Protein C inhibitor (PCI) binds to phosphatidylserine exposing cells with implications in the phagocytosis of apoptotic cells and activated platelets.

Protein C Inhibitor (PCI) is a secreted serine protease inhibitor, belonging to the family of serpins. In addition to activated protein C PCI inactivates several other proteases of the coagulation and fibrinolytic systems, suggesting a regulatory role in hemostasis. Glycosaminoglycans and certain ne...

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Autores principales:	Daniela Rieger, Alice Assinger, Katrin Einfinger, Barbora Sokolikova, Margarethe Geiger
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2014
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/54e791b57d954bb68352fa35ad513ded
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spelling	oai:doaj.org-article:54e791b57d954bb68352fa35ad513ded2021-11-25T06:09:27ZProtein C inhibitor (PCI) binds to phosphatidylserine exposing cells with implications in the phagocytosis of apoptotic cells and activated platelets.1932-620310.1371/journal.pone.0101794https://doaj.org/article/54e791b57d954bb68352fa35ad513ded2014-01-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/25000564/pdf/?tool=EBIhttps://doaj.org/toc/1932-6203Protein C Inhibitor (PCI) is a secreted serine protease inhibitor, belonging to the family of serpins. In addition to activated protein C PCI inactivates several other proteases of the coagulation and fibrinolytic systems, suggesting a regulatory role in hemostasis. Glycosaminoglycans and certain negatively charged phospholipids, like phosphatidylserine, bind to PCI and modulate its activity. Phosphatidylerine (PS) is exposed on the surface of apoptotic cells and known as a phagocytosis marker. We hypothesized that PCI might bind to PS exposed on apoptotic cells and thereby influence their removal by phagocytosis. Using Jurkat T-lymphocytes and U937 myeloid cells, we show here that PCI binds to apoptotic cells to a similar extent at the same sites as Annexin V, but in a different manner as compared to live cells (defined spots on ∼10-30% of cells). PCI dose dependently decreased phagocytosis of apoptotic Jurkat cells by U937 macrophages. Moreover, the phagocytosis of PS exposing, activated platelets by human blood derived monocytes declined in the presence of PCI. In U937 cells the expression of PCI as well as the surface binding of PCI increased with time of phorbol ester treatment/macrophage differentiation. The results of this study suggest a role of PCI not only for the function and/or maturation of macrophages, but also as a negative regulator of apoptotic cell and activated platelets removal.Daniela RiegerAlice AssingerKatrin EinfingerBarbora SokolikovaMargarethe GeigerPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 9, Iss 7, p e101794 (2014)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Daniela Rieger Alice Assinger Katrin Einfinger Barbora Sokolikova Margarethe Geiger Protein C inhibitor (PCI) binds to phosphatidylserine exposing cells with implications in the phagocytosis of apoptotic cells and activated platelets.
description	Protein C Inhibitor (PCI) is a secreted serine protease inhibitor, belonging to the family of serpins. In addition to activated protein C PCI inactivates several other proteases of the coagulation and fibrinolytic systems, suggesting a regulatory role in hemostasis. Glycosaminoglycans and certain negatively charged phospholipids, like phosphatidylserine, bind to PCI and modulate its activity. Phosphatidylerine (PS) is exposed on the surface of apoptotic cells and known as a phagocytosis marker. We hypothesized that PCI might bind to PS exposed on apoptotic cells and thereby influence their removal by phagocytosis. Using Jurkat T-lymphocytes and U937 myeloid cells, we show here that PCI binds to apoptotic cells to a similar extent at the same sites as Annexin V, but in a different manner as compared to live cells (defined spots on ∼10-30% of cells). PCI dose dependently decreased phagocytosis of apoptotic Jurkat cells by U937 macrophages. Moreover, the phagocytosis of PS exposing, activated platelets by human blood derived monocytes declined in the presence of PCI. In U937 cells the expression of PCI as well as the surface binding of PCI increased with time of phorbol ester treatment/macrophage differentiation. The results of this study suggest a role of PCI not only for the function and/or maturation of macrophages, but also as a negative regulator of apoptotic cell and activated platelets removal.
format	article
author	Daniela Rieger Alice Assinger Katrin Einfinger Barbora Sokolikova Margarethe Geiger
author_facet	Daniela Rieger Alice Assinger Katrin Einfinger Barbora Sokolikova Margarethe Geiger
author_sort	Daniela Rieger
title	Protein C inhibitor (PCI) binds to phosphatidylserine exposing cells with implications in the phagocytosis of apoptotic cells and activated platelets.
title_short	Protein C inhibitor (PCI) binds to phosphatidylserine exposing cells with implications in the phagocytosis of apoptotic cells and activated platelets.
title_full	Protein C inhibitor (PCI) binds to phosphatidylserine exposing cells with implications in the phagocytosis of apoptotic cells and activated platelets.
title_fullStr	Protein C inhibitor (PCI) binds to phosphatidylserine exposing cells with implications in the phagocytosis of apoptotic cells and activated platelets.
title_full_unstemmed	Protein C inhibitor (PCI) binds to phosphatidylserine exposing cells with implications in the phagocytosis of apoptotic cells and activated platelets.
title_sort	protein c inhibitor (pci) binds to phosphatidylserine exposing cells with implications in the phagocytosis of apoptotic cells and activated platelets.
publisher	Public Library of Science (PLoS)
publishDate	2014
url	https://doaj.org/article/54e791b57d954bb68352fa35ad513ded
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Protein C inhibitor (PCI) binds to phosphatidylserine exposing cells with implications in the phagocytosis of apoptotic cells and activated platelets.

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