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...

Descripción completa

Detalles Bibliográficos
Autores principales: Robson, Simon C., Kaczmarek, Elzbieta, Siegel, Jonathan B., Candinas, Daniel, Koziak, Katarzyna, Millan, Maria, Hancock, Wayne W., Bach, Fritz H.
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