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Journal articles on the topic 'Thrombin inhibitor'

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Published: 4 June 2021

Last updated: 6 February 2022

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1

Pahl, M. V., N. D. Vaziri, F. Oveisi, J. Wang, and Y. Ding. "Antithrombin III inhibits mesangial cell proliferation." Journal of the American Society of Nephrology 7, no. 10 (1996): 2249–53. http://dx.doi.org/10.1681/asn.v7102249.

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Thrombin stimulates and heparin and heparan sulfate inhibit mesangial cell proliferation. In addition, heparin has been shown to inhibit thrombin-stimulated smooth muscle cell proliferation. The anticoagulant action of heparin is mediated by antithrombin III. This study investigated whether heparin's antiproliferative action is also mediated by antithrombin III. To this end, the effect of antithrombin III on thrombin-stimulated mesangial cell growth was examined. As expected, thrombin stimulated DNA synthesis and cell growth in cultured human mesangial cells. The effect of thrombin on DNA synt

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2

Glusa, Erika, Ellen Bretschneider, Joachim Daum, and Christiane Noeske-Jungblut. "Inhibition of Thrombin-mediated Cellular Effects by Triabin, a Highly Potent Anion-binding Exosite Thrombin Inhibitor." Thrombosis and Haemostasis 77, no. 06 (1997): 1196–200. http://dx.doi.org/10.1055/s-0038-1656137.

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SummaryTriabin, a 17 kDa protein from the saliva of the assassin bug Triatoma pallidipennis is a potent thrombin inhibitor interfering with the anion-binding exosite of the enzyme. The recombinant protein, produced by the baculovirus/insect cell system, was used to study the inhibitory effect on thrombin-mediated cellular responses. The thrombin (1 nM)-stimulated aggregation of washed human platelets and the rise in cytoplasmic calcium in platelets were inhibited by triabin at nanomolar concentrations. In contrast, the rise in calcium induced by the thrombin receptor-activating peptide (10 μM)

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3

Bagdy, Dániel, Gabriella Szabó, Éva Barabás, and Sándor Bajusz. "Inhibition by D-MePhe-Pro-Arg-H (GYKI-14766) of Thrombus Growth in Experimental Models of Thrombosis." Thrombosis and Haemostasis 68, no. 02 (1992): 125–29. http://dx.doi.org/10.1055/s-0038-1656336.

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SummaryThe antithrombotic action of the highly effective synthetic thrombin inhibitor D-MePhe-Pro-Arg-H (GYKI-14766) was studied in various models of experimental thrombosis. The compound administered to rats and rabbits by i. v. bolus injections, continuous i. v. infusions, subcutaneously and orally, respectively, induced significant decrease in thrombus weight (i) in a quantitative venous thrombosis model with stasis based on vascular lesion in rats, (ii) in an extracorporeal arterio-venous shunt model in rabbits, and (iii) prevented the occlusion of the vessel in arterial thrombosis induced

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4

Wang, Wei-Ya, Chien-Kei Wei, Che-Ming Teng, and Chin-Chung Wu. "Combined blockade of thrombin anion binding exosite-1 and PAR4 produces synergistic antiplatelet effect in human platelets." Thrombosis and Haemostasis 105, no. 01 (2011): 88–95. http://dx.doi.org/10.1160/th10-05-0305.

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SummaryThrombin exosite-1 mediates the specific binding of thrombin with fibrinogen and protease-activated receptor (PAR) 1. Exosite-1 inhibitors have been shown to effectively decrease the clotting activity of thrombin, while their antiplatelet effects are relatively weak. In the present study, the inhibitory effects of two exosite-1 inhibitors, hirugen and HD1, but not the exosite-2 inhibitor HD22, on thrombin-induced platelet aggregation and P-selectin expression were dramatically enhanced by a PAR4 antagonist, YD-3. In contrast, the PAR1 antagonist SCH-79797 did not affect the antiplatelet

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5

Lunven, Catherine, Christiane Gauffeny, Catherine Lecoffre, Donogh P. O’Brien, Nigel O. Roome, and Christopher N. Berry. "Inhibition by Argatroban, a Specific Thrombin Inhibitor, of Platelet Activation by Fibrin Clot-associated Thrombin." Thrombosis and Haemostasis 75, no. 01 (1996): 154–69. http://dx.doi.org/10.1055/s-0038-1650236.

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SummaryClot-associated thrombin retains amidolytic activity, and is resistant to inhibition by heparin, but not to low molecular weight thrombin inhibitors. We show that clot-associated thrombin induces platelet aggregation, is resistant to heparin:antithrombin III, less so to recombinant hirudin (rHV2Lys47) but not to argatroban, an active-site directed thrombin inhibitor. Fibrin clots prepared with human fibrinogen and thrombin were used to aggregate rabbit washed platelets assessed by single platelet counting, thromboxane B2 (TXB2) immunoassay and scanning electron microscopy. Fibrin clots

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6

Kaminski, M., and J. McDonagh. "Inhibited thrombins. Interactions with fibrinogen and fibrin." Biochemical Journal 242, no. 3 (1987): 881–87. http://dx.doi.org/10.1042/bj2420881.

