 to determine flux changes that accompany the adipose conversion process. Dilution of oleate by intracellular fatty acids (FA) was estimated from the 3H/14C incorporation ratios and from relating steady-state radioactivity in diglycerides to their measured cellular levels. The data indicated that exogenous FA mixed with less than 1% of endogenous FA on its pathway to esterification. Conversion of preadipocytes to adipocytes increased uptake of FA and glucose by approximately 3-fold and synthesis of diglycerides and triglycerides by 5- and 16-fold, respectively, with little if any increase of phospholipid synthesis. A 50% drop in 3H/14C incorporation ratio indicated a doubling of the rate at which endogenous FA mixed with the exogenous FA that had entered the cell. Adipocytes compared with preadipocytes exhibited a 50% greater cell diameter and a doubling of intracellular water volume and of protein and phospholipid levels, reflecting cellular enlargement consequent to the arrest of cell division that precedes adipose conversion. Diglyceride levels were also increased in adipocytes, however, since their turnover was fast, as indicated by rapid equilibration of diglyceride labeling; the increase reflected changes in their relative rates of synthesis and disposal. Diglyceride levels related to cell phospholipid, and other indexes of cell size remained constant. This indicated that the supply of diglycerides was tightly coupled to the synthesis of triglycerides and phospholipids, which suggested feedback regulation of diglyceride formation. The studies provide a methodological approach to measurement and interpretation of rates of lipid deposition in cultured cells.
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19 MeSH Terms
Arachidonic acid metabolism of cytosolic fractions of Lewis lung carcinoma cells.
Marnett LJ, Leithauser MT, Richards KM, Blair I, Honn KV, Yamamoto S, Yoshimoto T
(1991) Adv Prostaglandin Thromboxane Leukot Res 21B: 895-900
MeSH Terms: 12-Hydroxy-5,8,10,14-eicosatetraenoic Acid, Animals, Arachidonic Acid, Arachidonic Acids, Cytosol, Hydroxyeicosatetraenoic Acids, Lipoxygenase Inhibitors, Lung Neoplasms, Mice, Molecular Structure, Substrate Specificity, Tumor Cells, Cultured
Added March 5, 2014
0 Communities
1 Members
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12 MeSH Terms
Cytosolic acidification stimulates a calcium influx that activates Na(+)-H+ exchange in LLC-PK1.
Burns KD, Homma T, Breyer MD, Harris RC
(1991) Am J Physiol 261: F617-25
MeSH Terms: Ammonium Chloride, Animals, Calcium, Carrier Proteins, Cytosol, Epithelial Cells, Epithelium, Hydrogen-Ion Concentration, Kidney, Osmolar Concentration, Sodium-Hydrogen Exchangers
Show Abstract · Added January 28, 2014
We have previously shown that cytosolic acidification-stimulated Na(+)-H+ exchange in LLC-PK1 cells is inhibited by calmodulin antagonists. To investigate further the role of Ca(2+)-calmodulin-dependent processes in intracellular pH (pHi) regulation in these cells, we studied the effects of pHi changes on cytosolic Ca2+ concentration ([Ca2+]i). In fura-2/acetoxymethylester (fura-2/AM)-loaded cells maintained in isotonic Na(+)-free buffer containing 1.8 mM CaCl2, [Ca2+]i was 168 +/- 59 nM (n = 5). After NH4Cl-induced alkalinization, [Ca2+]i decreased to 83 +/- 28 nM and partially recovered to 126 +/- 42 nM. Cytosolic acidification, after NH4Cl washout, caused an increase in [Ca2+]i to 481 +/- 166 nM (P less than 0.05; n = 5) that was dependent on extracellular Ca2+. An increase in [Ca2+]i was also observed in cells acidified with KCl-nigericin, with a return of [Ca2+]i to baseline with cell alkalinization. No increase in 45Ca2+ efflux occurred in association with initial NH4Cl-induced [Ca2+]i decrease, suggesting Ca2+ flux into an intracellular store during alkalinization. Membrane depolarization did not alter [Ca2+]i. The acidification-induced [Ca2+]i increase was inhibited by preincubation with verapamil or the calmodulin antagonist N-(6-aminohexyl)-5-chloro-1-naphthalenesulfonamide (W-7). Na(+)-dependent pHi recovery in 2,'7'-bis(carboxyethyl)-5(6)-carboxyfluorescein acetoxymethylester (BCECF/AM)-loaded LLC-PK1 cells and cytosolic acidification-stimulated basolateral Na(+)-H+ exchange activity in LLC-PK1/CL4 cells were both attenuated in the absence of extracellular Ca2+. The results indicate that cytosolic acidification activates an influx of extracellular Ca2+ in LLC-PK1 cells. Furthermore, in the absence of Ca2+ influx, Na(+)-H+ exchange is inhibited.(ABSTRACT TRUNCATED AT 250 WORDS)
1 Communities
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11 MeSH Terms
Regulation of Na(+)-H+ exchange by ATP depletion and calmodulin antagonism in renal epithelial cells.
