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Journal articles on the topic 'Anti-thrombin'

Author: Grafiati

Published: 3 June 2025

Last updated: 1 August 2025

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1

Sosolik, Randy C., Karl S. Theil, and John T. Brandt. "Anti-Bovine Thrombin Antibody." Laboratory Medicine 27, no. 10 (1996): 651–54. http://dx.doi.org/10.1093/labmed/27.10.651.

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2

EVINGTON, JOHN R. N., PETER A. FELDMAN, MOLLIE LUSCOMBE, and J. JOHN HOLBROOK. "Fluorescence polarization studies of the thrombin/anti-thrombin reactions." Biochemical Society Transactions 13, no. 4 (1985): 773–74. http://dx.doi.org/10.1042/bst0130773a.

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3

Proulle, Valerie, Celine Desconclois, Cecile Lavenu-Bombled, Cecile Goujard, Anish V. Sharda, and Ali G. Turhan. "Severe Acquired Bleeding Tendency Secondary To An Anti-Thrombin Antibody In a Patient With Monoclonal Gammapathy Of Unknown Significance: Direct In Vivo evidence." Blood 122, no. 21 (2013): 1111. http://dx.doi.org/10.1182/blood.v122.21.1111.1111.

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Abstract Introduction Anti-thrombin antibodies are a rare cause of acquired bleeding disorder. We report a case of a patient with a monoclonal gammapathy of unknown significance (MGUS) referred to us for an acquired bleeding tendency. We found that he had an isolated anti-thrombin antibody and showed that this antibody inhibit platelet accumulation and fibrin generation in vivo in a mouse model of arterial thrombus formation. Patient A 40-year-old man with no personal or familial history of bleeding was referred to us for multiple bleeding episodes (rectal bleeding, hematoma) for 18 years. He

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4

Norton, KJ, RM Scarborough, JL Kutok, MA Escobedo, L. Nannizzi, and BS Coller. "Immunologic analysis of the cloned platelet thrombin receptor activation mechanism: evidence supporting receptor cleavage, release of the N-terminal peptide, and insertion of the tethered ligand into a protected environment." Blood 82, no. 7 (1993): 2125–36. http://dx.doi.org/10.1182/blood.v82.7.2125.2125.

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Abstract The recently cloned functional thrombin receptor is thought to be activated by thrombin cleavage of the bond between R41 and S42, followed by the insertion of the new N-terminal region (“tethered ligand”) into an unknown site in the receptor. Antibodies to peptides at or near the cleavage site have been reported to inhibit thrombin- induced platelet activation to varying extents, but the precise mechanism(s) of their inhibition is unknown. We have produced: (1) a polyclonal antibody in rabbits to a peptide containing amino acids 34 to 52 (anti-TR34–52); enzyme-linked immunosorbent ass

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Norton, KJ, RM Scarborough, JL Kutok, MA Escobedo, L. Nannizzi, and BS Coller. "Immunologic analysis of the cloned platelet thrombin receptor activation mechanism: evidence supporting receptor cleavage, release of the N-terminal peptide, and insertion of the tethered ligand into a protected environment." Blood 82, no. 7 (1993): 2125–36. http://dx.doi.org/10.1182/blood.v82.7.2125.bloodjournal8272125.

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The recently cloned functional thrombin receptor is thought to be activated by thrombin cleavage of the bond between R41 and S42, followed by the insertion of the new N-terminal region (“tethered ligand”) into an unknown site in the receptor. Antibodies to peptides at or near the cleavage site have been reported to inhibit thrombin- induced platelet activation to varying extents, but the precise mechanism(s) of their inhibition is unknown. We have produced: (1) a polyclonal antibody in rabbits to a peptide containing amino acids 34 to 52 (anti-TR34–52); enzyme-linked immunosorbent assays (ELIS

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6

Kimura, M., T. T. Andersen, J. W. Fenton, W. F. Bahou, and A. Aviv. "Plasmin-platelet interaction involves cleavage of functional thrombin receptor." American Journal of Physiology-Cell Physiology 271, no. 1 (1996): C54—C60. http://dx.doi.org/10.1152/ajpcell.1996.271.1.c54.

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We tested the hypothesis that the inhibition of thrombin-induced platelet activation by plasmin is mediated via the enzymatic action of plasmin on the functional thrombin receptor. We monitored the binding of the anti-thrombin receptor antibody [anti-TR-(34-46)] to platelets; this binding is sensitive to the cleavage of the thrombin receptor at amino acid residues Arg-41 to Ser-42. Plasmin inhibited anti-TR-(34-46) binding in dose- and time-dependent manners. The inactive synthetic peptide with the amino acid sequence 40-55 of the thrombin receptor (D-FPRSFLLRNPNDKYEPF) was similarly cleaved b

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7

Billoir, Paul, Thomas Elie, Jerrold H. Levy, et al. "Anticoagulation Monitoring with Activated Partial ThromboPlastin Time and Anti-Xa Activity in Intensive Care Unit Patients: Interest of Thrombin Generation Assay." International Journal of Molecular Sciences 23, no. 19 (2022): 11219. http://dx.doi.org/10.3390/ijms231911219.