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Fibrin-monomer-Sepharose was used to study thrombin binding to fibrin and the role of the enzyme active centre in this interaction. Binding properties of preformed enzyme-inhibitor complexes, as well as inhibition of thrombin already adsorbed to fibrin monomer, were investigated. No apparent difference was found in binding properties of phenylmethanesulphonyl fluoride-, D-Phe-Pro-Arg-CH2Cl- and dansylarginine NN-(3-ethylpentane-1,5-diyl)amide-inhibited thrombins. Also, the elution profile of phenylmethane-sulphonyl fluoride-inhibited thrombin from fibrinogen-Sepharose was identical with that o

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7

Finkle, Carolyn, Annie Pierre, Lorraine Leblond, Isabelle Deschenes, John DiMaio, and Peter Winocour. "BCH-2763, a Novel Potent Parenteral Thrombin Inhibitor, Is an Effective Antithrombotic Agent in Rodent Models of Arterial and Venous Thrombosis – Comparisons with Heparin, r-Hirudin, Hirulog, Inogatran and Argatroban." Thrombosis and Haemostasis 79, no. 02 (1998): 431–38. http://dx.doi.org/10.1055/s-0037-1615003.

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SummaryCurrent clinical use of heparin as an antithrombotic agent is limited by suboptimal efficacy and safety considerations. Thrombin’s central role in thrombosis makes it an attractive target to develop more effective and safer antithrombotic agents. BCH-2763 is a novel, potent (Ki: 0.11 nM), low molecular weight (1.51 kDa), bivalent direct thrombin inhibitor. The antithrombotic efficacy of BCH-2763 in vivo following i.v. bolus plus infusion in rats was compared in arterial and venous thrombosis models with two other bivalent direct thrombin inhibitors, r-hirudin and hirulog, with two catal

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8

Hashimoto, Masaru, Tsutomu Yamashita, Kazuhiro Oiwa, Sadahiro Watanabe, John Giddings, and Junichiro Yamamoto. "Enhancement of Endogenous Plasminogen Activator-induced Thrombolysis by Argatroban and APC and Its Control by TAFI, Measured in An Arterial Thrombolysis Model In Vivo Using Rat Mesenteric Arterioles." Thrombosis and Haemostasis 87, no. 01 (2002): 110–13. http://dx.doi.org/10.1055/s-0037-1612952.

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SummaryRecent in vitro studies have demonstrated that thrombin inhibits fibrinolysis through thrombin-activatable fibrinolysis inhibitor (TAFI, plasma procarboxypeptidase B). We have recently shown that endogenous fibrinolysis in vivo is enhanced by activated protein C (APC) and the selective thrombin inhibitor, argatroban. The aim of the present study was to examine the role of TAFI in these fibrinolytic mechanisms in vivo using purified porcine pancreatic carboxypeptidase B (PPCPB) and a specific TAFIa inhibitor, potato tuber carboxypeptidase B inhibitor (PTCI) in a newly established arteria

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9

Li, WX, AV Kaplan, GW Grant, JJ Toole, and LL Leung. "A novel nucleotide-based thrombin inhibitor inhibits clot-bound thrombin and reduces arterial platelet thrombus formation." Blood 83, no. 3 (1994): 677–82. http://dx.doi.org/10.1182/blood.v83.3.677.677.

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Abstract A novel thrombin inhibitor based on single-stranded (ss) deoxynucleotides with the sequence GGTTGGTGTGGTTGG (thrombin aptamer) has been recently discovered. In this study, we tested its efficacy in inhibiting clot-bound thrombin activity and platelet thrombus formation in an ex vivo whole artery angioplasty model. The thrombin aptamer showed a specific dose-dependent inhibition of thrombin-induced platelet aggregation (0.5 U/mL) in human platelet-rich plasma, with an IC50 of approximately 70 to 80 nmol/L. In an in vitro clot-bound thrombin assay system, heparin, used at clinically rel

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10

Li, WX, AV Kaplan, GW Grant, JJ Toole, and LL Leung. "A novel nucleotide-based thrombin inhibitor inhibits clot-bound thrombin and reduces arterial platelet thrombus formation." Blood 83, no. 3 (1994): 677–82. http://dx.doi.org/10.1182/blood.v83.3.677.bloodjournal833677.

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A novel thrombin inhibitor based on single-stranded (ss) deoxynucleotides with the sequence GGTTGGTGTGGTTGG (thrombin aptamer) has been recently discovered. In this study, we tested its efficacy in inhibiting clot-bound thrombin activity and platelet thrombus formation in an ex vivo whole artery angioplasty model. The thrombin aptamer showed a specific dose-dependent inhibition of thrombin-induced platelet aggregation (0.5 U/mL) in human platelet-rich plasma, with an IC50 of approximately 70 to 80 nmol/L. In an in vitro clot-bound thrombin assay system, heparin, used at clinically relevant con

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11

Li, Zhenyu, Guoying Zhang, Robert Feil, Jiahuai Han та Xiaoping Du. "Sequential activation of p38 and ERK pathways by cGMP-dependent protein kinase leading to activation of the platelet integrin αIIbβ3". Blood 107, № 3 (2006): 965–72. http://dx.doi.org/10.1182/blood-2005-03-1308.

