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Article ; Online: Histones induce phosphatidylserine exposure and a procoagulant phenotype in human red blood cells.

Semeraro, F / Ammollo, C T / Esmon, N L / Esmon, C T

Journal of thrombosis and haemostasis : JTH

2014 Volume 12, Issue 10, Page(s) 1697–1702

Abstract: Background: Extracellular histones exert part of their prothrombotic activity through the stimulation of blood cells. Besides platelets, histones can bind to red blood cells (RBCs), which are important contributors to thrombogenesis, but little is known ...

Abstract	Background: Extracellular histones exert part of their prothrombotic activity through the stimulation of blood cells. Besides platelets, histones can bind to red blood cells (RBCs), which are important contributors to thrombogenesis, but little is known about the functional consequences of this interaction. Objectives: To evaluate the effect of histones on the procoagulant potential of human RBCs with particular regard to the expression of surface phosphatidylserine (PS). Methods: PS exposure on human RBCs treated with a natural mixture of histones or recombinant individual histones was evaluated with fluorescein isothiocyanate-annexin-V binding and measured with flow cytometry. Calcium influx in RBCs loaded with the calcium-sensitive fluorophore Fluo-4 AM was assessed with flow cytometry. The procoagulant potential of histone-treated RBCs was evaluated with a purified prothrombinase assay and a one-stage plasma recalcification clotting test. Results: Natural histones induced PS exposure on RBCs in a dose-dependent manner, and neutralization or cleavage of histones by heparin or activated protein C, respectively, abolished PS externalization. H4 was mainly responsible for the stimulating activity of histones, whereas the other subtypes were almost ineffective. Similarly, natural histones and H4 induced influx of calcium into RBCs, whereas the other individual histones did not. Histone-induced exposure of PS on RBCs translated into increased prothrombinase complex-mediated prothrombin activation and accelerated fibrin formation in plasma. Conclusions: Histones induce RBCs to express a procoagulant phenotype through the externalization of PS. This finding provides new insights into the prothrombotic activity of extracellular histones.
MeSH term(s)	Aniline Compounds/chemistry ; Animals ; Annexin A5/chemistry ; Blood Coagulation ; Blood Platelets/metabolism ; Calcium/chemistry ; Cattle ; Coagulants/chemistry ; Erythrocytes/cytology ; Flow Cytometry ; Fluorescein-5-isothiocyanate/chemistry ; Histones/chemistry ; Humans ; Inflammation ; Phenotype ; Phosphatidylserines/chemistry ; Recombinant Proteins/chemistry ; Thromboplastin/chemistry ; Xanthenes/chemistry
Chemical Substances	Aniline Compounds ; Annexin A5 ; Coagulants ; Fluo 4 ; Histones ; Phosphatidylserines ; Recombinant Proteins ; Xanthenes ; Thromboplastin (9035-58-9) ; Fluorescein-5-isothiocyanate (I223NX31W9) ; Calcium (SY7Q814VUP)
Language	English
Publishing date	2014-08-26
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	2112661-6
ISSN	1538-7836 ; 1538-7933
ISSN (online)	1538-7836
ISSN	1538-7933
DOI	10.1111/jth.12677
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Article: Thrombomodulin.

Esmon, N L

Progress in hemostasis and thrombosis

1989 Volume 9, Page(s) 29–55

MeSH term(s)	Amino Acid Sequence ; Animals ; Blood Coagulation ; Blood Coagulation Factors/immunology ; Calcium/metabolism ; Cell Membrane/metabolism ; Endocytosis ; Endothelium, Vascular/injuries ; Endothelium, Vascular/metabolism ; Factor V/metabolism ; Factor Va ; Humans ; Lupus Coagulation Inhibitor ; Molecular Sequence Data ; Molecular Structure ; Protein C/metabolism ; Protein Conformation ; Rabbits ; Receptors, Cell Surface/metabolism ; Receptors, Thrombin ; Thrombin/metabolism
Chemical Substances	Blood Coagulation Factors ; Lupus Coagulation Inhibitor ; Protein C ; Receptors, Cell Surface ; Receptors, Thrombin ; Factor Va (65522-14-7) ; Factor V (9001-24-5) ; Thrombin (EC 3.4.21.5) ; Calcium (SY7Q814VUP)
Language	English
Publishing date	1989
Publishing country	United States
Document type	Journal Article ; Research Support, U.S. Gov't, P.H.S. ; Review
ZDB-ID	121802-5
ISSN	0362-6350
ISSN	0362-6350
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Article: Thrombomodulin.

