Inhibitory action of cyclic GMP on secretion, polyphosphoinositide hydrolysis and calcium mobilization in thrombin-stimulated human platelets |
| |
| Authors: | S Nakashima T Tohmatsu H Hattori Y Okano Y Nozawa |
| |
| Affiliation: | 1. The Cardeza Foundation for Hematologic Research and the Department of Medicine, Thomas Jefferson University, Jefferson Medical College, Philadelphia, PA, USA;2. Department of Human & Molecular Genetics, Baylor College of Medicine, Houston, TX, USA;3. Department of Pharmacology, Case Western Reserve University, Cleveland, OH, USA;4. Program in Molecular Medicine and the Division of Hematology and Hematologic Malignancies, Department of Internal Medicine, University of Utah, Salt Lake City, UT, USA;5. Department of Pharmacology, University of Michigan, Ann Arbor, MI, USA;6. Department of Statistics, Rice University, Houston, TX, USA;1. Faculty of Physics, Lomonosov Moscow State University, 1-2 Leninskie Gory, GSP-1, Moscow 119991, Rusia;2. Federal Research and Clinical Center of Pediatric Hematology, Oncology and Immunology, 1 Samory Mashela St, Moscow 117198, Russia;3. Center for Theoretical Problems of Physicochemical Pharmacology, Russian Academy of Sciences, 4 Kosygina St, Moscow 119991, Russia;4. Faculty of Biological and Medical Physics, Moscow Institute of Physics and Technology, 9 Institutskii per., Dolgoprudnyi, 141700, Russia;1. Department of Chemical and Biomolecular Engineering, Institute for Medicine and Engineering, University of Pennsylvania, Philadelphia, PA, USA |
| |
| Abstract: | The effect of cyclic GMP (cGMP) on human platelet activation was investigated, using its metabolically stable analogue, 8-bromo cGMP (8-bcGMP). Thrombin-induced serotonin secretion was inhibited by pretreatment with 8bcGMP in a dose-dependent manner. Production of inositol trisphosphate (IP3), a Ca2+ releaser was inhibited by 8bcGMP pretreatment of platelets. Preincubation of platelets with 8bcGMP was without effect on the basal level of cytosolic free Ca2+, measured by fluorescent indicator quin2, but suppressed its thrombin-induced enhancement independently of extracellular Ca2+. These results indicate that cGMP may be implicated in phospholipase C activation and Ca2+ mobilization (both influx through the plasma membrane and efflux from internal stores) in thrombin-activated human platelets. |
| |
| Keywords: | |
| 本文献已被 ScienceDirect 等数据库收录！ |
|