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AbstractIntegrin activation (inside-out signaling) in platelets can be initiated by agonists such as von Willebrand factor (VWF) and thrombin. Here we show that a mitogen-activated protein kinase (MAPK), p38, plays an important role in the activation of integrin αIIbβ3 induced by VWF and thrombin. A dominant-negative mutant of p38, p38AF, inhibits αIIbβ3 activation induced by VWF binding to its receptor, the platelet glycoprotein Ib-IX (GPIb-IX), and p38 inhibitors diminish platelet aggregation induced by VWF or low-dose thrombin. The inhibitory effect of p38 inhibitor is unlikely to be caused

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12

Tesfamariam, B., G. T. Allen, D. Normandin, and M. J. Antonaccio. "Involvement of the "tethered ligand" receptor in thrombin-induced endothelium-mediated relaxations." American Journal of Physiology-Heart and Circulatory Physiology 265, no. 5 (1993): H1744—H1749. http://dx.doi.org/10.1152/ajpheart.1993.265.5.h1744.

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The mechanisms by which the serine protease, alpha-thrombin, mediates relaxations were examined in isolated dog and pig coronary arteries and dog saphenous veins. In rings of coronary arteries and saphenous veins contracted submaximally with prostaglandin F2 alpha or U46619, alpha-thrombin (0.1-10 nM) caused relaxations that were abolished by treatment with N omega-nitro-L-arginine (L-NNA) or removal of the endothelium, indicating that the relaxations were mediated by endothelium-derived nitric oxide. These relaxations were blocked by the thrombin active site inhibitor, MD-805, indicating the

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13

Tang, Xiaopeng, Mengrou Chen, Zilei Duan, James Mwangi, Pengpeng Li, and Ren Lai. "Isolation and Characterization of Poecistasin, an Anti-Thrombotic Antistasin-Type Serine Protease Inhibitor from Leech Poecilobdella manillensis." Toxins 10, no. 11 (2018): 429. http://dx.doi.org/10.3390/toxins10110429.

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Antistasin, first identified as a potent inhibitor of the blood coagulation factor Xa, is a novel family of serine protease inhibitors. In this study, we purified a novel antistasin-type inhibitor from leech Poecilobdella manillensis called poecistasin. Amino acid sequencing of this 48-amino-acid protein revealed that poecistasin was an antistasin-type inhibitor known to consist of only one domain. Poecistasin inhibited factor XIIa, kallikrein, trypsin, and elastase, but had no inhibitory effect on factor Xa and thrombin. Poecistasin showed anticoagulant activities. It prolonged the activated

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14

Schmidt, Barbara, Lesley Mitchell, Frederick A. Ofosu, and Maureen Andrew. "Alpha-2-Macroglobulin Is an Important Progressive Inhibitor of Thrombin in Neonatal and Infant Plasma." Thrombosis and Haemostasis 62, no. 04 (1989): 1074–77. http://dx.doi.org/10.1055/s-0038-1647120.

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SummaryAntithrombin III (ATIII) is the main inhibitor of thrombin in adult plasma; α2-macroglobulin (α2M) and heparin cofactor II (HCII) are of lesser importance. The relative contributions of these inhibitors to the inactivation of thrombin may differ during the neonatal period and infancy, when plasma concentrations of α2M are about twice as high as those of ATIII. We therefore compared the relative importance of these anti-proteases for the inhibition of 125I-thrombin in defibrinated pooled adult and neonatal plasma. Observations were also made in pooled plasma of 6 months old infants. 125I

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15

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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16

Suzuki, Makoto, Emika Sugimoto, Minako Sata, Syuji Yamamoto, Ikuro Maruyama, and Mitsunobu Mohri. "Effects of Recombinant Human Soluble Thrombomodulin (rhs-TM) on Clot-induced Coagulation in Human Plasma." Thrombosis and Haemostasis 80, no. 12 (1998): 925–29. http://dx.doi.org/10.1055/s-0037-1615390.

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SummaryRecent studies have suggested that clot-bound thrombin plays an important role in thrombus growth. In this study, we examined the effects of recombinant human soluble thrombomodulin (rhsTM) on clot-induced coagulation. rhsTM enhanced the activation of protein C by clots, and attenuated clot-induced thrombin generation and fibrinopep-tide A (FPA) production in a dose-dependent manner. The inhibitory effect of rhsTM was abolished by anti-protein C antibody. The inhibitory effect of rhsTM on clot-induced thrombin generation continued for over 60 min after the addition of the clot, while an

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17

Witting, J. I., P. Bourdon, D. V. Brezniak, J. M. Maraganore, and J. W. Fenton. "Thrombin-specific inhibition by and slow cleavage of hirulog-1." Biochemical Journal 283, no. 3 (1992): 737–43. http://dx.doi.org/10.1042/bj2830737.

