https://doi.org/10.4081/btvb.2023.51
Interaction between adenosine diphosphate receptors and protein-kinase C isoforms in platelet adhesion under flow condition
Submitted: 24 August 2022
Accepted: 18 January 2023
Published: 16 February 2023
Accepted: 18 January 2023
Abstract Views: 1181
pdf: 174
Publisher's note
All claims expressed in this article are solely those of the authors and do not necessarily represent those of their affiliated organizations, or those of the publisher, the editors and the reviewers. Any product that may be evaluated in this article or claim that may be made by its manufacturer is not guaranteed or endorsed by the publisher.
All claims expressed in this article are solely those of the authors and do not necessarily represent those of their affiliated organizations, or those of the publisher, the editors and the reviewers. Any product that may be evaluated in this article or claim that may be made by its manufacturer is not guaranteed or endorsed by the publisher.
Authors
Adenosine diphosphate (ADP) receptors and protein-kinase C (PKC) isoforms play different role in platelet activity. In the present study, whole blood platelet adhesion at 200 - 1800 s-1 shear rates was investigated by Impact-R system, measuring percent of surface coverage (SC) by platelets. Gradual heightened shear rate par-alleled increase of platelet adhesion. At relatively low shear (200 and 1000 s-1) blockade of neither P2Y1 receptor nor P2Y12 receptor (by A2P5P and 2MeSAMP, respectively) affected SC. At high shear rate (1800 s-1) reduction of SC was observed by 2MeSAMP. Treatment of blood with PKCδ inhibitor (rottlerin) but not PKCα,β inhibitor (Gö6976) diminished platelet adhe-sion. Among all the agents, only combination of 2MeSAMP and rottlerin used at subthreshold concentrations was able to inhibit platelet adhesion under high shear condition. We suggest that platelet agonist-induced P2Y12 and PKCδ signaling essentially stimulates platelet adhesion under flow condition, the important initiating step of thrombin formation.
Burnstock G. Blood cells an historical account of the roles of purinergic signaling. Purinergic Signal 2015:11;411-4.
DOI: https://doi.org/10.1007/s11302-015-9462-7
Yanachkov IB, Chang H, Yanachkova MI, et al. New highly active antiplatelet agents with dual specificity for platelet P2Y1 and P2Y12 adenosine diphosphate receptors. Europ J Med Chem 2016;107:204-8.
DOI: https://doi.org/10.1016/j.ejmech.2015.10.055
Hechler B, Léon C, Vial C, et al. The P2Y1 receptor is neces-sary for adenosine 5′-diphosphate-induced platelet aggrega-tion. Blood 1998;92:152-9.
DOI: https://doi.org/10.1182/blood.V92.1.152.413k27_152_159
Kunapuli SP, Dorsam RT, Kim S, et al. Platelet purinergic re-ceptors. Curr Opin Pharmacol 2003;3:175–80.
DOI: https://doi.org/10.1016/S1471-4892(03)00007-9
Oliphant CS, Doby J B, Blade CL, et al. Emerging P2Y12 re-ceptor antagonists: role in coronary artery disease. Curr Vasc Pharmacol 2010;8:93-101.
DOI: https://doi.org/10.2174/157016110790226615
Machal J, Hinomaz O. Efficacy of P2Y12 receptor blockers after myocardial infarction and genetic variability of their metabolic pathways. Curr Vasc Pharmacol 2019;17:35-40.
DOI: https://doi.org/10.2174/1570161116666180206110657
Mellor H, Parker PJ. The extented protein kinase C superfam-ily. Biochem J 1998;332;281-92.
DOI: https://doi.org/10.1042/bj3320281
Harper MT, Poole AW. Diverse functions of protein kinase C isoforms in platelet activation and thrombus formation. J Thromb Haemost 2010;8:454-62.
DOI: https://doi.org/10.1111/j.1538-7836.2009.03722.x
Unsworth AJ, Smith H, Gissen P, et al. Submaximal inhibition of protein kinase C restores ADP-induced dense granule se-cretion in platelets in the presence of Ca2+. J Biol Chem 2011;286:21073-82.
DOI: https://doi.org/10.1074/jbc.M110.187138
Mundell SJ, Jones ML, Hardy AR, et al. Distinct roles for pro-tein kinase C isoforms in regulating platelet purinergic recep-tor function. Mol Pharmacol 2006;70:1132-42.
DOI: https://doi.org/10.1124/mol.106.023549
Xiang B, Zhang G, Ren H, et al. The P2Y(12) antagonists, 2MeSAMP and cangrelor, inhibit platelet activation through P2Y(12)/G(i)-dependent mechanism. PLoS One 2012;7; e51037.
DOI: https://doi.org/10.1371/journal.pone.0051037
Koivunen J, Aaltonen V, Koskela S, et al. Protein kinase C alpha/beta inhibitor Go6976 promotes formation of cell junc-tions and inhibitors invasion of urinary bladder carcinoma cells. Cancer Res 2005;64:5693-701.
DOI: https://doi.org/10.1158/0008-5472.CAN-03-3511
Bong KA, Se KJ, Hee SK, et al. Rottlerin, a specific inhibitor of protein kinase C-delta, impedes barrier repair response by increasing intracellular free calcium. J Invest Dermatol 2006;126:1348-55.
DOI: https://doi.org/10.1038/sj.jid.5700244
Lee TH, Chen JL, Liu PS, et al. Rottlerin, a natural polyphenol compound, inhibits upregulation of matrix metalloproteinase-9 and brain astrocytic migration by reducing PKC-δ-depen-dent ROS signal. J Neuroinflammation 2020;17:177.
