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An Antithrombotic Strategy by Targeting Phospholipase D in Human Platelets
Phospholipase D (PLD) is involved in many biological processes. PLD1 plays a crucial role in regulating the platelet activity of mice; however, the role of PLD in the platelet activation of humans remains unclear. Therefore, we investigated whether PLD is involved in the platelet activation of human...
Autores principales: | , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2018
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6262437/ https://www.ncbi.nlm.nih.gov/pubmed/30441821 http://dx.doi.org/10.3390/jcm7110440 |
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author | Lu, Wan Jung Chung, Chi Li Chen, Ray Jade Huang, Li Ting Lien, Li Ming Chang, Chao Chien Lin, Kuan Hung Sheu, Joen Rong |
author_facet | Lu, Wan Jung Chung, Chi Li Chen, Ray Jade Huang, Li Ting Lien, Li Ming Chang, Chao Chien Lin, Kuan Hung Sheu, Joen Rong |
author_sort | Lu, Wan Jung |
collection | PubMed |
description | Phospholipase D (PLD) is involved in many biological processes. PLD1 plays a crucial role in regulating the platelet activity of mice; however, the role of PLD in the platelet activation of humans remains unclear. Therefore, we investigated whether PLD is involved in the platelet activation of humans. Our data revealed that inhibition of PLD1 or PLD2 using pharmacological inhibitors effectively inhibits platelet aggregation in humans. However, previous studies have showed that PLD1 or PLD2 deletion did not affect mouse platelet aggregation in vitro, whereas only PLD1 deletion inhibited thrombus formation in vivo. Intriguingly, our data also showed that the pharmacological inhibition of PLD1 or PLD2 does not affect mouse platelet aggregation in vitro, whereas the inhibition of only PLD1 delayed thrombus formation in vivo. These findings indicate that PLD may play differential roles in humans and mice. In humans, PLD inhibition attenuates platelet activation, adhesion, spreading, and clot retraction. For the first time, we demonstrated that PLD1 and PLD2 are essential for platelet activation in humans, and PLD plays different roles in platelet function in humans and mice. Our findings also indicate that targeting PLD may provide a safe and alternative therapeutic approach for preventing thromboembolic disorders. |
format | Online Article Text |
id | pubmed-6262437 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2018 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-62624372018-12-03 An Antithrombotic Strategy by Targeting Phospholipase D in Human Platelets Lu, Wan Jung Chung, Chi Li Chen, Ray Jade Huang, Li Ting Lien, Li Ming Chang, Chao Chien Lin, Kuan Hung Sheu, Joen Rong J Clin Med Article Phospholipase D (PLD) is involved in many biological processes. PLD1 plays a crucial role in regulating the platelet activity of mice; however, the role of PLD in the platelet activation of humans remains unclear. Therefore, we investigated whether PLD is involved in the platelet activation of humans. Our data revealed that inhibition of PLD1 or PLD2 using pharmacological inhibitors effectively inhibits platelet aggregation in humans. However, previous studies have showed that PLD1 or PLD2 deletion did not affect mouse platelet aggregation in vitro, whereas only PLD1 deletion inhibited thrombus formation in vivo. Intriguingly, our data also showed that the pharmacological inhibition of PLD1 or PLD2 does not affect mouse platelet aggregation in vitro, whereas the inhibition of only PLD1 delayed thrombus formation in vivo. These findings indicate that PLD may play differential roles in humans and mice. In humans, PLD inhibition attenuates platelet activation, adhesion, spreading, and clot retraction. For the first time, we demonstrated that PLD1 and PLD2 are essential for platelet activation in humans, and PLD plays different roles in platelet function in humans and mice. Our findings also indicate that targeting PLD may provide a safe and alternative therapeutic approach for preventing thromboembolic disorders. MDPI 2018-11-14 /pmc/articles/PMC6262437/ /pubmed/30441821 http://dx.doi.org/10.3390/jcm7110440 Text en © 2018 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Article Lu, Wan Jung Chung, Chi Li Chen, Ray Jade Huang, Li Ting Lien, Li Ming Chang, Chao Chien Lin, Kuan Hung Sheu, Joen Rong An Antithrombotic Strategy by Targeting Phospholipase D in Human Platelets |
title | An Antithrombotic Strategy by Targeting Phospholipase D in Human Platelets |
title_full | An Antithrombotic Strategy by Targeting Phospholipase D in Human Platelets |
title_fullStr | An Antithrombotic Strategy by Targeting Phospholipase D in Human Platelets |
title_full_unstemmed | An Antithrombotic Strategy by Targeting Phospholipase D in Human Platelets |
title_short | An Antithrombotic Strategy by Targeting Phospholipase D in Human Platelets |
title_sort | antithrombotic strategy by targeting phospholipase d in human platelets |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6262437/ https://www.ncbi.nlm.nih.gov/pubmed/30441821 http://dx.doi.org/10.3390/jcm7110440 |
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