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Hirulog-1 [D-Phe-Pro-Arg-Pro-[Gly]4-desulphohirudin-(53-64) (HV1)] was designed to bind by its first four and last 12 residues to the alpha-thrombin catalytic site and anion-binding exosite for fibrin(ogen) recognition respectively, with a [Gly]4 bridge and an Arg-Pro bond at the scissional position. Human alpha-, gamma- and zeta-thrombins, as well as bovine trypsin, readily hydrolyse Spectrozyme-TH (D-hexahydrotyrosyl-Ala-Arg p-nitroanilide) at pH 7.4 and approx. 23 degrees C. Both alpha- and zeta-thrombins, which have high fibrinogen-clotting activities (greater than 3000 kunits/g), were inh

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18

Aschner, J. L., J. M. Lennon, J. W. Fenton, M. Aschner, and A. B. Malik. "Enzymatic activity is necessary for thrombin-mediated increase in endothelial permeability." American Journal of Physiology-Lung Cellular and Molecular Physiology 259, no. 4 (1990): L270—L275. http://dx.doi.org/10.1152/ajplung.1990.259.4.l270.

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alpha-Thrombin causes a dose-dependent increase in endothelial permeability as measured by the clearance rate of 125I-albumin across a monolayer of bovine pulmonary artery endothelial cells. We determined if an active catalytic site is necessary for the thrombin-mediated increase in endothelial permeability. alpha-Thrombin was reacted with 10-fold excess D-phenylalanyl-prolyl-arginine chloromethyl ketone (PPACK), an irreversible inhibitor that forms a covalent bond with thrombin's active site, producing an enzymatically inactive thrombin. PPACK completely inhibited the alpha-thrombin-mediated

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Prasa, D., L. Svendsen, and J. Stürzebecher. "Inhibition of Thrombin Generation in Plasma by Inhibitors of Factor Xa." Thrombosis and Haemostasis 78, no. 04 (1997): 1215–20. http://dx.doi.org/10.1055/s-0038-1657717.

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SummaryA series of inhibitors of factor Xa (FXa) were investigated using the thrombin generation assay to evaluate the potency and specificity needed to efficiently block thrombin generation in activated human plasma. By inhibiting FXa the generation of thrombin in plasma is delayed and decreased. Inhibitor concentrations which cause 50 percent inhibition of thrombin generation (IC50) correlate in principle with the Ki values for inhibition of free FXa. Recombinant tick anticoagulant peptide (r-TAP) is able to inhibit thrombin generation with considerably low IC50 values of 49 nM and 37 nM for

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Muldowney III, James, Corrie Painter, Elaine Sanders-Bush, Nancy Brown та Douglas Vaughan. "Acute tissue-type plasminogen activator release in human microvascular endothelial cells: The roles of Gαq, PLC-β, IP3 and 5,6-epoxyeicosatrienoic acid". Thrombosis and Haemostasis 97, № 02 (2007): 263–71. http://dx.doi.org/10.1160/th05-02-0092.

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SummaryThe acute physiologic release of tissue-type plasminogen activator (t-PA) from the endothelium is critical for vascular homeostasis. This process is prostacyclin- and nitric oxide (NO)-independent in humans. It has been suggested that calcium signaling and endothelial-derived hyperpolarizing factors (EDHF) may play a role in t-PA release. G-protein-coupled receptor-dependent calcium signaling is typically Gαq -dependent. EDHFs have been functionally defined and in various tissues are believed to be various regioisomers of the epoxyeicosatrienoic acids (EETs). We tested the hypothesis in

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21

Lewis, Sidney, Dale Lehman, Stephen Gardell, Sherri Motzel, Joseph Lynch, and Elizabeth Marsh Lyle. "Assessment of Thrombin Inhibitor Efficacy in a Novel Rabbit Model of Simultaneous Arterial and Venous Thrombosis." Thrombosis and Haemostasis 79, no. 03 (1998): 656–62. http://dx.doi.org/10.1055/s-0037-1614962.

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SummaryThe importance of thrombin in arterial and venous thrombosis renders thrombin inhibition an important therapeutic target. Identification of novel inhibitors requires an appropriate animal model. We modified a previously reported rat arterial thrombosis model to allow simultaneous assessment of the arterial and venous antithrombotic efficacies of heparin, hirudin, hirulog, a novel thrombin inhibitor H-(N-Me-D-Phe)-Pro-L-trans-4-aminocyclohexyl-Gly-[CO-CO]-NHCH3 (L-370,518) and the factor Xa inhibitor tick anticoagulant peptide in rabbits. Thrombosis was induced through application of 70%

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22

Hérault, J. P., F. Dol, C. Gaich, A. Bernat, and J. M. Herbert. "Effect of Clopidogrel on Thrombin Generation in Platelet-Rich Plasma in the Rat." Thrombosis and Haemostasis 81, no. 06 (1999): 957–60. http://dx.doi.org/10.1055/s-0037-1614606.

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SummaryClopidogrel (25 mg/kg, p.o.), a potent and selective inhibitor of ADP-induced platelet aggregation, significantly inhibited, in the presence of platelets, ex vivo thrombin generation triggered by low concentrations of tissue factor. Clopidogrel reduced the area under the curve (23%, p <0.05) and the thrombin peak concentration (35%, p <0.05) but did not affect the lag phase of thrombin generation. Under the same experimental conditions, heparin (100 μg/ml) inhibited thrombin generation mostly by delaying and by reducing the burst of thrombin. In a stasis-induced venous thrombosis

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23

Declerck, P. J. "Thrombin activatable fibrinolysis inhibitor." Hämostaseologie 31, no. 03 (2011): 165–73. http://dx.doi.org/10.5482/ha-1155.

