Prostacyclin-lipoprotein interactions. Studies on human platelet aggregation and adenylate cyclase |
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| Authors: | S Colli P Maderna E Tremoli A Baraldi G E Rovati G Gianfranceschi S Nicosia |
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| Affiliation: | 1. Faculty of Pharmacy, University of Sydney, NSW, Australia;2. School of Life Sciences, University of Technology Sydney, NSW, Australia;3. Woolcock Emphysema Centre, Woolcock Institute of Medical Research, University of Sydney, NSW, Australia;1. Institute for Clinical Biochemistry and Pathobiochemistry, University of Wuerzburg, Wuerzburg, Germany;2. Institut für Physik, University of Freiburg, Freiburg, Germany;3. BIOSS Centre for Biological Signalling Studies, University of Freiburg, Freiburg, Germany;4. BioCytex, Marseille, France;5. Center for Thrombosis & Haemostasis, Universitätsklinikum der Johannes Gutenberg‐Universität Mainz, Mainz, Germany;6. Interdisciplinary Bank of Biomaterials and Data Wuerzburg, Straubmuehlweg 2a, 97078 Wuerzburg, Germany;1. Department of Biomedical Laboratory Science, College of Biomedical Science and Engineering, Inje University, Gyungnam, Republic of Korea;2. Department of Biomedical Laboratory Science, College of Medical Science, Konyang University, Daejeon, Republic of Korea;3. Laboratory of Veterinary Physiology and Signaling, College of Veterinary Medicine, Kyungpook National University, Daegu, Republic of Korea;1. Leibniz-Institut für Analytische Wissenschaften–ISAS–e.V., Dortmund, Germany;;2. Institut für Klinische Biochemie und Pathobiochemie, Universitätsklinikum Würzburg, Würzburg, Germany;;3. Sechenov Institute of Evolutionary Physiology and Biochemistry, Russian Academy of Sciences, S. Petersburg, Russia;;4. Center for Bioinformatics, Universität Tübingen, Tübingen, Germany;;5. Institute of Clinical Chemistry, University Medical Center Hamburg–Eppendorf, Hamburg, Germany;;6. Department of Medical Protein Research, Vlaams Instituut voor Biotechnologie, Ghent, Belgium;;7. Department of Biochemistry, Ghent University, Ghent, Belgium;;8. Center for Thrombosis & Hemostasis, Universitätsklinikum der Johannes Gutenberg-Universität Mainz, Mainz, Germany;9. Medizinisches Proteom-Center, Ruhr-Universität, Bochum, Germany;1. Faculty of Biology, M.V. Lomonosov Moscow State University, Leninskie Gory 1-12, 119234, Moscow, Russia;2. Institute for Biomedical Problems, Russian Academy of Sciences, Khoroshevskoe shosse 76A, 123007, Moscow, Russia;3. Department of Physiology, Russian National Research Medical University, Ostrovitianova str. 1, 117997, Moscow, Russia;4. Institute of Experimental Cardiology, Russian Cardiology Research Center, 3rd Cherepkovskaya Street 15a, 121552, Moscow, Russia |
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| Abstract: | The in vitro effects of different lipoprotein fractions (VLDL, LDL and HDL) on human washed platelet aggregation, induced by collagen and thrombin, were evaluated in the presence and absence of PGI2. Although VLDL and LDL increased the platelet aggregation while HDL showed an opposite effect, none of the tested lipoprotein fractions affected the potency of PGI2 as inhibitor of platelet aggregation (IC50). In addition, studies were performed to evaluate the effects of lipoproteins on adenylate cyclase activity in human platelet membranes. The three lipoprotein classes inhibited both basal and PGI2-stimulated adenylate cyclase without affecting the EC50 for PGI2. This inhibitory activity was not specifically elicited by any protein or lipid since neither bovine serum albumin nor a lipid emulsion (Intralipid) displayed any inhibition. The effect on adenylate cyclase elicited by VLDL, LDL and HDL does not seem to be correlated with the activity on platelet aggregation. It is concluded that mediators other than cAMP might be involved in the control of platelet function by lipoproteins. |
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