Diadenosine Pentaphosphate

2007 ◽  
pp. 1-5
Author(s):  
Charles Kennedy
Keyword(s):  
Diadenosine Pentaphosphate

scholarly journals Endogenous Diadenosine Tetraphosphate, Diadenosine Pentaphosphate, and Diadenosine Hexaphosphate in Human Myocardial Tissue

Hypertension ◽  
2004 ◽  
Vol 43 (5) ◽  
pp. 1055-1059 ◽  
Author(s):  
Jiankai Luo ◽  
Vera Jankowski ◽  
Nihayrt Güngär ◽  
Joachim Neumann ◽  
Wilhelm Schmitz ◽  
...  
Keyword(s):  
Myocardial Tissue ◽  
Diadenosine Tetraphosphate ◽  
Diadenosine Pentaphosphate

Cathodal bands in electrophoretograms of creatine kinase isoenzymes in serum collected after cardiac surgery: a poor prognostic sign.

1983 ◽  
Vol 29 (10) ◽  
pp. 1727-1730 ◽  
Author(s):  
A A Keshgegian ◽  
B L Marchant
Keyword(s):  
Creatine Kinase ◽  
Cardiac Surgery ◽  
Adenylate Kinase ◽  
Poor Prognosis ◽  
Postoperative Mortality ◽  
Serum Lactate ◽  
Serum Lactate Dehydrogenase ◽  
Diadenosine Pentaphosphate ◽  
Postoperative Serum ◽  
Very High

Abstract Of 708 patients who had undergone cardiac surgery, the serum of 23 showed one or two enzyme bands cathodal to CK-MM in creatine kinase (CK) isoenzyme electrophoretograms. Postoperative mortality rate during hospitalization was: no bands, 8.8%; one band, 13%, two bands, 63% (p less than 0.001). Patients whose sera showed cathodal bands were slightly older than those without, and their postoperative serum lactate dehydrogenase (LD) activity was greater, with very high proportions of LD 5. The two cathodal bands in patients who died differed in cathodal electrophoretic mobility from the two bands in survivors, implying that different enzyme forms were involved. All cathodal bands were inhibited by reagent containing diadenosine pentaphosphate, as was adenylate kinase from erythrocytes and liver cytoplasm. Mitochondrial CK from liver and presumed mitochondrial CK in serum from a patient with malignancy were not inhibited. We conclude that the appearance of two enzyme bands cathodal to CK-MM, probably representing adenylate kinase and possibly originating from various tissues, is associated with a poor prognosis in patients after cardiac surgery.

Potentiation of adenosine 5′-triphosphate calcium responses by diadenosine pentaphosphate in individual rat cerebellar astrocytes

1998 ◽  
Vol 246 (2) ◽  
pp. 109-111 ◽  
Author(s):  
Ana I Jiménez ◽  
Enrique Castro ◽  
Esmerilda G Delicado ◽  
M.Teresa Miras-Portugal
Keyword(s):  
Diadenosine Pentaphosphate ◽  
Cerebellar Astrocytes

Creatine kinase in serum: 2. Interference of adenylate kinase with the assay.

1976 ◽  
Vol 22 (11) ◽  
pp. 1806-1811 ◽  
Author(s):  
G Szasz ◽  
W Gerhardt ◽  
W Gruber ◽  
E Bernt
Keyword(s):  
Creatine Kinase ◽  
Adenylate Kinase ◽  
Kinase Activity ◽  
Kinase Inhibitor ◽  
Hepatic Damage ◽  
Complete Inhibition ◽  
Kinase Assay ◽  
Competitive Inhibitors ◽  
Diadenosine Pentaphosphate ◽  
Adenylate Kinases

Abstract Interference of adenylate kinase with Oliver's method [Biochem. J. 61, 116 (1955)] for creatine kinase is usually suppressed by including an adenylate kinase inhibitor, AMP. We studied the kinetics and compared the inhibition capacities of AMP and diadenosine pentaphosphate. Both are competitive inhibitors, AMP being markedly weaker, with a Ki of about 300 mumol/liter for adenylate kinase from erythrocyte, muscle, and liver. AMP also weakly inhibitis creatine kinase. Diadenosine pentaphosphate inhibits erythrocyte and muscle adenylate kinase strongly (Ki about 0.03 mumol/liter), the liver isoenzyme less strongly (Ki about 3 mumol/liter), and has no effect on creatine kinase up to 100 mumol/liter. All three adenylate kinases may be present in a patinet's serum, causing sample blanks to be high in a creatine kinase assay that lacks inhibitors. In acute hepatic damage, liver adenylate kinase activity in serum can be grossly increased. Use of sufficient diadenosine pentaphosphate alone for complete inhibition is relatively expensive. Consequently, we recommend a combination of both inhibitors. Diadenosine pentaphosphate, 10 mumol, combined with 5 mmol of AMP per liter inhibits adenylate kinase from erythrocytes and muscle by 97% and from liver by 95%.

scholarly journals Specific diadenosine pentaphosphate receptor coupled to extracellular regulated kinases in cerebellar astrocytes

2002 ◽  
Vol 83 (2) ◽  
pp. 299-308 ◽  
Author(s):  
Ana I. Jiménez ◽  
Enrique Castro ◽  
Esmerilda G. Delicado ◽  
M. Teresa Miras-Portugal
Keyword(s):  
Diadenosine Pentaphosphate ◽  
Cerebellar Astrocytes

scholarly journals The pnhA Gene of Pasteurella multocida Encodes a Dinucleoside Oligophosphate Pyrophosphatase Member of the Nudix Hydrolase Superfamily

2005 ◽  
Vol 187 (16) ◽  
pp. 5809-5817 ◽  
Author(s):  
Tonia Urick ◽  
Chien I-Chang ◽  
Ellen Arena ◽  
WenLian Xu ◽  
Maurice J. Bessman ◽  
...  
Keyword(s):  
Type Strain ◽  
Pasteurella Multocida ◽  
Wild Type Strain ◽  
Divalent Metal ◽  
Nudix Hydrolase ◽  
Alkaline Ph ◽  
Wild Type ◽  
Optimal Activity ◽  
Diadenosine Pentaphosphate ◽  
Hydrolysis Of

ABSTRACT The pnhA gene of Pasteurella multocida encodes PnhA, which is a member of the Nudix hydrolase subfamily of dinucleoside oligophosphate pyrophosphatases. PnhA hydrolyzes diadenosine tetra-, penta-, and hexaphosphates with a preference for diadenosine pentaphosphate, from which it forms ATP and ADP. PnhA requires a divalent metal cation, Mg2+ or Mn2+, and prefers an alkaline pH of 8 for optimal activity. A P. multocida strain that lacked a functional pnhA gene, ACP13, was constructed to further characterize the function of PnhA. The cellular size of ACP13 was found to be 60% less than that of wild-type P. multocida, but the growth rate of ACP13 and its sensitivity to heat shock conditions were similar to those of the wild type, and the wild-type cell size was restored in the presence of a functional pnhA gene. Wild-type and ACP13 strains were tested for virulence by using the chicken embryo lethality model, and ACP13 was found to be up to 1,000-fold less virulent than the wild-type strain. This is the first study to use an animal model in assessing the virulence of a bacterial strain that lacked a dinucleoside oligophosphate pyrophosphatase and suggests that the pyrophosphatase PnhA, catalyzing the hydrolysis of diadenosine pentaphosphates, may also play a role in facilitating P. multocida pathogenicity in the host.

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