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SummaryThrombin activatable fibrinolysis inhibitor (TAFI) was discovered two decades ago as a consequence of the identification of an unstable carboxypeptidase (CPU), which was formed upon thrombin activation of the respective pro-enzyme (proCPU). The antifibrinolytic function of the activated form (TAFIa, CPU) is directly linked to its capacity to remove C-terminal lysines from the surface of the fibrin clot. No endogenous inhibitors have been identified, but TAFIa activity is regulated by its intrinsic temperature-dependent instability with a half-life of 8 to 15 min at 37 °C. A variety of s

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24

Tapparelli, Carlo, Rainer Metternich, Patrick Gfeller, Bernhard Gafner, and Michael Powling. "Antithrombotic Activity in vivo of SDZ 217-766, a Low-molecular Weight Thrombin Inhibitor in Comparison to Heparin." Thrombosis and Haemostasis 73, no. 04 (1995): 641–47. http://dx.doi.org/10.1055/s-0038-1653834.

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SummaryAntithrombotic potency of SDZ 217-766, a potent inhibitor of thrombin and other trypsin-like serine proteases, was studied in comparison with heparin in rat models of thrombin induced lung platelet accumulation, of thrombosis in arterio-venous shunt, and of venous thrombosis induced by tissue factor. Thrombin-induced platelet accumulation in the lung was inhibited dose-dependently by SDZ 217-766 following intravenous (i.v.) administration of 0.03 mg/kg to 0.3 mg/kg as well as by intraduodenal (i.d.) administration of 3 mg/kg and 10 mg/kg. Comparable inhibitory effects were observed with

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25

Mende, Katrin, Goetz Nowak, and Mercedes López. "Improvement of the specificity of dipetarudin by site directed mutagenesis." Thrombosis and Haemostasis 93, no. 03 (2005): 430–36. http://dx.doi.org/10.1160/th04-08-0480.

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SummaryProtease specificity is crucial to the design of thrombin inhibitors as inhibition of other physiologically relevant serine-proteases can compromise their clinical use. Dipetarudin, a potent thrombin inhibitor, also inhibits trypsin and plasmin. Due to the specificity of an inhibitor being influenced by the amino acid residue at the P1 position, we replaced the Arg10 at P1 position of dipetarudin by a histidine, which is the P1 residue of rhodniin, a very specific thrombin inhibitor. The amino acid replacement was carried out by site directed mutagenesis. The mutant, dipetarudin R10H, s

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Parker, Andrew, and William Fay. "Effects of Radiographic Contrast Agents on Thrombin Formation and Activity." Thrombosis and Haemostasis 80, no. 08 (1998): 266–72. http://dx.doi.org/10.1055/s-0037-1615186.

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SummaryClinical trials suggest that the risk of thrombosis during coronary angioplasty is lower with ionic contrast agents than with nonionic contrast agents. However, the molecular mechanisms underlying this effect are unknown. This study examined the effects of contrast agents on thrombin formation and its interaction with substrates, inhibitors, and ligands to define potential mechanisms by which contrast agents affect thrombus formation. Two ionic agents, diatrizoate and ioxaglate, and one nonionic agent, ioversol, were studied. Ionic agents inhibited factor X activation by the tissue fact

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27

Atarashi, Hirotsugu. "Thrombin Inhibitor or Factor Xa Inhibitor?" Circulation Journal 75, no. 8 (2011): 1819–20. http://dx.doi.org/10.1253/circj.cj-11-0564.

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28

Kaiser, Brigitte. "State-of-the-Art Review: Factor Xa Versus Factor IIa Inhibitors." Clinical and Applied Thrombosis/Hemostasis 3, no. 1 (1997): 16–24. http://dx.doi.org/10.1177/107602969700300102.

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The development of specific inhibitors of blood coagulation enzymes has led to a number of new anticoagulant/antithrombotic agents that could be useful for prophylaxis and/or treatment of thromboembolic disorders. Because thrombin is the central bioregulatory enzyme in hemostasis, blocking of the active site of the enzyme by a fast reaction with an inhibitor may effectively prevent intravascular coagulation as well as other important biological effects of thrombin. For the direct inactivation of thrombin, several classes of compounds have been developed and characterized in vitro and in vivo a

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29

Horgan, M. J., J. W. Fenton, and A. B. Malik. "Alpha-thrombin-induced pulmonary vasoconstriction." Journal of Applied Physiology 63, no. 5 (1987): 1993–2000. http://dx.doi.org/10.1152/jappl.1987.63.5.1993.