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Current guidelines recommend monitoring the anticoagulant effect of unfractionated heparin (UFH) by measuring anti-Xa activity rather than activated partial thromboplastin time (aPTT) in intensive care unit (ICU) patients. The primary objective of this study was to evaluate the correlation of aPTT, anti-Xa activity, and thrombin generation in UFH-treated ICU patients. A prospective observational pilot study was conducted in adult surgical ICU patients treated with UFH. aPTT and anti-Xa activity were monitored daily. The therapeutic target was aPTT between 50 s and 84 s, and/or anti-Xa between

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8

Dolor, MC, and M. Kastetter. "Anti-D in human thrombin." Transfusion 26, no. 2 (1986): 215. http://dx.doi.org/10.1046/j.1537-2995.1986.26286152922.x.

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9

Leclerc, J. R., W. Geerts, A. Panju, P. Nguyen, and J. Hirsh. "Management of anti-thrombin III deficiency during pregnancy without administration of anti-thrombin III." Thrombosis Research 41, no. 4 (1986): 567–73. http://dx.doi.org/10.1016/0049-3848(86)91702-0.

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10

Brisson, Christine, Gisèle Archipoff, Marie-Louise Hartmann, et al. "Antibodies to Thrombomodulin Induce Receptor-Mediated Endocytosis in Human Saphenous Vein Endothelial Cells." Thrombosis and Haemostasis 68, no. 06 (1992): 737–43. http://dx.doi.org/10.1055/s-0038-1646353.

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SummaryThe membrane glycoprotein thrombomodulin (TM) is an essential endothelial cell (EC) cofactor, which forms a 1:1 stoichiometric complex with thrombin. Binding of thrombin to the high affinity TM receptor transforms its procoagulant activity into an anticoagulant potential, by activating protein C. The fate of TM in the presence of thrombin is still unclear: some authors claim that the thrombin-TM complex is internalized in EC, while others find this complex to be stable for at least 2 h at 37° C on the EC surface. In the present study, we investigated the interactions of thrombin and Fab

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11

Zhu, He, Debra Hoppensteadt, Rakesh Wahi, Craig Paterson та Jawed Fareed. "Cross-Reactivity of Rabbit Anti-Bovine Thrombin IgGs with Human α-Thrombin and a Recombinant Version of Human Thrombin (Recothrom™)." Blood 114, № 22 (2009): 4211. http://dx.doi.org/10.1182/blood.v114.22.4211.4211.

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Abstract Abstract 4211 It has been reported that patients exposed to topical bovine thrombin preparations may develop antibodies to bovine thrombin, factor V or various other proteins. In some cases these antibodies can cross-react with the corresponding human coagulation proteins. The present study was undertaken to determine if the antibodies induced by bovine thrombin antigens in rabbits could also cross-react with human a-thrombin and RecothromTM. Bovine crude thrombin and its purified versions, thrombin 4A and 4B, were administered to individual groups of rabbits on 0, 21, 42, 91, 123 and

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12

Schoen, Pieter, Theo Lindhout, Jo Franssen, and H. Coenraad Hemker. "Low Molecular Weight Heparin-Catalyzed Inactivation of Factor Xa and Thrombin by Antithrombin III – Effect of Platelet Factor 4." Thrombosis and Haemostasis 66, no. 04 (1991): 435–41. http://dx.doi.org/10.1055/s-0038-1646434.

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SummaryLow molecular weight (LMW) heparin preparations have unknown distributions of ATIII-binding material, so mean molecular weights as such might bear little information on their anti-factor Xa and anti-thrombin activities, and on the neutralization of these activities by platelet factor 4 (PF4). These properties were investigated in pure systems with proteins of human origin. Pseudo-first order rate constants of inactivation of factor Xa and thrombin by antithrombin III were determined as function of heparin concentration, in the presence of 4.0 mM CaCl2. Despite a large variation in the m

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13

Sadeghi, Nasir, Josephine Cunanan, Debra Hoppensteadt, Indermohan Thethi, Rakesh Wahi, and Jawed Fareed. "Cross Reactivity of Rabbit Anti-Recothrom (Human Recombinant Thrombin) Antibodies with Molecular Variants of Human Thrombin, and Various Bovine Thrombin Preparations." Blood 116, no. 21 (2010): 4418. http://dx.doi.org/10.1182/blood.v116.21.4418.4418.

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Abstract Abstract 4418 Bovine thrombin preparations are widely used as topical hemostatic agents. While earlier bovine thrombin preparations were reported to produce immunologic responses upon repeated exposure, the refined bovine thrombin and recombinant human thrombin preparations (Zymogenetics, Seattle, WA, USA) are claimed to be less immunogenic. It was hypothesized that recombinant human thrombin despite its reduced immunogenic nature, upon repeated administration may result in the generation of antibodies and that may cross react with bovine and human thrombin. To test this hypothesis, g

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14

Mismetti, P., S. Laporte-Simitsidis, C. Navarro, et al. "Aging and Venous Thromboembolism Influence the Pharmacodynamics of the Anti-Factor Xa and Anti-thrombin Activities of a Low Molecular Weight Heparin (Nadroparin)." Thrombosis and Haemostasis 79, no. 06 (1998): 1162–65. http://dx.doi.org/10.1055/s-0037-1615034.

