Cargando…
Loss of ATP Diphosphohydrolase Activity with Endothelial Cell Activation
Quiescent endothelial cells (EC) regulate blood flow and prevent intravascular thrombosis. This latter effect is mediated in a number of ways, including expression by EC of thrombomodulin and heparan sulfate, both of which are lost from the EC surface as part of the activation response to proinflamm...
Autores principales: | , , , , , , , |
---|---|
Formato: | Texto |
Lenguaje: | English |
Publicado: |
The Rockefeller University Press
1997
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2196106/ https://www.ncbi.nlm.nih.gov/pubmed/8996251 |
_version_ | 1782147998110711808 |
---|---|
author | Robson, Simon C. Kaczmarek, Elzbieta Siegel, Jonathan B. Candinas, Daniel Koziak, Katarzyna Millan, Maria Hancock, Wayne W. Bach, Fritz H. |
author_facet | Robson, Simon C. Kaczmarek, Elzbieta Siegel, Jonathan B. Candinas, Daniel Koziak, Katarzyna Millan, Maria Hancock, Wayne W. Bach, Fritz H. |
author_sort | Robson, Simon C. |
collection | PubMed |
description | Quiescent endothelial cells (EC) regulate blood flow and prevent intravascular thrombosis. This latter effect is mediated in a number of ways, including expression by EC of thrombomodulin and heparan sulfate, both of which are lost from the EC surface as part of the activation response to proinflammatory cytokines. Loss of these anticoagulant molecules potentiates the procoagulant properties of the injured vasculature. An additional thromboregulatory factor, ATP diphosphohydrolase (ATPDase; designated as EC 3.6.1.5) is also expressed by quiescent EC, and has the capacity to degrade the extracellular inflammatory mediators ATP and ADP to AMP, thereby inhibiting platelet activation and modulating vascular thrombosis. We describe here that the antithrombotic effects of the ATPDase, like heparan sulfate and thrombomodulin, are lost after EC activation, both in vitro and in vivo. Because platelet activation and aggregation are important components of the hemostatic changes that accompany inflammatory diseases, we suggest that the loss of vascular ATPDase may be crucial for the progression of vascular injury. |
format | Text |
id | pubmed-2196106 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 1997 |
publisher | The Rockefeller University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-21961062008-04-16 Loss of ATP Diphosphohydrolase Activity with Endothelial Cell Activation Robson, Simon C. Kaczmarek, Elzbieta Siegel, Jonathan B. Candinas, Daniel Koziak, Katarzyna Millan, Maria Hancock, Wayne W. Bach, Fritz H. J Exp Med Article Quiescent endothelial cells (EC) regulate blood flow and prevent intravascular thrombosis. This latter effect is mediated in a number of ways, including expression by EC of thrombomodulin and heparan sulfate, both of which are lost from the EC surface as part of the activation response to proinflammatory cytokines. Loss of these anticoagulant molecules potentiates the procoagulant properties of the injured vasculature. An additional thromboregulatory factor, ATP diphosphohydrolase (ATPDase; designated as EC 3.6.1.5) is also expressed by quiescent EC, and has the capacity to degrade the extracellular inflammatory mediators ATP and ADP to AMP, thereby inhibiting platelet activation and modulating vascular thrombosis. We describe here that the antithrombotic effects of the ATPDase, like heparan sulfate and thrombomodulin, are lost after EC activation, both in vitro and in vivo. Because platelet activation and aggregation are important components of the hemostatic changes that accompany inflammatory diseases, we suggest that the loss of vascular ATPDase may be crucial for the progression of vascular injury. The Rockefeller University Press 1997-01-06 /pmc/articles/PMC2196106/ /pubmed/8996251 Text en This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 4.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/4.0/). |
spellingShingle | Article Robson, Simon C. Kaczmarek, Elzbieta Siegel, Jonathan B. Candinas, Daniel Koziak, Katarzyna Millan, Maria Hancock, Wayne W. Bach, Fritz H. Loss of ATP Diphosphohydrolase Activity with Endothelial Cell Activation |
title | Loss of ATP Diphosphohydrolase Activity with Endothelial Cell Activation |
title_full | Loss of ATP Diphosphohydrolase Activity with Endothelial Cell Activation |
title_fullStr | Loss of ATP Diphosphohydrolase Activity with Endothelial Cell Activation |
title_full_unstemmed | Loss of ATP Diphosphohydrolase Activity with Endothelial Cell Activation |
title_short | Loss of ATP Diphosphohydrolase Activity with Endothelial Cell Activation |
title_sort | loss of atp diphosphohydrolase activity with endothelial cell activation |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2196106/ https://www.ncbi.nlm.nih.gov/pubmed/8996251 |
work_keys_str_mv | AT robsonsimonc lossofatpdiphosphohydrolaseactivitywithendothelialcellactivation AT kaczmarekelzbieta lossofatpdiphosphohydrolaseactivitywithendothelialcellactivation AT siegeljonathanb lossofatpdiphosphohydrolaseactivitywithendothelialcellactivation AT candinasdaniel lossofatpdiphosphohydrolaseactivitywithendothelialcellactivation AT koziakkatarzyna lossofatpdiphosphohydrolaseactivitywithendothelialcellactivation AT millanmaria lossofatpdiphosphohydrolaseactivitywithendothelialcellactivation AT hancockwaynew lossofatpdiphosphohydrolaseactivitywithendothelialcellactivation AT bachfritzh lossofatpdiphosphohydrolaseactivitywithendothelialcellactivation |