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We examined the direct effects of thrombin on pulmonary vasomotor tone in isolated guinea pig lungs perfused with Ringer albumin (0.5% g/100 ml). The injection of alpha-thrombin (the native enzyme) resulted in rapid dose-dependent increases in pulmonary arterial pressure (Ppa) and pulmonary capillary pressure (Ppc), which were associated with an increase in the lung effluent thromboxane B2 concentration. The Ppa and Ppc responses decreased with time but then increased again within 40 min after thrombin injection. The increases in Ppc were primarily the result of postcapillary vasoconstriction.

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30

Hecquet, Claudie, Dauren Biyashev, Fulong Tan, and Ervin G. Erdös. "Positive cooperativity between the thrombin and bradykinin B2 receptors enhances arachidonic acid release." American Journal of Physiology-Heart and Circulatory Physiology 290, no. 3 (2006): H948—H958. http://dx.doi.org/10.1152/ajpheart.00868.2005.

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Bradykinin (BK) or kallikreins activate B2 receptors (R) that couple Gαi and Gαq proteins to release arachidonic acid (AA) and elevate intracellular Ca2+ concentration ([Ca2+]i). Thrombin cleaves the protease-activated-receptor-1 (PAR1) that couples Gαi, Gαq, and Gα12/13 proteins. In Chinese hamster ovary cells stably transfected with human B2R, thrombin liberated little AA, but it significantly potentiated AA release by B2R agonists. We explored mechanisms of cooperativity between constitutively expressed PAR1 and B2R. We also examined human endothelial cells expressing both Rs constitutively

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31

Nakamura, K., M. Kimura, J. W. Fenton, T. T. Andersen, and A. Aviv. "Duality of plasmin effect on cytosolic free calcium in human platelets." American Journal of Physiology-Cell Physiology 268, no. 4 (1995): C958—C967. http://dx.doi.org/10.1152/ajpcell.1995.268.4.c958.

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Plasmin caused a modest and gradual increase in platelet cytosolic Ca2+, mediated through both Ca2+ mobilization and external Ca2+ entry. This response was associated with accelerated Ca2+ extrusion and protein tyrosine phosphorylation. Plasmin-enhanced external Ca2+ entry and Ca2+ extrusion (but not Ca2+ mobilization) were attenuated by the tyrosine kinase inhibitor, genistein. Plasmin inhibited the thrombin-evoked increase in cytosolic Ca2+ and also inhibited the Ca2+ response to the tethered peptide TRAP-6 of the thrombin receptor. Furthermore, plasmin inhibited the binding of 125I-labeled

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32

Olson, Steven T., Richard Swanson, and Maurice Petitou. "Specificity and selectivity profile of EP217609: a new neutralizable dual-action anticoagulant that targets thrombin and factor Xa." Blood 119, no. 10 (2012): 2187–95. http://dx.doi.org/10.1182/blood-2011-09-381764.

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Abstract EP217609 is a new dual-action parenteral anticoagulant that combines an indirect factor Xa inhibitor (fondaparinux analog) and a direct thrombin inhibitor (α-NAPAP analog) in a single molecule together with a biotin tag to allow avidin neutralization. EP217609 exhibits an unprecedented pharmacologic profile in showing high bioavailability, long plasma half-life, and potent antithrombotic activity in animals without the complications of thrombin rebound. Here we report the exceptional specificity and selectivity profile of EP217609. EP217609 inhibited thrombin with rapid kinetics (kon

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Lewis, B. E., W. P. Jeske, F. Leya, et al. "Combined Thrombin and Platelet Inhibition Treatment for HIT Patients." Hämostaseologie 19, no. 03 (1999): 128–33. http://dx.doi.org/10.1055/s-0038-1660400.

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SummaryDespite the use of potent anticoagulants such as r-hirudin and argatroban, the morbidity and mortality in heparin-induced thrombocytopenia (HIT) patients remains unacceptable. Data from our in vitro investigations show that thrombin inhibitors do not block platelet activation induced by heparin antibodies and heparin but that GPIIb/IIIa receptor inhibitors do block this process. We have treated four HIT positive patients with a combined therapy of thrombin inhibitor and GPIIb/IIIa receptor inhibitor when treatment with thrombin inhibitor alone failed to alleviate acute thrombosis. Combi

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Zhang, Wei, Gary Nale, and Robert W. Colman. "Thrombin Regulates the Camp Level in Human Platelets through Phosphorylation /Activation of Akt." Blood 104, no. 11 (2004): 3538. http://dx.doi.org/10.1182/blood.v104.11.3538.3538.

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Abstract Phosphorylation /activation of Akt is a critical event in platelet activation stimulated by thrombin. We previous demonstrated that the activation of PDE3A was increased concomitantly with the phosphorylation /activation of Akt. In order to demonstrate a link between these two events, in this study, we monitored thrombin-induced cAMP changes in washed platelets. We confirmed that the platelet cAMP level decreased following thrombin stimulation. The thrombin-induced decrease of cAMP was inhibited by an Akt specific inhibitor (1l-6-hydroxymethyl-chiro-inositol 2-(R)-2-O-methyl-3-O-octad

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Marx, Pauline. "Thrombin-Activatable Fibrinolysis Inhibitor." Current Medicinal Chemistry 11, no. 17 (2004): 2335–48. http://dx.doi.org/10.2174/0929867043364586.