Burns KD, Homma T, Harris RC
(1991) Am J Physiol 261: F607-16
MeSH Terms: Adenosine Triphosphate, Amiloride, Animals, Calmodulin, Carrier Proteins, Cell Membrane, Cells, Cultured, Cytosol, Epithelial Cells, Epithelium, Hydrogen-Ion Concentration, Kidney, Protein Kinase C, Sodium-Hydrogen Exchangers, Sulfonamides
Show Abstract · Added January 28, 2014
The present studies examined effects of ATP depletion and calmodulin antagonism on stimulation of Na(+)-H+ exchange by cytosolic acidification in renal epithelial cells (LLC-PK1). ATP depletion significantly inhibited both amiloride-sensitive 22Na+ uptake (P less than 0.001; n = 12) and Na(+)-dependent intracellular pH (pHi) recovery in 2',7'-bis (carboxyethyl)-5(6)-carboxyfluorescein acetoxymethylester (BCECF/AM)-loaded cells. Calmodulin antagonists, N-(6-aminohexyl)-5-chloro-1-naphthalene-sulfonamide (W-7) and calmidazolium, both caused a concentration-dependent inhibition of Na(+)-H+ exchange activity. The W-7-induced inhibition of Na(+)-H+ exchange occurred in cells incubated for 24 h with phorbol 12-myristate 13-acetate, indicating that the effect of W-7 was not mediated by protein kinase C inhibition. Both W-7 and ATP depletion shifted the pHi dependence of the antiporter, and ATP depletion also reduced the maximal activity. In LLC-PK1/CL4 cells grown on permeable filters, W-7 inhibited the cytosolic acidification-stimulated basolateral exchanger by 54 +/- 5% (P less than 0.005; n = 7) and, in contrast, stimulated the apical exchanger by 28 +/- 13% (P less than 0.05; n = 6). ATP depletion significantly inhibited apical Na(+)-H+ exchange. These results suggest that an ATP-Ca(2+)-calmodulin-dependent process is involved in regulation of Na(+)-H+ exchange in LLC-PK1 cells. A Ca(2+)-calmodulin-dependent process activated the amiloride-sensitive basolateral Na(+)-H+ exchanger and inhibited the amiloride-resistant apical antiporter. Phosphorylation of these two Na(+)-H+ exchangers or regulatory proteins by a Ca(2+)-calmodulin-dependent protein kinase may mediate this differential regulation.
1 Communities
1 Members
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15 MeSH Terms
Glutathione conjugation of aflatoxin B1 exo- and endo-epoxides by rat and human glutathione S-transferases.