Esmon, N L

Seminars in thrombosis and hemostasis

1987 Volume 13, Issue 4, Page(s) 454–463

MeSH term(s)	Animals ; Endothelium, Vascular/metabolism ; Humans ; Molecular Weight ; Protein C/metabolism ; Receptors, Cell Surface/isolation & purification ; Receptors, Cell Surface/physiology ; Receptors, Thrombin ; Thrombin/physiology
Chemical Substances	Protein C ; Receptors, Cell Surface ; Receptors, Thrombin ; Thrombin (EC 3.4.21.5)
Language	English
Publishing date	1987-10
Publishing country	United States
Document type	Journal Article ; Research Support, U.S. Gov't, P.H.S. ; Review
ZDB-ID	196901-8
ISSN	1098-9064 ; 0094-6176
ISSN (online)	1098-9064
ISSN	0094-6176
DOI	10.1055/s-2007-1003522
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Article ; Online: Extracellular histones increase plasma thrombin generation by impairing thrombomodulin-dependent protein C activation.

Ammollo, C T / Semeraro, F / Xu, J / Esmon, N L / Esmon, C T

Journal of thrombosis and haemostasis : JTH

2010 Volume 9, Issue 9, Page(s) 1795–1803

Abstract: Background: Histones are basic proteins that contribute to cell injury and tissue damage when released into the extracellular space. They have been attributed a prothrombotic activity, because their injection into mice induces diffuse microvascular ... ...

Abstract	Background: Histones are basic proteins that contribute to cell injury and tissue damage when released into the extracellular space. They have been attributed a prothrombotic activity, because their injection into mice induces diffuse microvascular thrombosis. The protein C-thrombomodulin (TM) system is a fundamental regulator of coagulation, particularly in the microvasculature, and its activity can be differentially influenced by interaction with several cationic proteins. Objective: To evaluate the effect of histones on the protein C-TM system in a plasma thrombin generation assay and in purified systems. Methods: The effect of histones on plasma thrombin generation in the presence or absence of TM was analyzed by calibrated automated thrombinography. Protein C activation in purified systems was evaluated by chromogenic substrate cleavage. The binding of TM and protein C to histones was evaluated by solid-phase binding assay. Results: Histones dose-dependently increased plasma thrombin generation in the presence of TM, independently of its chondroitin sulfate moiety. This effect was not caused by inhibition of activated protein C activity, but by the impairment of TM-mediated protein C activation. Histones were able to bind to both protein C and TM, but the carboxyglutamic acid domain of protein C was required for their effect. Histones H4 and H3 displayed the highest activity. Importantly, unlike heparin, DNA did not inhibit the potentiating effect of histones on thrombin generation. Conclusions: Histones enhance plasma thrombin generation by reducing TM-dependent protein C activation. This mechanism might contribute to microvascular thrombosis induced by histones in vivo at sites of organ failure or severe inflammation.
MeSH term(s)	Animals ; Blood Coagulation/drug effects ; Blood Coagulation/physiology ; DNA/metabolism ; DNA/pharmacology ; Extracellular Space/metabolism ; Heparin/metabolism ; Heparin/pharmacology ; Histones/metabolism ; Histones/pharmacology ; Humans ; In Vitro Techniques ; Mice ; Protein Binding ; Protein C/metabolism ; Recombinant Proteins/metabolism ; Thrombin/biosynthesis ; Thrombomodulin/metabolism ; Thrombosis/blood ; Thrombosis/etiology
Chemical Substances	Histones ; Protein C ; Recombinant Proteins ; THBD protein, human ; Thrombomodulin ; Heparin (9005-49-6) ; DNA (9007-49-2) ; Thrombin (EC 3.4.21.5)
Language	English
Publishing date	2010-12-23
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2112661-6
ISSN	1538-7836 ; 1538-7933
ISSN (online)	1538-7836
ISSN	1538-7933
DOI	10.1111/j.1538-7836.2011.04422.x
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Article: Regulated endothelial protein C receptor shedding is mediated by tumor necrosis factor-alpha converting enzyme/ADAM17.