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SummaryVenous thromboembolism may be efficiently treated by one single daily administration of a high dose of low molecular weight heparin (LMWH). The present study investigates if the physiological deterioration of renal function associated with normal aging or the presence of an acute venous thromboembolism influences the pharmacodynamic pattern of the anti-factor Xa and anti-thrombin activities. Three groups of 12 subjects were investigated. The first 2 groups were composed of healthy volunteers differing by age (25 ± 4 and 65 ± 3 yrs) and creati-nine clearance (114 ± 15 and 62 ± 6 ml · min

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15

Hao, Lihua, and Qiang Zhao. "A fluorescein labeled aptamer switch for thrombin with fluorescence decrease response." Analytical Methods 7, no. 9 (2015): 3888–92. http://dx.doi.org/10.1039/c5ay00464k.

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16

Ansari, Umer Saeed. "Anti-Thrombin and its Biological Significance." Pakistan Journal of Medical and Health Sciences 17, no. 7 (2023): 1. http://dx.doi.org/10.53350/pjmhs20231771.

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Anti-thrombin (AT) is a small molecular weight glycoprotein molecule, synthesized by liver, and circulates in the plasma at a concentration approximately 150 mg/ml1. AT belongs to a family of serine proteases, and most potent inhibitor of coagulation, and has vital role in maintaining haemostatic balance. It is also termed as ‘Heparin Cofactor’, and is considered essential for effective heparin therapy. Under normal conditions, its biological half-life is 1.5–2.5 days; But in conditions of acquired deficiency, and in the presence of heparin, the half-life of AT is much shorter, even being redu

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17

Kaplanski, Gilles, Valérie Marin, Martine Fabrigoule, et al. "Thrombin-Activated Human Endothelial Cells Support Monocyte Adhesion In Vitro Following Expression of Intercellular Adhesion Molecule-1 (ICAM-1; CD54) and Vascular Cell Adhesion Molecule-1 (VCAM-1; CD106)." Blood 92, no. 4 (1998): 1259–67. http://dx.doi.org/10.1182/blood.v92.4.1259.

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Abstract Thrombin, a central molecule in coagulation, is also involved in inflammation. Notably, thrombin induces endothelial neutrophil adhesion, P- and E-selectin expression, and chemokine production. We show here that thrombin induces expression of intercellular adhesion molecule-1 (ICAM-1; CD54) and vascular cell adhesion molecule-1 (VCAM-1; CD106) on human umbilical vein endothelial cells (HUVECs) associated with increased adhesion of monocytes. Thrombin increased mRNA steady-state levels and expression of ICAM-1 over 24 hours. Thrombin-induced VCAM-1 expression exhibited unusual kinetics

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18

Kaplanski, Gilles, Valérie Marin, Martine Fabrigoule, et al. "Thrombin-Activated Human Endothelial Cells Support Monocyte Adhesion In Vitro Following Expression of Intercellular Adhesion Molecule-1 (ICAM-1; CD54) and Vascular Cell Adhesion Molecule-1 (VCAM-1; CD106)." Blood 92, no. 4 (1998): 1259–67. http://dx.doi.org/10.1182/blood.v92.4.1259.416k11_1259_1267.

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Thrombin, a central molecule in coagulation, is also involved in inflammation. Notably, thrombin induces endothelial neutrophil adhesion, P- and E-selectin expression, and chemokine production. We show here that thrombin induces expression of intercellular adhesion molecule-1 (ICAM-1; CD54) and vascular cell adhesion molecule-1 (VCAM-1; CD106) on human umbilical vein endothelial cells (HUVECs) associated with increased adhesion of monocytes. Thrombin increased mRNA steady-state levels and expression of ICAM-1 over 24 hours. Thrombin-induced VCAM-1 expression exhibited unusual kinetics, reachin

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19

Iqbal, Zafar, Gurinder Rana, and Marc Cohen. "Appropriate Anti-Thrombotic/Anti-Thrombin Therapy for Thrombotic Lesions." Current Cardiology Reviews 8, no. 3 (2012): 181–91. http://dx.doi.org/10.2174/157340312803217175.

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20

Shi, Xiaoli, Beena Gangadharan, Lawrence F. Brass, Wolfram Ruf, and Barbara M. Mueller. "Protease-Activated Receptors (PAR1 and PAR2) Contribute to Tumor Cell Motility and Metastasis." Molecular Cancer Research 2, no. 7 (2004): 395–402. http://dx.doi.org/10.1158/1541-7786.395.2.7.

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Abstract The effects of the pleiotropic serine protease thrombin on tumor cells are commonly thought to be mediated by the thrombin receptor protease-activated receptor 1 (PAR1). We demonstrate here that PAR1 activation has a role in experimental metastasis using the anti-PAR1 antibodies ATAP2 and WEDE15, which block PAR1 cleavage and activation. Thrombin also stimulates chemokinesis of human melanoma cells toward fibroblast conditioned media and soluble matrix proteins. Thrombin-enhanced migration is abolished by anti-PAR1 antibodies, demonstrating that PAR1 cleavage and activation are requir

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21

Kim, Young Eun, Se In Sung, Yun Sil Chang, So Yoon Ahn, Dong Kyung Sung, and Won Soon Park. "Thrombin Preconditioning Enhances Therapeutic Efficacy of Human Wharton’s Jelly–Derived Mesenchymal Stem Cells in Severe Neonatal Hypoxic Ischemic Encephalopathy." International Journal of Molecular Sciences 20, no. 10 (2019): 2477. http://dx.doi.org/10.3390/ijms20102477.

