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At least 1,333 records · Page 74Linked to original sources
PubMed1991

The mechanism for synergism between phospholipase C- and adenylylcyclase-linked hormones in liver. Cyclic AMP-dependent kinase augments inositol trisphosphate-mediated Ca2+ mobilization without increasing the cellular levels of inositol polyphosphates.

The ability of cAMP-dependent hormones to modulate the actions of Ca2(+)-mobilizing hormones was studied in single fura-2-injected guinea pig hepatocytes. In 91% of cells the cAMP-linked hormone, isoproterenol, applied alone, did not alter cytosolic Ca2+ concentration. In 78% of cells which had been pre-exposed to a low concentration of angiotensin II, isoproterenol was able to increase cytosolic Ca2+. Isoproterenol did not, however, increase inositol 1,4,5-trisphosphate or inositol tetrakisphosphate on its own, or in the presence of angiotensin II. Isoproterenol was also able to raise cytosolic Ca2+ concentration in cells microinjected with inositol 2,4,5-trisphosphate or a photoactivatable derivative of inositol 1,4,5-trisphosphate. The elevation of cytosolic Ca2+ concentration induced by isoproterenol in angiotensin II-treated cells and cells injected with caged inositol 1,4,5-trisphosphate was blocked by heparin, implying that the effect was mediated by an inositol 1,4,5-trisphosphate receptor agonist. In permeabilized hepatocytes, inositol 1,4,5-trisphosphate-induced Ca2+ release was enhanced by 8-bromo-cAMP and the catalytic subunit of cAMP-dependent kinase. Cyclic AMP-dependent kinase shifted the dose-response curve for inositol 1,4,5-trisphosphate-mediated Ca2+ release to the left by a factor of 4 and increased the total amount of Ca2+ released by 25%. These results indicate that increased sensitivity of the intracellular Ca2+ releasing organelle to inositol 1,4,5-trisphosphate is responsible for synergism between phospholipase C- and adenylylcyclase-linked hormones in the liver.

Adenylyl Cyclases↗
PubMed1991

Diadenosine polyphosphates inhibit the action of ribonucleotide reductase on ADP.

Using permeabilized cells prepared according to Lammers, M. and Follmann, H. (Arch. Biochem. Biophys. 244, 430-438, 1986), the ribonucleotide reductase (EC 1.17.4.1) of yeast was assayed in situ. In our experimental conditions, 40-200 pmoles of ADP were reduced in 10 min per 5 x 10(7) cells. Concentrations of 0.01 mM of diadenosine tri, tetra, penta and hexaphosphates elicited inhibitions of 37, 40, 63 and 58%, respectively. The enzyme was almost completely inhibited in the presence of 0.05 mM diadenosine pentaphosphate. As some of these dinucleotides are present in yeast cells at these concentrations, the reported inhibition may have physiological meaning.

Adenosine Diphosphate↗
PubMed1990

Cyclic AMP inhibits inositol polyphosphate production and calcium mobilization in neuroblastoma X glioma NG108-15 cells.

In the neuroblastoma X glioma hybrid cell line NG108-15, bradykinin (BK) receptor stimulation induced a rapid and concentration-dependent rise in cytosolic free Ca2+ levels, as measured with the Ca2(+)-sensitive fluorescent dye fura-2. The Ca2+ transient was present in the absence of extracellular Ca2+ and was associated with a concentration-dependent production of inositol phosphates, particularly inositol trisphosphate (InsP3). Pretreatment of intact NG108-15 cells with forskolin or dibutyryl-cAMP plus isobutylmethylxanthine reduced BK-stimulated InsP3 production and the increase in cytosolic free Ca2+. Membranes prepared from forskolin- and [3H]inositol-pretreated NG108-15 cells also showed a diminished production of InsP3 elicited by guanosine 5'-[gamma-thio]triphosphate, NaF, or BK plus GTP. On the other hand, the Ca2+ sensitivity of membrane-associated phosphoinositide-specific phospholipase C (PI-PLC) was unaffected by forskolin pretreatment of intact NG108-15 cells. Collectively, these results suggest that A-kinase may inhibit receptor-mediated and postreceptor stimulation of PI-PLC in neuron-like cells, perhaps by impairing the coupling between a guanine nucleotide-binding protein and PI-PLC.

Adenylyl Cyclases↗
PubMed1990

Formation of inositol polyphosphates in airway smooth muscle after muscarinic receptor stimulation.