Qu, D / Wang, Y / Esmon, N L / Esmon, C T

Journal of thrombosis and haemostasis : JTH

2006 Volume 5, Issue 2, Page(s) 395–402

Abstract: Endothelial protein C receptor (EPCR) plays an important role in the protein C anticoagulation pathway. Previously, we have reported that EPCR can be shed from the cell surface, and that this is mediated by an unidentified metalloproteinase. In this ... ...

Abstract	Endothelial protein C receptor (EPCR) plays an important role in the protein C anticoagulation pathway. Previously, we have reported that EPCR can be shed from the cell surface, and that this is mediated by an unidentified metalloproteinase. In this study, we demonstrate that tumor necrosis factor-alpha converting enzyme/ADAM17 (TACE) is responsible for EPCR shedding. Phorbol-12-myristate 13-acetate (PMA)-stimulated EPCR shedding is reduced by approximately 50% in HEK293 cells transfected with human EPCR cDNA and by 60% in human umbilical vein endothelial cells after transfection of TACE small interfering RNA (siRNA) into these cells. PMA-stimulated EPCR shedding is completely blocked in fibroblasts from TACE-deficient mice transfected with human EPCR cDNA, and restored by transfection of TACE cDNA into this cell line. To characterize the EPCR sequence requirement for shedding, we generated several mutants of EPCR. Replacing amino acids from residue 193 to residue 200 with the FLAG sequence (DYKDDDDK) completely blocks EPCR shedding, whereas a single amino acid substitution in this region has less effect on EPCR shedding.
MeSH term(s)	ADAM Proteins/metabolism ; ADAM Proteins/physiology ; ADAM17 Protein ; Animals ; Antigens, CD/genetics ; Antigens, CD/metabolism ; Cell Line ; Endothelial Protein C Receptor ; Endothelium, Vascular/cytology ; Endothelium, Vascular/metabolism ; Humans ; Mice ; Mice, Transgenic ; Receptors, Cell Surface/genetics ; Receptors, Cell Surface/metabolism ; Tetradecanoylphorbol Acetate/pharmacology ; Transfection ; Tumor Necrosis Factor-alpha
Chemical Substances	Antigens, CD ; Endothelial Protein C Receptor ; PROCR protein, human ; Receptors, Cell Surface ; Tumor Necrosis Factor-alpha ; ADAM Proteins (EC 3.4.24.-) ; ADAM17 Protein (EC 3.4.24.86) ; ADAM17 protein, human (EC 3.4.24.86) ; Adam17 protein, mouse (EC 3.4.24.86) ; Tetradecanoylphorbol Acetate (NI40JAQ945)
Language	English
Publishing date	2006-12-07
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	2112661-6
ISSN	1538-7836 ; 1538-7933
ISSN (online)	1538-7836
ISSN	1538-7933
DOI	10.1111/j.1538-7836.2007.02347.x
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Article: Reconstitution of the human endothelial cell protein C receptor with thrombomodulin in phosphatidylcholine vesicles enhances protein C activation.

Xu, J / Esmon, N L / Esmon, C T

The Journal of biological chemistry

1999 Volume 274, Issue 10, Page(s) 6704–6710

Abstract: Blocking protein C binding to the endothelial cell protein C receptor (EPCR) on the endothelium is known to reduce protein C activation rates. Now we isolate human EPCR and thrombomodulin (TM) and reconstitute them into phosphatidylcholine vesicles. The ... ...