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We investigated whether thrombin preconditioning of human Wharton’s jelly–derived mesenchymal stem cells (MSCs) improves paracrine potency and thus the therapeutic efficacy of naïve MSCs against severe hypoxic ischemic encephalopathy (HIE). Thrombin preconditioning significantly enhances the neuroprotective anti-oxidative, anti-apoptotic, and anti-cytotoxic effects of naïve MSCs against oxygen–glucose deprivation (OGD) of cortical neurons in vitro. Severe HIE was induced in vivo using unilateral carotid artery ligation and hypoxia for 2 h and confirmed using brain magnetic resonance imaging (M

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22

Litinas, Evangelos, Angel Gray, Nasir Sadeghi, Josephine Cunanan, Debra Hoppensteadt, and Jawed Fareed. "Persistant Inhibition of Thrombin Generation After Intravenous Administration of Enoxaparin in Primates." Blood 114, no. 22 (2009): 2095. http://dx.doi.org/10.1182/blood.v114.22.2095.2095.

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Abstract Abstract 2095 Poster Board II-72 The biologic half life (T12) of low molecular weight heparin (LMWH) is usually measured in terms of the circulating anti-Xa levels. Enoxaparin represents an unique LMWH whose biologic T12 is relatively longer than most LMWHs. Moreover, it is known that the antithrombotic effects of this agent last longer in comparison to the measurable circulating anti-Xa levels. Therefore besides the anti-Xa activity, additional non-measurable biologic effects are contributory to the clinical effects of this agent. Plasma based thrombin generation assays have recently

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23

Gerotziafas, Grigorios T., Galea Vasso, Jeanine M. Walenga, et al. "Thrombin Generation Assessment in Platelet Rich Plasma Offers Additional Criteria for Low Molecular Weight Heparin Antithrombotic Fingerprint Characterization." Blood 114, no. 22 (2009): 4177. http://dx.doi.org/10.1182/blood.v114.22.4177.4177.

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Abstract Abstract 4177 Introduction National and international organizations recognize that low molecular weight heparins (LMWHs) are distinct entities and that they should not be used interchangeably in clinical practice. Physicochemical properties, such as molecular weight anti-Xa/anti-IIa ratios, are used by health authorities to establish LMWHs differentiation. LMWHs are multitargeted drugs in which small differences in physicochemical properties may lead to significantly different inhibition of blood coagulation. In the present in vitro study we have investigated if thrombin generation as

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24

He Zhu, Debra Hoppensteadt, Michael Morris, and Jawed Fareed. "Cross-Reactivity of Rabbit Anti-Bovine Prothrombin/Thrombin IgGs With Bovine Factor V/Va-Related Antigens." Clinical and Applied Thrombosis/Hemostasis 16, no. 5 (2010): 522–28. http://dx.doi.org/10.1177/1076029610375423.

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The purpose of this study was to determine whether rabbit anti-bovine prothrombin/thrombin immunoglobulin Gs (IgGs) would cross-react with bovine factor V/Va-related antigens. Bovine prothrombin, crude thrombin, as well as 2 purified versions of thrombin, that is, thrombin 4A (the previous version of Thrombin-JMI marketed prior to 2008) and 4B (the currently marketed version of Thrombin-JMI), were administrated to individual groups of rabbits on days 0, 21, 42, 91, 123, and 151 using standard immunologic methods. Blood was drawn from each rabbit on days 30, 50, 105, 137, and 165 and the pooled

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25

Béguin, Suzette, Frédérique Dol, and H. Coenraad Hemker. "Factor IXa Inhibition Contributes to the Heparin Effect." Thrombosis and Haemostasis 66, no. 03 (1991): 306–9. http://dx.doi.org/10.1055/s-0038-1646412.

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SummaryWe investigated whether the inactivation of factor IXa contributes to the partial inhibition of thrombin formation that is observed at therapeutic concentrations of heparin. The action of standard unfractionated heparin (0.05 U/ml) on thrombin formation in the intrinsic system was compared to that of a mixture of dermatan sulfate (DS) and a synthetic pentasaccharide (PS). DS enhances the action of heparin cofactor II which inhibits thrombin only. PS specifically enhances the anti-factor Xa activity of antithrombin III (AT III). The concentrations of DS and PS were chosen so as to obtain

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26

Peyrou, V., J. C. Lormeau, C. Caranobe, et al. "Pharmacological Properties of CY 216 and of Its ACLM and BCLM Components in the Rabbit." Thrombosis and Haemostasis 72, no. 02 (1994): 268–74. http://dx.doi.org/10.1055/s-0038-1648851.

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SummaryThis study compares some in vivo pharmacological properties of CY 216 and of its ACLM and BCLM components having a molecular weight above and below 5.4 kDa respectively. The anti-factor Xa/anti-thrombin ratio of these compounds determined in a rabbit plasma system were 2.5 and 1.2 for CY 216 and ACLM respectively while BCLM was devoid of anti-thrombin effect. After bolus intravenous injection, continuous infusion and subcutaneous administration, the clearances of anti-factor Xa activity generated by ACLM were, on the average, 2 and 1.5 times higher than those generated by BCLM and CY 21

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27

de Fouw, N. J., V. W. M. van Hinsbergh, Y. F. de Jong, F. Haverkate, and R. M. Bertina. "The Interaction of Activated Protein C and Thrombin with the Plasminogen Activator Inhibitor Released from Human Endothelial Cells." Thrombosis and Haemostasis 57, no. 02 (1987): 176–82. http://dx.doi.org/10.1055/s-0038-1651089.