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Koh, Cho Yeow, Maria Kazimirova, Patricia A. Nuttall, and R. Manjunatha Kini. "Noncompetitive Inhibitor of Thrombin." ChemBioChem 10, no. 13 (2009): 2155–58. http://dx.doi.org/10.1002/cbic.200900371.

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DeAnda, A., S. Coutré, and D. C. Miller. "Synthetic peptide thrombin inhibitor." Circulation 90, no. 3 (1994): 1581–82. http://dx.doi.org/10.1161/01.cir.90.3.1581.

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Gapsys, Vytautas, and Bert de Groot. "Computational Thrombin Inhibitor Optimization." Biophysical Journal 106, no. 2 (2014): 262a—263a. http://dx.doi.org/10.1016/j.bpj.2013.11.1538.

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Yildirim, M. N., Y. Selcoki, S. Uysal, et al. "Thrombin activatable fibrinolysis inhibitor." Herz 39, no. 8 (2013): 993–1000. http://dx.doi.org/10.1007/s00059-013-3942-8.

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Hua, Ya, Guohua Xi, Richard F. Keep, Jimin Wu, Yajun Jiang, and Julian T. Hoff. "Plasminogen Activator Inhibitor-1 Induction after Experimental Intracerebral Hemorrhage." Journal of Cerebral Blood Flow & Metabolism 22, no. 1 (2002): 55–61. http://dx.doi.org/10.1097/00004647-200201000-00007.

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Serine proteases, such as thrombin and tissue-type plasminogen activator, play an important role in brain injury after intracerebral hemorrhage and other neurologic disorders. Plasminogen activator inhibitor-1 is one of the serine protease inhibitors, or serpins. The balance between serine proteases and serpins may affect the outcome of intracerebral hemorrhage. The purpose of this study was to determine whether plasminogen activator inhibitor-1 and tissue-type plasminogen activator are upregulated after intracerebral hemorrhage and the role that thrombin plays in that induction. Plasminogen a

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Jalink, K., and W. H. Moolenaar. "Thrombin receptor activation causes rapid neural cell rounding and neurite retraction independent of classic second messengers." Journal of Cell Biology 118, no. 2 (1992): 411–19. http://dx.doi.org/10.1083/jcb.118.2.411.

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The protease thrombin is a potent activator of various cell types. Thrombin cleaves and thereby activates its own seven-transmembrane-domain receptor which couples to G proteins. Thrombin also can inhibit neuronal differentiation, supposedly by degrading components of the extracellular matrix. Here we report that active thrombin induces immediate cell rounding and neurite retraction in differentiating N1E-115 and NG108-15 neural cells in serum-free culture. Serum (0.5-5% vol/vol) evokes similar responses, but the cell-rounding and neurite-retracting activity of serum is not attributable to thr

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Kwon, Hyuk-Woo, Jung-Hae Shin, Dong-Ha Lee, and Hwa-Jin Park. "Inhibitory Effects of Cytosolic Ca2+Concentration by Ginsenoside Ro Are Dependent on Phosphorylation of IP3RI and Dephosphorylation of ERK in Human Platelets." Evidence-Based Complementary and Alternative Medicine 2015 (2015): 1–13. http://dx.doi.org/10.1155/2015/764906.

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Intracellular Ca2+([Ca2+]i) is platelet aggregation-inducing molecule and is involved in activation of aggregation associated molecules. This study was carried out to understand the Ca2+-antagonistic effect of ginsenoside Ro (G-Ro), an oleanane-type saponin inPanax ginseng. G-Ro, without affecting leakage of lactate dehydrogenase, dose-dependently inhibited thrombin-induced platelet aggregation, and the half maximal inhibitory concentration was approximately 155 μM. G-Ro inhibited strongly thrombin-elevated[Ca2+]i, which was strongly increased by A-kinase inhibitor Rp-8-Br-cAMPS compared to G-

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Walsh, Peter N., and Syed S. Ahmad. "Proteases in blood clotting." Essays in Biochemistry 38 (October 1, 2002): 95–111. http://dx.doi.org/10.1042/bse0380095.

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The serine proteases, cofactors and cell-receptor molecules that comprise the haemostatic mechanism are highly conserved modular proteins that have evolved to participate in biochemical reactions in blood coagulation, anticoagulation and fibrinolysis. Blood coagulation is initiated by exposure of tissue factor, which forms a complex with factor VIIa and factor X, which results in the generation of small quantities of thrombin and is rapidly shutdown by the tissue factor pathway inhibitor. The generation of these small quantities of thrombin then activates factor XI, resulting in a sequence of

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Hofsteenge, J., H. Taguchi, and S. R. Stone. "Effect of thrombomodulin on the kinetics of the interaction of thrombin with substrates and inhibitors." Biochemical Journal 237, no. 1 (1986): 243–51. http://dx.doi.org/10.1042/bj2370243.