Abstract	Blocking protein C binding to the endothelial cell protein C receptor (EPCR) on the endothelium is known to reduce protein C activation rates. Now we isolate human EPCR and thrombomodulin (TM) and reconstitute them into phosphatidylcholine vesicles. The EPCR increases protein C activation rates in a concentration-dependent fashion that does not saturate at 14 EPCR molecules/TM. Without EPCR, the protein C concentration dependence fits a single class of sites (Km = 2.17 +/- 0.13 microM). With EPCR, two classes of sites are apparent (Km = 20 +/- 15 nM and Km = 3.2 +/- 1.7 microM). Increasing the EPCR concentration at a constant TM concentration increases the percentage of high affinity sites. Holding the TM:EPCR ratio constant while decreasing the density of these proteins results in a decrease in the EPCR enhancement of protein C activation, suggesting that there is little affinity of the EPCR for TM. Negatively charged phospholipids also enhance protein C activation. EPCR acceleration of protein C activation is blocked by anti-EPCR antibodies, but not by annexin V, whereas the reverse is true with negatively charged phospholipids. Human umbilical cord endothelium expresses approximately 7 times more EPCR than TM. Anti-EPCR antibody reduces protein C activation rates 7-fold over these cells, whereas annexin V is ineffective, indicating that EPCR rather than negatively charged phospholipid provide the surface for protein C activation. EPCR expression varies dramatically among vascular beds. The present results indicate that the EPCR concentration will determine the effectiveness of the protein C activation complex.
MeSH term(s)	Blood Coagulation Factors ; Cell Line ; Endothelium, Vascular/metabolism ; Humans ; Membranes, Artificial ; Phosphatidylcholines ; Protein C/metabolism ; Receptors, Cell Surface/chemistry ; Receptors, Cell Surface/metabolism ; Recombinant Proteins/chemistry ; Recombinant Proteins/metabolism ; Thrombomodulin/chemistry ; Thrombomodulin/metabolism
Chemical Substances	Blood Coagulation Factors ; Membranes, Artificial ; Phosphatidylcholines ; Protein C ; Receptors, Cell Surface ; Recombinant Proteins ; Thrombomodulin ; activated protein C receptor
Language	English
Publishing date	1999-03-05
Publishing country	United States
Document type	Journal Article ; Research Support, U.S. Gov't, P.H.S.
ZDB-ID	2997-x
ISSN	1083-351X ; 0021-9258
ISSN (online)	1083-351X
ISSN	0021-9258
DOI	10.1074/jbc.274.10.6704
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Article: Thrombogenic mechanisms of antiphospholipid antibodies.

Esmon, N L / Smirnov, M D / Esmon, C T

Thrombosis and haemostasis

1997 Volume 78, Issue 1, Page(s) 79–82

Abstract: These studies indicate how immunoglobulin populations that react with phospholipid surfaces in the absence of other cofactor molecules can selectively inhibit anticoagulant pathways and lead to a prothrombotic state. These studies combined with those of ... ...

Abstract	These studies indicate how immunoglobulin populations that react with phospholipid surfaces in the absence of other cofactor molecules can selectively inhibit anticoagulant pathways and lead to a prothrombotic state. These studies combined with those of others indicating the presence of a-PE antibodies (often in isolation) in thrombotic patients illustrate the need to better define the assays to determine patients at risk. Neither the LA assays nor the anti-cardiolipin assays presently in use may be testing for the population(s) of clinical importance. A better understanding of the biochemical requirements of the various reactions involved should help the rational design of such assays. The preliminary studies of Salmon, et al, also show that the genetic context of the patient may contribute to the thrombotic mechanism of any APA present. It is unlikely any single mechanism is responsible for the thrombogenic activity of all APAs associated with thrombosis and this will be a fertile field of investigation for a significant time to come.
MeSH term(s)	Antibodies, Antiphospholipid/immunology ; Blood Coagulation/immunology ; Disease Susceptibility/immunology ; Humans ; Lupus Coagulation Inhibitor/immunology ; Membranes/immunology ; Phosphatidylserines/blood ; Protein C/chemistry ; Protein C/physiology ; Thrombosis/immunology
Chemical Substances	Antibodies, Antiphospholipid ; Lupus Coagulation Inhibitor ; Phosphatidylserines ; Protein C
Language	English
Publishing date	1997-07
Publishing country	Germany
Document type	Journal Article ; Review
ZDB-ID	518294-3
ISSN	0340-6245
ISSN	0340-6245
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Article: Lupus anticoagulants and thrombosis: the role of phospholipids.