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SummaryThe effects of human activated protein C (APC) and thrombin on plasminogen activator inhibitor (PAI-1) released from cultured human umbilical endothelial cells, grown in serum-free 35S-methionine containing medium, were studied in two ways: 1) measurement of PAI-1 activity with an amidolytic assay, and 2) immunoprécipitation of the medium with anti-PAI-1 IgG, antiprotein C IgG or anti-thrombin IgG followed by SDS-PAGE and autoradiography.Addition of APC or thrombin to the endothelial cell conditioned medium results in a time and concentration dependent loss of PAI-1 activity and in the

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28

Legrand, C., V. Dubernard, and AT Nurden. "Studies on the mechanism of expression of secreted fibrinogen on the surface of activated human platelets." Blood 73, no. 5 (1989): 1226–34. http://dx.doi.org/10.1182/blood.v73.5.1226.1226.

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Abstract Affinity purified anti-fibrinogen (anti-Fg) Fab fragments were used to study the mechanism of expression of alpha-granule fibrinogen on activated platelets. Low amounts of the radiolabeled anti-Fg Fab bound to unstimulated or adenosine diphosphate (ADP)-stimulated cells. They readily bound to platelets stimulated with collagen, alpha-thrombin or gamma-thrombin in the presence of divalent cations. At 1 n mol/L alpha- thrombin or 25 nmol/L gamma-thrombin, platelet fibrinogen was expressed on the surface of the cells notwithstanding the presence of AP-2, a monoclonal antibody to the glyc

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29

Legrand, C., V. Dubernard, and AT Nurden. "Studies on the mechanism of expression of secreted fibrinogen on the surface of activated human platelets." Blood 73, no. 5 (1989): 1226–34. http://dx.doi.org/10.1182/blood.v73.5.1226.bloodjournal7351226.

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Affinity purified anti-fibrinogen (anti-Fg) Fab fragments were used to study the mechanism of expression of alpha-granule fibrinogen on activated platelets. Low amounts of the radiolabeled anti-Fg Fab bound to unstimulated or adenosine diphosphate (ADP)-stimulated cells. They readily bound to platelets stimulated with collagen, alpha-thrombin or gamma-thrombin in the presence of divalent cations. At 1 n mol/L alpha- thrombin or 25 nmol/L gamma-thrombin, platelet fibrinogen was expressed on the surface of the cells notwithstanding the presence of AP-2, a monoclonal antibody to the glycoprotein

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30

Selmeczi, Anna, Rachel E. J. Roach, Csaba More, et al. "Thrombin Generation and Low Molecular Weight Heparin Prophylaxis In Pregnant Women With Thrombophilia." Blood 122, no. 21 (2013): 1140. http://dx.doi.org/10.1182/blood.v122.21.1140.1140.

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Abstract Introduction Pregnancy is associated with an increased risk of venous thromboembolism (VTE) which is even more pronounced in the presence of inherited thrombophilia. Despite the well-established relation between thrombophilic pregnancies and VTE, there is no consensus on the optimal approach for thromboprophylaxis in this population. There is growing evidence that thrombin generation correlates with the overall procoagulant state of the plasma leading to elevated thrombosis risk. The aim of this study was to evaluate thrombin generation over the course of pregnancy in women with inher

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31

Ukan, Ürün, Fredy Delgado Lagos, Sebastian Kempf, et al. "Effect of Thrombin on the Metabolism and Function of Murine Macrophages." Cells 11, no. 10 (2022): 1718. http://dx.doi.org/10.3390/cells11101718.

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Macrophages are plastic and heterogeneous immune cells that adapt pro- or anti-inflammatory phenotypes upon exposure to different stimuli. Even though there has been evidence supporting a crosstalk between coagulation and innate immunity, the way in which protein components of the hemostasis pathway influence macrophages remains unclear. We investigated the effect of thrombin on macrophage polarization. On the basis of gene expression and cytokine secretion, our results suggest that polarization with thrombin induces an anti-inflammatory, M2-like phenotype. In functional studies, thrombin pola

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32

Wang, Xiaoyan, Zhen Yang, Feifei Su, et al. "Study on Structure Activity Relationship of Natural Flavonoids against Thrombin by Molecular Docking Virtual Screening Combined with Activity Evaluation In Vitro." Molecules 25, no. 2 (2020): 422. http://dx.doi.org/10.3390/molecules25020422.

