Characterization of ecto-ATPase on human blood cells. A physiological role in platelet aggregation?

@article{Beukers1993CharacterizationOE,
  title={Characterization of ecto-ATPase on human blood cells. A physiological role in platelet aggregation?},
  author={Margot W. Beukers and I. M. Pirovano and Anton W.M. van Weert and Cornel J. M. Kerkhof and Adriaan P. IJzerman and Willem Soudijn},
  journal={Biochemical pharmacology},
  year={1993},
  volume={46 11},
  pages={
          1959-66
        }
}
Ecto-ATPase (EC 3.6.1.15) is a plasma membrane-bound enzyme which degrades extracellular triphosphate nucleotides. Although its physiological function is still unclear, the enzyme obscures the study of P2 purinoceptors (i.e. receptors for ATP and other di- and triphosphate nucleotides), since it is capable of metabolizing the pharmacological ligands, such as ATP, for these receptors. We characterized the ecto-ATPase activity on human blood cells with a [gamma 32P]ATP assay and HPLC measurements… CONTINUE READING

Citations

Publications citing this paper.
SHOWING 1-10 OF 12 CITATIONS

Soluble purine-converting enzymes circulate in human blood and regulate extracellular ATP level via counteracting pyrophosphatase and phosphotransfer reactions.

  • FASEB journal : official publication of the Federation of American Societies for Experimental Biology
  • 2003
VIEW 7 EXCERPTS
CITES BACKGROUND
HIGHLY INFLUENCED

Disorders of Platelet Function Abnormalities of the Platelet P2 Receptors

  • Pathophysiology of Haemostasis and Thrombosis
  • 2006
VIEW 1 EXCERPT
CITES BACKGROUND