Esmon, N L / Smirnov, M D / Esmon, C T

Haematologica

1997 Volume 82, Issue 4, Page(s) 474–477

Abstract: Background and objective: Lupus anticoagulants (LAs) are loosely defined as immunoglobulins that inhibit phospholipid dependent coagulation assays. Antiphospholipid antibodies (APAs) are those immunoglobulins that are observed to bind to phospholipids, ... ...

Abstract	Background and objective: Lupus anticoagulants (LAs) are loosely defined as immunoglobulins that inhibit phospholipid dependent coagulation assays. Antiphospholipid antibodies (APAs) are those immunoglobulins that are observed to bind to phospholipids, usually cardiolipin, in ELISA type assays. Interest in these antibody populations derives from the observation that rather than being associated with bleeding disorders as would be expected, they correlate with an increased risk of thrombosis. Many mechanisms have been proposed to account for the prothrombotic activity of some LAs and APAs. These mechanisms are as diverse as inhibition of the production of endothelial prostacyclin synthesis or impaired fibrinolysis to interaction with beta 2-glycoprotein 1 or prothrombin bound to phospholipids. For the purposes of this review, we would like to focus on a potential mechanism that has been proposed by several labs in addition to our own, namely inhibition of the protein C anticoagulant pathway. Information sources: The authors have been working in this field and contributing original papers. In addition, the material examined in the present paper includes articles published in journals covered by the Science Citation Index and Medline. State of art and perspectives: In general, correlation of phospholipid specificity and thrombosis has not been performed on a large scale. We were therefore led to ask two questions. Are the membrane requirements of the protein C anticoagulant pathway really the same as those for the procoagulant complexes? Secondly, if they are not, do the membrane requirements of the anticoagulant complexes mimic those of the thrombotic LAs? The membrane requirements for the activated protein C anticoagulant complex differ from those of the prothrombinase complex. These requirements, i.e. the need for phosphatidylethanolamine for optimal activity, mimic the lipid requirements for at least a population of lupus anticoagulants associated with thrombosis. These observations may provide both the specificity and the link between the activated protein C pathway, lupus anticoagulants and thrombosis. Of course, no conclusion is ever that black and white. Only future studies into the fine specificity of lupus anticoagulants and anti-phospholipid antibodies associated with thrombosis will bear out the hypothesis that those directed towards the activated protein C pathway will be predictive of thrombotic risk.
MeSH term(s)	Humans ; Lupus Coagulation Inhibitor ; Phospholipids ; Thrombosis/immunology ; Thrombosis/metabolism
Chemical Substances	Lupus Coagulation Inhibitor ; Phospholipids
Language	English
Publishing date	1997-07
Publishing country	Italy
Document type	Journal Article ; Research Support, U.S. Gov't, P.H.S. ; Review
ZDB-ID	2333-4
ISSN	1592-8721 ; 0390-6078 ; 0017-6567
ISSN (online)	1592-8721
ISSN	0390-6078 ; 0017-6567
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Article: The Ser219-->Gly dimorphism of the endothelial protein C receptor contributes to the higher soluble protein levels observed in individuals with the A3 haplotype.

Qu, D / Wang, Y / Song, Y / Esmon, N L / Esmon, C T

Journal of thrombosis and haemostasis : JTH

2005 Volume 4, Issue 1, Page(s) 229–235

Abstract: The endothelial cell protein C receptor (EPCR) plays an important role in regulating blood coagulation and in activated protein C-mediated anti-inflammatory and antiapoptotic processes. Recent studies reported that there are polymorphisms in the human ... ...