Raney KD, Meyer DJ, Ketterer B, Harris TM, Guengerich FP
(1992) Chem Res Toxicol 5: 470-8
MeSH Terms: Aflatoxin B1, Animals, Catalysis, Cytosol, Glutathione, Glutathione Transferase, Humans, In Vitro Techniques, Liver, Magnetic Resonance Spectroscopy, Male, Mice, Rats, Rats, Sprague-Dawley, Stereoisomerism, Sulfhydryl Compounds
Show Abstract · Added March 5, 2014
Much evidence supports the view that the rate of conjugation of glutathione (GSH) with aflatoxin B1 (AFB1) exo-epoxide is an important factor in determining the species variation in risk to aflatoxins and that induction of GSH S-transferases can yield a significant protective effect. An assay has been developed in which the enzymatic formation of the conjugates of GSH and AFB1 exo-epoxide and the recently described AFB1 endo-epoxide is measured directly. 1H NMR spectra are reported for both the AFB1 exo- and endo-epoxide-GSH conjugates. Structural assignments were made by comparison with AFB1 exo- and endo-epoxide-ethanethiol conjugates, for which nuclear Overhauser effects were measured to establish relative configurations. The endo-epoxide was found to be a good substrate for GSH conjugate formation in rat liver cytosol while mouse liver cytosol conjugated the exo-epoxide almost exclusively. Human liver cytosol conjugated both epoxide isomers to much lower extents than did cytosols prepared from rats or mice. Purified rat GSH S-transferases catalyzed the formation of the AFB1 exo-epoxide-GSH conjugate in the order 1-1 approximately 4-4 approximately 3-3 greater than 2-2 greater than 4-6 (7-7 and 8-8 did not form the exo-epoxide-GSH conjugate at levels above the nonenzymatic rate). The only rat GSH S-transferases that conjugated the endo-epoxide were 4-4 and 4-6, with 4-4 being the more active.(ABSTRACT TRUNCATED AT 250 WORDS)
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16 MeSH Terms
Effect of folacin deficiency on folacin-binding proteins in the rat.
Zamierowski MM, Wagner C
(1977) J Nutr 107: 1937-45
MeSH Terms: Animals, Carrier Proteins, Cell Fractionation, Cytosol, Diet, Folic Acid, Folic Acid Deficiency, Liver, Male, Mitochondria, Liver, Rats, Tissue Distribution
Show Abstract · Added January 20, 2015
The effect of experimental folacin deficiency on the uptake and distribution of radioactive folic acid in the rat was investigated. Less radioactivity was taken up by livers of deficient rats than controls 24 hours after intraperitoneal injection of [3H]-folic acid, although more radioactivity was incorporated by the brain and kidneys of deficient rats. The distribution of radioactivity among the three folacin-binding proteins of rat liver cytosol and the binding protein of mitochondria was also studied. In deficiency, very little radioactivity was incorporated into cytosol binding proteins I and II, while more radioactivity was incorporated into cytosol binding protein II and the mitochondrial binding protein. A decrease in the endogenous folacin associated with all protein-bound and free forms was seen in deficiency with the major decrease coming at the expense of unbound folacin, and cytosol binding protein I. This latter protein may have a primary storage role in the liver.
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12 MeSH Terms
Identification of folate binding proteins in rat liver.
Zamierowski MM, Wagner C
(1977) J Biol Chem 252: 933-8
MeSH Terms: Animals, Biological Transport, Carrier Proteins, Cell Fractionation, Cell Membrane, Cell Nucleus, Cytosol, Folic Acid, Liver, Mitochondria, Liver, Molecular Weight, Rats, Subcellular Fractions, Tetrahydrofolate Dehydrogenase
Show Abstract · Added January 20, 2015
Intraperitoneal injection of tritiated folic acid (PteGlu) into rats has revealed the presence of three separate protein fractions in the cytosol fraction of the liver and one in the mitochondria which bind folate derivatives. The proteins in the cytosol (cytosol I, II and III) have approximate molecular weights of 350,000, 150,000, and 25,000 and the protein in the mitochondria has an approximate molecular weight of 90,000 as estimated by gel filtration. The bound folate derivatives are primarily polyglutamate forms while cytosol II contains primarily bound 5-methyltetrahydrofolate polyglutamate derivatives. Little binding of radioactively labeled folic acid or 5-methyltetrahydrofolate to these fractions was observed when binding was carried out in vitro. Significant binding in vitro was observed, however, when a mixture of biosynthetically labeled natural folate derivatives was used. These proteins have not been purified, but cytosol III partially consists of the enzyme, tetrahydrofolate dehydrogenase (EC 1.5.1.3). Studies on the time course of folic acid incorporation into the liver showed that soon after injection nonmetabolized folic acid was bound to the plasma membrane fraction of the liver cell. It is suggested that at least one of the binding proteins in the cytosol may be involved in storage of the vitamin while the binding of nonmetabolized folic acid to the plasma membrane may reflect the existence of a carrier for folic acid transport into the cell.
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14 MeSH Terms