Evidence that most high-affinity ATP binding sites on aortic endothelial cells and membranes do not correspond to P2 receptors
- 27 June 1996
- journal article
- Published by Elsevier in European Journal of Pharmacology
- Vol. 307 (2) , 201-209
- https://doi.org/10.1016/0014-2999(96)00234-8
Abstract
No abstract availableKeywords
This publication has 24 references indexed in Scilit:
- Evidence that a form of ATP uncomplexed with divalent cations is the ligand of P2y and nucleotide/P2u receptors on aortic endothelial cellsBritish Journal of Pharmacology, 1993
- Heterogeneity of ATP receptors in aortic endothelial cells. Involvement of P2y and P2u receptors in inositol phosphate response.Circulation Research, 1993
- Adenine nucleotide analogues, including γ-phosphate-substituted analogues, are metabolised extracellularly in innervated frog sartorius muscleEuropean Journal of Pharmacology, 1992
- A nucleotide receptor in vascular endothelial cells is specifically activated by the fully ionized forms of ATP and UTPBiochemical Journal, 1992
- Characterization of the purinoceptors present in rabbit and guinea pig liverEuropean Journal of Pharmacology, 1990
- P2 purinoceptors on vascular endotheliai cells: physiological significance and transduction mechanismsTrends in Pharmacological Sciences, 1990
- Characterization of purinoceptors present on human liver plasma membranesFEBS Letters, 1989
- Regulation of P2y‐purinoceptor‐mediated prostacyclin release from human endothelial cells by cytoplasmic calcium concentrationBritish Journal of Pharmacology, 1988
- Characterization of the liver P2-purinoceptor involved in the activation of glycogen phosphorylaseBiochemical Journal, 1986
- Specificity of P2-purinoceptor that mediates endothelium-dependent relaxation of the pig aortaEuropean Journal of Pharmacology, 1985