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Thrombin, a key enzyme of the serine protease superfamily, plays an integral role in the blood coagulation cascade and thrombotic diseases. In view of this, it is worthwhile to establish a method to screen thrombin inhibitors (such as natural flavonoid-type inhibitors) as well as investigate their structure activity relationships. Virtual screening using molecular docking technique was used to screen 103 flavonoids. Out of this number, 42 target compounds were selected, and their inhibitory effects on thrombin assayed by chromogenic substrate method. The results indicated that the carbon-carbo

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33

Sassi, Mouna, Taher Chakroun, Elisabeth Mbemba, et al. "The Antithrombotic Potential of Tinzaparin and Enoxaparin Upon Thrombin Generation Triggered In Vitro by Human Ovarian Cancer Cells IGROV1." Clinical and Applied Thrombosis/Hemostasis 23, no. 2 (2016): 155–63. http://dx.doi.org/10.1177/1076029616665922.

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Background: A documented relationship between ovarian cancer and thrombosis does exist. Low-molecular-weight heparins (LMWHs) are cornerstone drugs in the primary prevention and treatment of venous thromboembolic events in patients with cancer. However, cancer cells may alter the efficiency of these antithrombotic agents. Objective: We aimed to characterize the procoagulant phenotype of human epithelial ovarian adenocarcinoma cells, IGROV1, and to compare the capacity of tinzaparin and enoxaparin to inhibit thrombin generation triggered by these cells. Methods: Thrombin generation induced by d

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34

Syed, Daneyal, Debra Hoppensteadt, Daniel Kahn, Job Harenberg, and Jawed Fareed. "Oral Anti-Factor Xa and Factor IIa Agent Mediated Inhibition Of Tissue-Factor Mediated Generation Of Thrombin In Prothrombin Complex Concentrates." Blood 122, no. 21 (2013): 4810. http://dx.doi.org/10.1182/blood.v122.21.4810.4810.

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Introduction Several oral anti-factor IIa and factor Xa agents have recently been developed. These include the thrombin inhibitors Ximelagatran/Melagatran (M) and Dabigatran Etexilate/Dabigatran (D), which require endogenous conversion to the active agents D and M. The factor Xa inhibitors, Rivaroxaban (R) and Apixaban (A), are anti-Xa agents that do not require any endogenous activation. Ximelagatran was withdrawn from the market due to adverse reactions. Dabigatran, Rivaroxaban, and Apixaban are approved for various clinical indications. Antagonism of the anticoagulant effect may be required

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35

Sheu, Meei-Ling, Liang-Yi Pan, Cheng-Ning Yang, et al. "Neuronal Death Caused by HMGB1-Evoked via Inflammasomes from Thrombin-Activated Microglia Cells." International Journal of Molecular Sciences 24, no. 16 (2023): 12664. http://dx.doi.org/10.3390/ijms241612664.

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Microglial cells are a macrophage-like cell type residing within the CNS. These cells evoke pro-inflammatory responses following thrombin-induced brain damage. Inflammasomes, which are large caspase-1-activating protein complexes, play a critical role in mediating the extracellular release of HMGB1 in activated immune cells. The exact role of inflammasomes in microglia activated by thrombin remains unclear, particularly as it relates to the downstream functions of HMGB1. After receiving microinjections of thrombin, Sprague Dawley rats of 200 to 250 gm were studied in terms of behaviors and imm

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36

Jewell, Megan P., Alexandra Bernal, Christine Baird, Marilyn Manco-Johnson, Dougald M. Monroe, and Keith B. Neeves. "Low Normal Levels of Factor V Enhance Thrombin Generation in Hemophilia a in a Tissue Factor Pathway Inhibitor Independent Manner." Blood 144, Supplement 1 (2024): 2579. https://doi.org/10.1182/blood-2024-210722.

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Background: Low normal levels (50%-75%) of factor V (FV) enhance thrombin generation in hemophilia A (Link, JTH, 2020). A mathematical model of coagulation predicts this observation that can be explained by substrate competition for FXa between FV and FVIII. Alternatively, this observation could be explained by reduced inhibition of TF:FVIIa by TFPIα bound to FV-short. Aims: The objective of this study was to determine whether FXa substrate competition between FV and FVIII explains enhanced thrombin generation with decreasing FV levels independent of TFPIα. Methods: FV and FVIII were immunodep

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Metcalfe, Paul, Alison Goodall, Elaine Gray та Stephen Thomas. "Monoclonal Antibodies against Platelet Membrane Glycoproteins IIb/IIIa and Ibα Inhibit Platelet Dependent Thrombin Generation by Different Mechanisms". Thrombosis and Haemostasis 84, № 07 (2000): 98–103. http://dx.doi.org/10.1055/s-0037-1613975.

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SummaryThe antithrombotic effect of antiplatelet agents is principally due to their anti-aggregatory action, but these agents may also interfere with coagulation. We have investigated the effect of monoclonal antibodies (MAb) to platelet membrane glycoproteins (GP) IIb/IIIa and Iba on thrombin generation.Antibodies to platelet membrane glycoprotein IIb/IIIa (RFGP56 and c7E3) were shown to inhibit platelet-mediated thrombin generation stimulated by both intrinsic and extrinsic methods. An antibody to GP Ibα (RFGP37) also inhibited thrombin generation in these systems.FITC-annexin V was used to

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38

Hourdille, P., M. Hasitz, F. Belloc, and AT Nurden. "Immunocytochemical study of the binding of fibrinogen and thrombospondin to ADP- and thrombin-stimulated human platelets." Blood 65, no. 4 (1985): 912–20. http://dx.doi.org/10.1182/blood.v65.4.912.912.