The effect of muscarinic-receptor stimulation on [3H]inositol mono-, bis-, tris- and tetrakisphosphate (InsP1, InsP2, InsP3 and InsP4) accumulation was examined in bovine tracheal smooth muscle slices prelabeled with myo-[3H]inositol. Carbachol (0.1 mM) caused a rapid increase in [3H]InsP3 and [3H]InsP2 followed by delayed increases in [3H]InsP1 and [3H]InsP4 accumulation. Analysis of the [3H]InsP3 isomers by HPLC showed an immediate although transient increase in [3H]Ins(1,4,5)P3 with a progressive and sustained accumulation of [3H]Ins(1,3,4)P3. [3H]Ins(1,3,4)P3 was confirmed as the predominant (greater than 80%) [3H]InsP3 isomer present at 1 and 30 min using an enzymatic method which causes selective hydrolysis of Ins(1,3,4)P3. Lithium enhanced markedly the carbachol-stimulated accumulation of [3H]InsP1 and [3H]InsP2 with a lower potency than that observed in other tissues but had no significant influence on [3H]InsP3 or [3H]InsP4 values. These data support a role for Ins(1,4,5)P3 in initiating airway smooth muscle contraction and indicate the importance of the Ins(1,3,4,5)P4/Ins(1,3,4)P4 pathway in this tissue.

Animals↗
PubMed1985

Relationship between secretagogue-induced Ca2+ release and inositol polyphosphate production in permeabilized pancreatic acinar cells.

We have previously shown that inositol trisphosphate (IP3) releases Ca2+ from a nonmitochondrial pool of permeabilized rat pancreatic acinar cells (Streb, H., Irvine, R. F., Berridge, M. J., and Schulz, I. (1984) Nature 306, 67-69). This pool was later identified as endoplasmic reticulum (Streb, H., Bayerdorffer, E., Haase, W., Irvine, R. F., and Schulz, I. (1984) J. Membr. Biol. 81, 241-253). As IP3 is produced by hydrolysis of phosphatidylinositol bisphosphate on activation of many "Ca2+-mobilizing receptors," our observation supported the proposal that IP3 functions as a second messenger to release Ca2+ from the endoplasmic reticulum. We have here used the same preparation of permeabilized acinar cells to study the relationship of secretagogue-induced Ca2+ release and IP3 production. We show that: 1) secretagogue-induced Ca2+ release in permeabilized cells is accompanied by a parallel production of inositol trisphosphate. 2) When the secretagogue-induced increase in intracellular free Ca2+ concentration was abolished by ethylene glycol bis(beta-aminoethyl ether)-N,N,N',N'-tetraacetic acid buffering, secretagogue-induced IP3 production was unimpaired. 3) When secretagogue-induced IP3 production was reduced by inhibiting phospholipase C with neomycin, secretagogue-induced Ca2+ release was also abolished. 4) When the IP3 breakdown was reduced either by lowering the free Mg2+ concentration of the incubation medium or by adding 2.3-diphosphoglyceric acid, the rise in IP3 and the release of Ca2+ induced by secretagogues were both increased. These results further support the role of IP3 as a second messenger to induce Ca2+ mobilization.

2,3-Diphosphoglycerate↗
PubMed1985

Variation of Ap4A and other dinucleoside polyphosphates in stressed Drosophila cells.

The unusual bis(5'-nucleosidyl)oligophosphates: Ap4A, Ap4G, Ap3A, and Ap3G, have been measured in cultures of Drosophila cells. Exponentially growing cells contain concentrations of 0.25, 0.31, 0.87, and 2.25 microM, respectively. These nucleotides have been followed after stressing the cells either by CdCl2 addition or by heat-shock treatment. Their concentrations are not affected by exposure to 500 microM CdCl2 during 6 h. Beyond this threshold of cadmium concentration, the nucleotides increase. With 5 mM CdCl2, an enhancement by 2 orders of magnitude of all the dinucleoside tri- and tetra-phosphates is observed. Upon heat-shock from 19 to 37 degrees C, Ap4A, Ap3A, and Ap3G increase up to 2.2, 3, and 3.3 times their initial levels, respectively. The increase is achieved within 1 h.

Adenine Nucleotides↗
PubMed1977

Polyphosphate-glucose phosphotransferase. Purification of Mycobacterium tuberculosis H37Ra enzyme to apparent homogeneity.

1. The enzyme (EC 2.7.1.63) was isolated from glucose-grown M. tuberculosis H37Ra; during the purification procedure, 2-mercaptoethanol, glucose, EDTA and NaCl served as protecting agents. 2. The enzyme was purified about 600-fold. The preparation was homogeneous on polyacrylamide-gel electrophoresis and gave one precipitin line in double immunodiffusion test. Molecular weight of the enzyme determined by Sephadex G-100 filtration was about 118 000. 3. The enzyme preparation showed also glucokinase activity with ATP.

Cell-Free System↗