RSS-Feed abonnieren
DOI: 10.1055/s-0038-1657875
Highly Efficient Induction of Human Platelet Aggregation in Heparinized Platelet-Rich Plasma by Diadenosine Triphosphate (Ap3A)
Publikationsverlauf
Received 27. Dezember 1984
Accepted 17. Mai 1985
Publikationsdatum:
18. Juli 2018 (online)
![](https://www.thieme-connect.de/media/10.1055-s-00035024/198502/lookinside/thumbnails/10-1055-s-0038-1657875-1.jpg)
Summary
Diadenosine triphosphate (Ap3A), which is a releasable dinucleotide of human platelets, induces platelet aggregation when added to heparinized platelet-rich plasma. The concentration dependence of the dinucleotide is similar to ADP. This finding is fully compatible with our recent report of the low potency of Ap3A in citrated platelet-rich plasma relative to ADP.
The aggregatory effect of Ap3A in heparinized versus citrated plasma is reflected in the corresponding rates of Ap3A degradation. In citrated plasma, the hydrolysis of Ap3A is drastically slowed down because the hydrolase needs divalent metal ions. The results strongly support the assumption that the aggregatory effect of Ap3A is mediated by the enzymatic hydrolysis of Ap3A which generates ADP as the ultimate stimulus.
-
References
- 1 Flodgaard H, Klenow H. Abundant amounts of diadenosine 5′,5′″-P1,P4-tetraphospahte are present and releasable, but metabolically inactive, in human platelets. Biochem J 1982; 208: 737-742
- 2 Lüthje J, Ogilvie A. The presence of diadenosine 5′,5′″-P1,P3-triphosphate (Ap3A) in human platelets. Biochem Biophys Res Commun 1983; 115: 253-260
- 3 Lüthje J, Ogilvie A. Diadenosine triphosphate (Ap3A) mediates human platelet aggregation by liberation of ADP. Biochem Biophys Res Commun 1984; 118: 704-709
- 4 Harrison MJ, Brossmer R, Goody RS. Inhibition of platelet aggregation and the platelet release reaction by α, ω diadenosine polyphosphates. FEBS Letters 1975; 54: 57-60
- 5 Lüthje J, Ogilvie A. Isolation and partial characterization of diadenosine triphosphatase from human plasma – a potential factor of hemostasis. Hoppe-Seyler’s Z Physiol Chem 1984; 365: 1028-1029
- 6 Lüthje J, Ogilvie A. Catabolism of Ap3A and Ap4A in Human Plasma: Purification and Characterization of a Glycoprotein Complex with 5’-Nucleotide Phosphodiesterase Activity. Eur J Biochem; 1985; 149: 119-127
- 7 Ogilvie A, Jakob P. Diadenosine 5′,5′″-P1, p3-triphosphate in eukaryotic cells: identification and quantitation. Anal Biochem 1983; 134: 382-392
- 8 Born GVR. Aggregation of blood platelets by adenosine diphosphate and its reversal. Nature 1962; 194: 927-929
- 9 O’Brien JR, Shoobridge SM, Finch WJ. Comparison of the effect of heparin and citrate on platelet aggregation. J Clin Pathol 1969; 22: 28-31
- 10 Zucker MB. Heparin and platelet function. Fed Proc 1977; 36: 47-50
- 11 Reches A, Eldor A, Salomon Y. Heparin inhibits PGE1-sensitive adenylate cyclase and antagonizes PGE1 antiaggregating effect in human platelets. J Lab Clin Med 1979; 93: 638-644
- 12 Bjoraker DG, Ketcham TR. Hemodynamic and platelet response to the bolus intravenous administration of porcine heparin. Thromb Haemostas 1983; 49: 1-4
- 13 Ruggiero M, Fedi S, Bianchini P, Vannucchi S, Chiarugi V. Molecular events involved in the proaggregating effect of heparin on human platelets. Biochim Biophys Acta 1984; 802: 372-377
- 14 Woodward SC, Worthylake KM, Linker A, Mohammad SF. Potentiation of platelet aggregation by heparin is independent of anticoagulant activity. Thromb Haemostas 1983; 50: 126 (Abstr)
- 15 Newhouse P, Clark C. The variability of platelet aggregation. In: Triplett DA. (ed). Platelet function; laboratory evaluation and clinical application. 82 87 American Society of Clinical Pathologists Chicago; 1978