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Abstract We have used immunogold staining to locate thrombospondin (TSP) on thrombin-activated human platelets, and have compared its distribution with that of fibrinogen (or fibrin) on thrombin- and ADP-stimulated platelets. To do this, isolated platelets were incubated with monospecific antibodies to TSP or fibrinogen (fib) and the bound IgG located with a second antibody adsorbed to gold particles. Thrombin- induced secretion in Tyrode-Ca2+ was followed by both anti-TSP and anti- fib binding, with large clusters of gold particles observed on the platelet surface. Little or no labeling was o

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39

Hourdille, P., M. Hasitz, F. Belloc, and AT Nurden. "Immunocytochemical study of the binding of fibrinogen and thrombospondin to ADP- and thrombin-stimulated human platelets." Blood 65, no. 4 (1985): 912–20. http://dx.doi.org/10.1182/blood.v65.4.912.bloodjournal654912.

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We have used immunogold staining to locate thrombospondin (TSP) on thrombin-activated human platelets, and have compared its distribution with that of fibrinogen (or fibrin) on thrombin- and ADP-stimulated platelets. To do this, isolated platelets were incubated with monospecific antibodies to TSP or fibrinogen (fib) and the bound IgG located with a second antibody adsorbed to gold particles. Thrombin- induced secretion in Tyrode-Ca2+ was followed by both anti-TSP and anti- fib binding, with large clusters of gold particles observed on the platelet surface. Little or no labeling was observed o

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40

Zania, Panagiota, Matthew Papaconstantinou, Christodoulos S. Flordellis, Michael E. Maragoudakis, and Nikos E. Tsopanoglou. "Thrombin mediates mitogenesis and survival of human endothelial cells through distinct mechanisms." American Journal of Physiology-Cell Physiology 294, no. 5 (2008): C1215—C1226. http://dx.doi.org/10.1152/ajpcell.00452.2007.

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Thrombin has been reported to play a pivotal role in the initiation of angiogenesis by indirectly regulating and organizing a network of angiogenic molecules. In addition, it has been proposed that thrombin can directly activate endothelial cell proliferation. However, in this report it was shown that thrombin is a poor growth factor for human endothelial cells, and its modest mitogenic activity is mediated indirectly by the release of heparin-binding epidermal growth factor, subsequent to proteinase-activated receptor 1 (PAR1) activation. On the other hand, it was demonstrated that thrombin i

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41

Doshi, Bhavya, Courtney Cox, Bagirath Gangadharan, Christopher B. Doering, and Shannon L. Meeks. "Factor VIII Supplementation Improves Recombinant VIIa Initiated Thrombin Generation in Hemophilia A Inhibitor Patient Plasmas." Blood 118, no. 21 (2011): 28. http://dx.doi.org/10.1182/blood.v118.21.28.28.

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Abstract Abstract 28 Hemophilia A is an X-linked recessive disorder that is caused by a deficiency or defect of factor VIII (fVIII) coagulant protein. Approximately 20–30% of patients with severe hemophilia A develop antibodies (Abs) against fVIII (inhibitors) following fVIII replacement therapy, which makes bleeding episodes more difficult to control. Patients with inhibitors are treated with fVIII-bypassing agents such as recombinant factor VIIa (rfVIIa) or activated prothrombin-complex concentrate. However for unknown reasons, some patients display poor hemostatic response to bypass therapy

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42

Salvemini, Daniela, Gilberto de Nucci, and John R. Vane. "Superoxide Dismutase Cooperates with Prostacyclin to Inhibit Platelet Aggregation: a Comparative Study in Washed Platelets and Platelet Rich Plasma." Thrombosis and Haemostasis 65, no. 04 (1991): 421–24. http://dx.doi.org/10.1055/s-0038-1648164.

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SummaryThe role of superoxide anions (O2 −) in human platelet aggregation in Krebs’ buffer or plasma was investigated. In indome thacin (10 μM)-treated washed platelets superoxide dismutase (SOD; 60 U/ml) or ferricytochrome c (FCC; 70 μM) inhibited platelet aggregation by thrombin but not that by collagen or ADP. In addition, in indomethacin (10 μM)-treated washed platelets, SOD significantly potentiated the anti-aggregatory activity of prostacyclin (PGI2) or iloprost when thrombin but not collagen was used as the aggregating agent. In platelet rich plasma, SOD (60 U/ml) did not inhibit platel

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43

Yeh, Trai-Ming. "Antibodies in dengue patients contain both anti-thrombotic and pro-fibrinolytic activities (P6359)." Journal of Immunology 190, no. 1_Supplement (2013): 216.4. http://dx.doi.org/10.4049/jimmunol.190.supp.216.4.

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Abstract Dengue virus (DENV) infection may result in severe dengue hemorrhagic fever (DHF). However, the mechanisms that cause hemorrhage in DHF are unclear. In this study, we demonstrated that antibodies against human thrombin were increased in the sera of dengue patients but not in other virus-infected patients. To further characterize the properties of these antibodies, affinity-purified anti-thrombin antibodies (ATA) were collected from DENV patients’ sera by thrombin and protein A/L affinity columns. We found human ATA bound not only to DENV, human thrombin, but also cross-reacted to huma

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Dr., Fahd Fayyaz Dr. Tahir Iqbal Dr.Muhammad Asif Ashiq. "A STUDY ON THE NORMAL LEVEL OF ANTI-THROMBIN IN ADULTS." INDO AMERICAN JOURNAL OF PHARMACEUTICAL SCIENCES 05, no. 11 (2018): 11107–11. https://doi.org/10.5281/zenodo.1476040.