Abstract	The endothelial cell protein C receptor (EPCR) plays an important role in regulating blood coagulation and in activated protein C-mediated anti-inflammatory and antiapoptotic processes. Recent studies reported that there are polymorphisms in the human EPCR gene. One of the polymorphisms (haplotype A3) results in substitution of the Ser at residue 219 with Gly in the transmembrane domain. This haplotype is associated with increased plasma levels of soluble EPCR and is a candidate risk factor for thrombosis. We established stable cell lines expressing either the EPCR A1 (Ser at residue 219) or A3 (Gly at residue 219) haplotype. Both constitutive and PMA-stimulated shedding are five- to sevenfold higher in the A3 cell line than the A1 cell line. We also isolated human umbilical vein endothelial cells (HUVEC) from A1/A1 or A1/A3 origins. PMA-stimulated shedding is fourfold higher in HUVEC derived from A1/A3 origin than from A1/A1 origin. After PMA treatment, the rate of human protein C activation decreased 36% in HUVEC derived from A1/A3 origin, while it only decreased 18% in HUVEC derived from A1/A1 origin. These results indicate that the A3 haplotype does promote cellular shedding in either 293 or endothelial cells and therefore is likely directly contributory to the higher soluble EPCR levels seen in patients carrying this haplotype.
MeSH term(s)	Amino Acid Substitution ; Antigens/analysis ; Antigens/genetics ; Antigens, CD ; Blood Coagulation Factors/analysis ; Blood Coagulation Factors/genetics ; Cells, Cultured ; Endothelial Protein C Receptor ; Endothelium, Vascular/cytology ; Endothelium, Vascular/metabolism ; Glycoproteins/analysis ; Glycoproteins/genetics ; Haplotypes ; Humans ; Polymorphism, Genetic ; Protein C/metabolism ; Receptors, Cell Surface/analysis ; Receptors, Cell Surface/genetics ; Solubility ; Tetradecanoylphorbol Acetate/pharmacology ; Umbilical Veins/cytology
Chemical Substances	Antigens ; Antigens, CD ; Blood Coagulation Factors ; Endothelial Protein C Receptor ; Glycoproteins ; PROCR protein, human ; Protein C ; Receptors, Cell Surface ; Tetradecanoylphorbol Acetate (NI40JAQ945)
Language	English
Publishing date	2005-12-23
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	2112661-6
ISSN	1538-7836 ; 1538-7933
ISSN (online)	1538-7836
ISSN	1538-7933
DOI	10.1111/j.1538-7836.2005.01676.x
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Article: Protein C and the endothelium.

Esmon, N L / Esmon, C T

Seminars in thrombosis and hemostasis

1988 Volume 14, Issue 2, Page(s) 210–215

Abstract: With the continued accumulation of clinical and animal studies, it is becoming abundantly clear that the protein C anticoagulant pathway plays a critical role in the regulation of coagulation. Investigations also indicate that this pathway is intimately ... ...

Abstract	With the continued accumulation of clinical and animal studies, it is becoming abundantly clear that the protein C anticoagulant pathway plays a critical role in the regulation of coagulation. Investigations also indicate that this pathway is intimately involved in the interaction of the coagulation and inflammatory systems. Although no direct information is presently available, the function of this pathway is likely depressed in the regions of atherosclerotic plaque. It is clear that monocytes accumulate in this region and release many growth factors and monokines that are capable of endothelial function perturbation. Perturbation of the protein C anticoagulant pathway is one viable mechanism for the hypercoagulable state in this disease. As indicated here, the endothelial cells of the vessel wall play a critical role in the initiation, and possibly expression, of this pathway. Any injury to these cells that affects the proper expression of thrombomodulin, synthesis of protein S, or Factor Va inactivation complex formation could potentially lead to a hypercoagulable state and thrombotic complications. As has been discussed, several inflammatory mediators are already known that fulfill the criteria of endothelial cell perturbants that may lead to such a state. What other entities might have similar effects, either directly or indirectly through induction of cytokines, is not known at this time. A more complete understanding of this critical pathway and the effects of vascular disease on it should lead to a better understanding of many diverse disease processes and potential therapeutic strategies in the future.
MeSH term(s)	Animals ; Arteriosclerosis/blood ; Endothelium, Vascular/metabolism ; Humans ; Protein C/metabolism ; Receptors, Cell Surface/metabolism ; Receptors, Thrombin ; Thrombosis/blood
Chemical Substances	Protein C ; Receptors, Cell Surface ; Receptors, Thrombin
Language	English
Publishing date	1988-04
Publishing country	United States
Document type	Journal Article ; Research Support, U.S. Gov't, P.H.S. ; Review
ZDB-ID	196901-8
ISSN	1098-9064 ; 0094-6176
ISSN (online)	1098-9064
ISSN	0094-6176
DOI	10.1055/s-2007-1002779
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