Desensitization of platelets to iloprost. Loss of specific binding sites and heterologous desensitization of adenylate cyclase
- 1 March 1988
- journal article
- research article
- Published by Elsevier in European Journal of Pharmacology
- Vol. 147 (2) , 187-196
- https://doi.org/10.1016/0014-2999(88)90777-7
Abstract
No abstract availableThis publication has 41 references indexed in Scilit:
- Prostacyclin analogues reduce ADP‐ribosylation of the α‐subunit of the regulatory Gs‐protein and diminish adenosine (A2) responsiveness of plateletsBritish Journal of Pharmacology, 1987
- Dual regulation of adenylate cyclase. A signal transduction mechanism of membrane receptorsBasic Research in Cardiology, 1986
- Desensitization of prostacyclin responsiveness in a neuronal hybrid cell line: selective loss of high affinity receptorsBritish Journal of Pharmacology, 1985
- The use of a prostacyclin analogue, [3H]iloprost, for studying prostacyclin-binding sites on human platelets and neuronal hybrid cellsBioscience Reports, 1984
- Guanine nucleotide-binding regulatory proteins and dual control of adenylate cyclase.Journal of Clinical Investigation, 1984
- The cytoplasmic concentration of free calcium in platelets is controlled by stimulators of cyclic AMP production (PGD2, PGE1, forskolin)Biochemical and Biophysical Research Communications, 1983
- Phosphatidylinositol-specific phospholipase-C of platelets: Association with 1,2-diacylglycerol-kinase and inhibition by cyclic-AMPBiochemical and Biophysical Research Communications, 1979
- Cyclic adenosine 3′,5′-monophosphate and prostacyclin inhibit membrane phospholipase activity in plateletsBiochemical and Biophysical Research Communications, 1977
- Modulation of human platelet adenylate cyclase by prostacyclin (PGX)Prostaglandins, 1977
- Activation and dissociation of adenosine 3′,5′-monophosphate-dependent and guanosine 3′,5′-monophosphate-dependent protein kinases by various cyclic nucleotide analogsBiochemical Pharmacology, 1974