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<strong><em>Objective:</em></strong><em> The aim of this research work is to conclude the antigenic & anti-thrombin functional activation amount in the vigorous males of Pakistan. </em> <strong><em>Methodology:</em></strong><em> This research was conducted from January 2017 to December 2017. Fifty vigorous healthy men who were willing for this case study included in this research work. These participants separated into two different age groups. Tests carried out on those participants to know about the amounts of anti-thrombin with the help of RID (radial immune diffusion). This research wo

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45

Tripodi, A., A. Krachmalnicoff, and P. M. Mannucci. "Characterization of an Abnormal Antithrombin (Milano 2) with Defective Thrombin Binding." Thrombosis and Haemostasis 56, no. 03 (1986): 349–52. http://dx.doi.org/10.1055/s-0038-1661681.

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SummaryFour members of an Italian family (two with histories of venous thromboembolism) had a qualitative defect of antithrombin III reflected by normal antigen concentrations and halfnormal antithrombin activity with or without heparin. Anti-factor Xa activities were consistently borderline low (about 70% of normal). For the propositus’ plasma and serum the patterns of antithrombin III in crossed-immunoelectrophoresis with or without heparin were indistinguishable from those of normal plasma or serum. A normal affinity of antithrombin III for heparin was documented by heparin-sepharose chroma

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46

Sugama, Y., C. Tiruppathi, K. offakidevi, T. T. Andersen, J. W. Fenton, and A. B. Malik. "Thrombin-induced expression of endothelial P-selectin and intercellular adhesion molecule-1: a mechanism for stabilizing neutrophil adhesion." Journal of Cell Biology 119, no. 4 (1992): 935–44. http://dx.doi.org/10.1083/jcb.119.4.935.

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Thrombin-induced expression of endothelial adhesivity toward neutrophils (PMN) was studied using human umbilical vein endothelial cells (HUVEC). HUVEC were challenged with human alpha-thrombin for varying durations up to 120 min, after which the cells were fixed with 1% paraformaldehyde and 51Cr-labeled human PMN were added to determine PMN adhesion. Endothelial adhesivity increased within 15 min after alpha-thrombin exposure, and the response persisted up to 120 min. Expression of endothelial adhesion proteins, P-selectin (GMP-140, PADGEM, CD62), and intercellular adhesion molecule-1 (ICAM-1;

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47

Moneta, Gregory, Jeffrey Ballard, Carlton Randleman, Kenneth Renkens, Neil Singla, and W. Allan Alexander. "Favorable Immunologic Response to Recombinant Thrombin Application in Surgery among Subjects with Pre-Existing Antibodies to Bovine Thrombin." Blood 112, no. 11 (2008): 3390. http://dx.doi.org/10.1182/blood.v112.11.3390.3390.

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Abstract Recombinant thrombin (rThrombin) is an active topical hemostat that is approved by the FDA as an aid to hemostasis. The safety, immunogenicity, and efficacy of rThrombin have been demonstrated in 1 Phase 1 study, 5 Phase 2 studies, and 1 randomized, double-blind Phase 3 study. No safety observations have been deemed clearly causally related to exposure to rThrombin; favorable immunologic response to rThrombin was observed in these trials. Treatment with thrombin derived from bovine sources has occasionally been associated with adverse events which appear to be related to the formation

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48

Le Guyader, Maïlys, Mohammed Kaabar, Pierre Lemaire, and Fabienne Pineau Vincent. "Thrombin time and anti-IIa dabigatran's activity: hypothesis of thrombin time's predictive value." Annales de biologie clinique 73, no. 5 (2015): 544–46. http://dx.doi.org/10.1684/abc.2015.1072.

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49

Liu, Jun T., William Paul, Michael Emerson, Carla Cicala, and Clive P. Page. "Thrombin inhibitors and anti-coagulants on thrombin-induced embolisation in rabbit cranial vasculature." European Journal of Pharmacology 264, no. 2 (1994): 183–90. http://dx.doi.org/10.1016/0014-2999(94)00464-1.

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50

Caunt, Maresa, Liang Hu, Thomas Tang, Peter C. Brooks та Simon Karpatkin. "Growth Regulated Oncogene (GRO-α) Is Pivotal in Thrombin-Induced Angiogenesis." Blood 106, № 11 (2005): 530. http://dx.doi.org/10.1182/blood.v106.11.530.530.

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Abstract The mechanism of thrombin-induced angiogenesis is poorly understood. Using a gene chip array to investigate the pro-malignant phenotype of thrombin-stimulated cells we observed that thrombin (0.5–1 u/ml/24 hr) upregulates GRO-α 168 fold in an undifferentiated mouse cell line (UMCL). Thrombin-induced GRO-α upregulation was also observed in several tumor cell lines [murine B16F10 melanoma and 4T1 breast CA, human DU145 and PC3 prostate CA, human MCF7 breast CA, as well as human umbilical vein (HUVEC) and brain microvascular endothelial cells] by mRNA and protein analysis. Thrombin enhan

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