Diadenosine 5′,5′′′-P1,P4-tetraphosphate (Ap4A), ATP and catecholamine content in bovine adrenal medulla, chromaffin granules and chromaffin cells

Sillero, Marı́a A. Günther; Valle, Mercedes del; Zaera, E.; Michelena, Pedro; Garcı́a, Antonio G.; Sillero, Antonio

doi:10.1016/0300-9084(94)90116-3

Cited by 31 publications

(9 citation statements)

References 26 publications

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“…Diadenosine polyphosphates (Ap n A; where n =3, 4, 5 or 6) have been identified in a wide variety of cells [1]. In mammalian cells they account for a significant proportion of the nucleotide content of a variety of storage granules including dense granules of platelets [2], secretory granules of chromaffin cells [3] and neuronal synaptic vesicles [4]. Liberation into the extracellular environment allows diadenosine polyphosphates to exert effects on a diverse range of target cells [5].…”

Section: Introductionmentioning

confidence: 99%

Diadenosine polyphosphates and the control of cyclic AMP concentrations in isolated rat liver cells

1999

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Extracellular diadenosine polyphosphates (Ap n A), through their interactions with appropriate P 2 receptors, influence a diverse range of intracellular activities. In particular, Ap 4 A stimulates alterations in intracellular calcium homeostasis and subsequent activation of glycogen breakdown in isolated liver cells. Here we show that, like ATP, Ap 4 A and other naturally occurring diadenosine polyphosphates attenuate glucagon-stimulated accumulation of cyclic AMP in isolated rat liver cells. The characteristics of Ap 4 A-and ATP-dependent modulation of glucagon-stimulated cyclic AMP accumulation are similar. These results are discussed in the context of the repertoire of intracellular signalling processes modulated by extracellular nucleotides.z 1999 Federation of European Biochemical Societies.

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Section: Introductionmentioning

confidence: 99%

Diadenosine polyphosphates and the control of cyclic AMP concentrations in isolated rat liver cells

1999

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“…Adenine nucleotides are released into the extracellular environment after discharge of a variety of storage granules. A significant proportion of the nucleotide content of dense granules of platelets [3], secretory granules of chromaffin cells [4] and neuronal synaptic granules [5] is in the form of diadenosine polyphosphates (Ap n A; where n l 3, 4, 5, 6). Although Ap % A and Ap $ A are the best characterized of the diadenosine polyphosphates, all of these unusual compounds appear to exert a wide range of effects on a variety of tissues [6,7].…”

Section: Introductionmentioning

confidence: 99%

Diadenosine polyphosphate-stimulated gluconeogenesis in isolated rat proximal tubules

Edgecombe

Craddock

Smith

et al. 1997

Biochemical Journal

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Diadenosine polyphosphates released into the extracellular environment influence a variety of metabolic and other cellular activities in a wide range of target tissues. Here we have studied the impact of these novel nucleotides on gluconeogenesis in isolated rat proximal tubules. Gluconeogenesis was stimulated following exposure of isolated proximal tubules to a range of adenine-containing nucleotides including ADP, ATP, Ap3A, Ap4A, Ap5A and Ap6A. The concentration-dependence of ATP-, Ap3A- and Ap4A-mediated stimulation of gluconeogenesis was similar and was consistent with a role for these agents in the physiological control of renal metabolism. Nucleotide-stimulated gluconeogenesis was diminished in the presence of agents that interfere with phospholipase C activation or intracellular Ca2+ metabolism, indicative of a role for polyphosphoinositide-mediated Ca2+ mobilization in the mechanism of action of ATP, Ap3A and Ap4A. The characteristics of binding of [2-3H]Ap4A to renal plasma-membrane preparations suggest that Ap4A mediates its effects on proximal tubule gluconeogenesis via interaction with P2y-like purinoceptor(s) also recognized by extracellular ATP.

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“…Cells contain several rare adenine nucleotides in addition to AMP, ADP and ATP. Foremost among them are the diadenosine polyphosphates : diadenosine 5h,5e-P",P$-triphosphate (Ap $ A), diadenosine 5h,5e-P",P%-tetraphosphate (Ap % A) [1], Ap & A and Ap ' A [2][3][4], as well as adenosine 5h-tetraphosphate (p % A) and adenosine 5h-pentaphosphate (p & A) [5][6][7][8], which have been studied less extensively. There is no information on the occurrence and biological role of p % A and p & A in plants.…”

Section: Introductionmentioning

confidence: 99%

“…There is no information on the occurrence and biological role of p % A and p & A in plants. In animal tissues, the concentration of p % A (2 µM) is three to four orders of magnitude lower than that of ATP [5,7]. In sporulating yeast cultures, p % A and p & A constitute 2 % and 1.5 % respectively of the ATP content, whereas in vegetatively growing cells or early during sporulation the content of those nucleotides is less than 0.1 % that of ATP [6].…”

Section: Introductionmentioning

confidence: 99%

Adenosine 5′-tetraphosphate phosphohydrolase from yellow lupin seeds: purification to homogeneity and some properties

Guranowski

Starzyńska

Brown

et al. 1997

Biochemical Journal

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Adenosine 5'-tetraphosphate phosphohydrolase (EC 3.6.1.14) has been purified to homogeneity from the meal of yellow lupin (Lupinus luteus) seeds. The enzyme is a single polypeptide chain of 25+/-1 kDa. It catalyses the hydrolysis of a nucleoside 5'-tetraphosphate to a nucleoside triphosphate and orthophosphate, and hydrolysis of tripolyphosphate but neither pyrophosphate nor tetraphosphate. A divalent cation, Mg2+, Co2+, Ni2+ or Mn2+, is required for these reactions. The pH optimum for hydrolysis of adenosine 5'-tetraphosphate (p4A) is 8.2, Vmax is 21+/-1.7 micromol/min per mg of protein and the Km for p4A is 3+/-0.6 microM. At saturating p4A concentrations, the rate constant for the reaction is 8.5+/-0.7 s-1 [at 30 degrees C, in 50 mM Hepes/KOH (pH8.2)/5 mM MgCl2/0.1 mM dithiothreitol]. p4A and guanosine 5'-tetraphosphate are hydrolysed at the same rate. Adenosine 5'-pentaphosphate (p5A) is degraded 1/200 as fast and is converted into ATP and two molecules of orthophosphate, which are liberated sequentially. This contrasts with the cleavage of p5A by the lupin diadenosine tetraphosphate hydrolase (EC 3.6.1.17), which gives ATP and pyrophosphate. Zn2+, F- and Ca2+ ions inhibit the hydrolysis of p4A with I50 values of 0.1, 0.12 and 0.2 mM respectively.

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Diadenosine 5′,5′′′-P1,P4-tetraphosphate (Ap4A), ATP and catecholamine content in bovine adrenal medulla, chromaffin granules and chromaffin cells

Cited by 31 publications

References 26 publications

Diadenosine polyphosphates and the control of cyclic AMP concentrations in isolated rat liver cells

Diadenosine polyphosphates and the control of cyclic AMP concentrations in isolated rat liver cells

Diadenosine polyphosphate-stimulated gluconeogenesis in isolated rat proximal tubules

Adenosine 5′-tetraphosphate phosphohydrolase from yellow lupin seeds: purification to homogeneity and some properties

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