DOI: https://doi.org/10.1186/s12974-020-01859-5
Pham VT, Joo JE, YS, et al. A concise synthesis of a promis-ing protein kinase C inhibitor: D-erythro-sphingosine. Arch Pharmacol Res 2007;30:22-7.
DOI: https://doi.org/10.1007/BF02977774
Shenkman B, Einav Y, Salomon O, et al. Testing agonist-in-duced platelet aggregation by the Impact-R [Cone and Plate(let) analyzer (CPA)]. Platelet 2008;19:440-6.
DOI: https://doi.org/10.1080/09537100802082256
Zhang M, Wu Y, Hauch K, Horbett TA. Fibrinogen and von Willebrand factor mediated platelet adhesion to polystyrene under flow conditions. J Biomater Sci Polym 2008;19: 1383-410.
DOI: https://doi.org/10.1163/156856208786052353
Ramstrom S, Ranby M, Lindahl TL. Effects of P2Y(1) and P2Y(12) on whole blood clotting, coagulum elasticity and fib-rinolysis resistance studied with free oscillation rheometry. Thromb Res 2003;109:315-22.
DOI: https://doi.org/10.1016/S0049-3848(03)00254-8
Turner NA, Moake JL, McIntire LV. Blockade of adenosine diphosphate receptors P2Y12 and P2Y1 is required to inhibit platelet aggregation in whole blood under flow. Blood 2001;98:3340-5.
DOI: https://doi.org/10.1182/blood.V98.12.3340
Yacoub D, Theoret JF, Villneuve L, et al. Essential role of pro-tein kinase C delta in platelet signaling, alpha IIB beta 3 acti-vation, and thromboxane A2 release. J Biol Chem 2006;281: 30024-35.
DOI: https://doi.org/10.1074/jbc.M604504200
How to Cite
Shenkman, B., Budnik, I., & Einav, Y. (2023). Interaction between adenosine diphosphate receptors and protein-kinase C isoforms in platelet adhesion under flow condition . Bleeding, Thrombosis and Vascular Biology, 2(1). https://doi.org/10.4081/btvb.2023.51
Copyright (c) 2023 The Author(s)
This work is licensed under a Creative Commons Attribution-NonCommercial 4.0 International License.
PAGEPress has chosen to apply the Creative Commons Attribution NonCommercial 4.0 International License (CC BY-NC 4.0) to all manuscripts to be published.
Similar Articles
- Loredana Bury, Paolo Gresele, The amazing genetic complexity of anucleated platelets , Bleeding, Thrombosis and Vascular Biology: Vol. 1 No. 2 (2022)
- Yishi Tan, Marc Carrier, Nicola Curry, Michael Desborough, Kathryn Musgrave, Marie Scully, Tzu-Fei Wang, Mari Thomas, Simon J. Stanworth, Cancer complicated by thrombosis and thrombocytopenia: still a therapeutic dilemma , Bleeding, Thrombosis and Vascular Biology: Vol. 3 No. s1 (2024): 12th ICTHIC
- Luca Barcella, Chiara Ambaglio, Paolo Gritti, Francesca Schieppati, Varusca Brusegan, Eleonora Sanga, Marina Marchetti, Luca Lorini, Anna Falanga, Long-term persistence of high anti-PF4 antibodies titer in a challenging case of AZD1222 vaccine-induced thrombotic thrombocytopenia , Bleeding, Thrombosis and Vascular Biology: Vol. 2 No. 2 (2023)
- Ilaria Canobbio, Silvia Stella Barbieri, Are platelets more than a model of brain neurons? , Bleeding, Thrombosis and Vascular Biology: Vol. 1 No. 1 (2022)
- Betül Ünlü, Neha Joshi, Jamie M. O'Sullivan, Endothelial cell dysfunction in cancer: a not-so-innocent bystander , Bleeding, Thrombosis and Vascular Biology: Vol. 3 No. s1 (2024): 12th ICTHIC
- Luca Puccetti, Vincenzo Sammartano, Federico Caroni, Margherita Malchiodi, Paola Calzoni, Eleonora Franceschini, Lucrezia Galasso, Monica Bocchia, Safety of COVID-19 mRNA vaccination in patients with history of acquired hemophilia A: a case series , Bleeding, Thrombosis and Vascular Biology: Vol. 1 No. 3 (2022)
- Marco Cattaneo, Guided antiplatelet therapy in patients undergoing percutaneous coronary intervention , Bleeding, Thrombosis and Vascular Biology: Vol. 2 No. 2 (2023)
- Federica Azzolini, Antonio Bruno, Ettore Dolcetti, Diego Centonze, Fabio Buttari, Tumor necrosis factor superfamily in multiple sclerosis: from pathology to therapeutic implications , Bleeding, Thrombosis and Vascular Biology: Vol. 2 No. 2 (2023)
- Giovanni L. Tiscia, Donatella Colaizzo, Antonio De Laurenzo, Filomena Cappucci, Lucia Fischetti, Elena Chinni, Mario Mastroianno, Giovanni Favuzzi, Massimo Carella, Elvira Grandone, Thrombin generation assay in COVID-19 patients shows a hypocoagulable pattern , Bleeding, Thrombosis and Vascular Biology: Vol. 3 No. 3 (2024)
You may also start an advanced similarity search for this article.