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Thrombomodulin decreased by 20-30% the Michaelis constant of two tripeptidyl p-nitroanilide substrates of thrombin. Thrombomodulin increased the rate of inactivation of thrombin by two peptidyl chloromethane inhibitors by a similar amount. This effect appeared to be due to a decrease in the dissociation constants of the inhibitors. An improved method for the separation of fibrinopeptides A and B by h.p.l.c. was developed, and this method was used to study the effect of thrombomodulin on the thrombin-catalysed cleavage of fibrinogen. In this reaction, thrombomodulin was a competitive inhibitor

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Szegedi, Nándor, László Gellér, Tamás Tahin, Béla Merkely, and Gábor Széplaki. "Rivaroxabankezelés mellett kialakult bal pitvari fülcsethrombus sikeres kezelése direkt trombininhibitorral." Orvosi Hetilap 157, no. 4 (2016): 154–56. http://dx.doi.org/10.1556/650.2016.30350.

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The authors present the history of a 62-year-old man on continuous rivaroxaban therapy who was scheduled for pulmonary vein isolation due to persistent atrial fibrillation. Preoperative transesophageal echocardiography detected the presence of left atrial appendage thrombus. Thrombophilia tests showed that the patient was heterozygous carrier of the methylene-tetrahydrofolate reductase gene mutation. The authors hypothesized that a direct thrombin inhibitor might exert a more appropriate effect against thrombosis in this case and, therefore, a switch to dabigatran was performed. After two mont

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Obst, Ulrike, Volker Gramlich, François Diederich, Lutz Weber, and David W. Banner. "Design of Novel, Nonpeptidic Thrombin Inhibitors and Structure of a Thrombin–Inhibitor Complex." Angewandte Chemie International Edition in English 34, no. 16 (1995): 1739–42. http://dx.doi.org/10.1002/anie.199517391.

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Cornelissen, Ivo, Erica De Candia, and Shaun R. Coughlin. "GP-VI Disruption Confers Additional Protection against Arterial Thrombosis in PAR-4 Deficient Mice." Blood 112, no. 11 (2008): 3932. http://dx.doi.org/10.1182/blood.v112.11.3932.3932.

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Abstract Following vascular injury, platelets are recruited and activated by adhesive proteins exposed on the subendothelium (including collagen), released agonists and locally generated thrombin. In mice, protease activated receptor 4 (PAR-4) mediates the platelet signaling response to thrombin. Previous studies showed that platelets from PAR-4 null mice do not respond to thrombin and while platelet thrombi do form at the site of injury in PAR-4 deficient animals, they do not propagate and extend into the lumen like thrombi in wild-type mice. The activation pathway responsible for this juxtam

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Zhang, Wei, and Robert W. Colman. "Thrombin regulates intracellular cyclic AMP concentration in human platelets through phosphorylation/activation of phosphodiesterase 3A." Blood 110, no. 5 (2007): 1475–82. http://dx.doi.org/10.1182/blood-2006-10-052522.

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Abstract Thrombin-induced cyclic AMP (cAMP) reduction potentates several steps in platelet activation, including Ca++ mobilization, cytoskeletal reorganization, and fibrinogen receptor conformation. We now reinvestigate the signaling pathways by which intracellular cAMP content is controlled after platelet activation by thrombin. When washed human platelets were stimulated with thrombin, cAMP-dependent phosphodiesterase (PDE3A) activity was significantly increased. A nonselective PDE inhibitor, 3-isobutyl-1-methylxanthine (IBMX), and the PDE3 selective inhibitors milrinone and cilostazol each

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Florian-Kujawski, Michelle R., Debra Hoppensteadt, Josephine Cunanan, Marianne Wilmer, and Jawed Fareed. "Relative Inhibition of Thrombin Activatable Fibrinolytic Inhibitor by Newly Developed Thrombin Inhibitors: Impact on Bleeding and Antithrombotic Actions." Blood 106, no. 11 (2005): 4051. http://dx.doi.org/10.1182/blood.v106.11.4051.4051.

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Abstract Thrombin activatable fibrinolytic inhibitor (TAFI) or carboxypeptidase U plays a key role in the fibrinolytic cascade. It acts as an inhibitor of fibrinolysis by cleaving the arginine and lysine amino acid residues from the carboxy terminus of fibrin. The cleavage then renders the fibrin resistant to digestion by plasmin, forming a clot that cannot be easily digested. This stabilized thrombus can then cause myocardial infarction, stroke or pulmonary embolism. It has been shown that individuals with acute coronary syndrome tend to have elevated TAFI, which may lead to further complicat

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Touyz, R. M., and E. L. Schiffrin. "Role of Protein Kinase C in the Anti-Aggregatory Effects of Endothelin-1 on Human Platelets." Clinical Science 88, no. 3 (1995): 277–83. http://dx.doi.org/10.1042/cs0880277.

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1. Endothelin-1 has anti-aggregatory properties, but the mechanism underlying this inhibitory action is unknown. This in vitro study investigates effects of endothelin-1 on thrombin-stimulated aggregation and intracellular free calcium concentration in human platelets and assesses the role of protein kinase C in the interactions between endothelin-1 and thrombin. Aggregation was measured turbidometrically and the intracellular free calcium concentration was determined with the fluorescent indicator fura 2-acetoxymethyl ester. 2. Endothelin-1 at concentrations from 10−11 to 10−6 mol/l had no ef

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