DOCSLIB.ORG

References Used in the Tables 1 Thiagarajan P, Wu KK. in Vitro

Total Page：16

File Type：pdf, Size：1020Kb

Download full-text PDF Read full-text
References Used in the Tables 1 Thiagarajan P, Wu KK. in Vitro References used in the tables 1 Thiagarajan P, Wu KK. In vitro assays for evaluating platelet function. In: Gresele P, Page CP, Fuster V, Vermylen J, editors. Platelets in Thrombotic and Non-Thrombotic Disorders. Cambridge: Cambridge University Press; 2002: 459–70. 2 Burns ER, Lawrence C. Bleeding time. A guide to its diagnostic and clinical utility. Arch Pathol Lab Med 1989;113:1219-1224 3 Lind SE. The bleeding time does not predict surgical bleeding. Blood 1991;77:2547-2552. 4 Finazzi G, Budde U, Michiels JJ. Bleeding time and platelet function in essential thrombocythaemia and other myeloproliferative disorders. Leuk Lymphoma 1996; 22 suppl. 1:71-78. 5 De Paepe A, Malfait F. Bleeding and bruising in patients with Ehlers-Danlos syndrome and other collagen vascular disorders. Br J Haematol 2004; 127: 491-500. 6 Rand ML, Leung R, Packham MA. Platelet Function Assays. Transfus.Apher.Sci 2003;28:301-317. 7 Rodgers RP, Levin J. A critical reappraisal of the bleeding time. Semin Thromb Hemost 1990;16:1–20. 8 Shenkman B, Savion N, Dardik R, Tamarin I, Varon D. Testing of platelet deposition on polystyrene surface under flow conditions by cone and plate(let) analyzer: role of platelet activation, fibrinogen and von Willebrand factor. Thromb Res 2001;99:353–61. 9 Varon D, Savion N. Cone and plate(let) analyzer. In: Michelson A, editor. Platelets. San Diego: Academic Press 2002: 337–45. 10 Varon D, Lashevski I, Brenner B, Beyar R, Lanir N, Tamarin I, et al. Cone and plate(let) analyzer: monitoring glycoprotein IIb/IIIa antagonists and von Willebrand disease replacement therapy by testing platelet deposition under flow conditions. Am Heart J 1998;135:187–93. 11 Wang X, Dorsam RT, Lauver A, Wang H, Barbera FA, Gibbs S, Varon D, Savion N, Friedman SM, Feuerstein GZ. Comparative analysis of various platelet glycoprotein IIb/IIIa antagonists on shear-induced platelet activation and adhesion. J Pharmacol Exp Ther 2002;303:1114-20. 12 Cazenave JP, Packham MA, Mustard JF.Adherence of platelets to a collagen-coated surface: development of a quantitative method. J Lab Clin Med 1973 ;82:978-90. 13 Sun L, Feng S, Resendiz JC, Lu X, Durante W, Kroll MH.Role of the Pyk2-MAP kinase-cPLA2 signaling pathway in shear-dependent platelet aggregation. Ann Biomed Eng 2004 ;32:1193-201.. 14 Resendiz JC, Feng S, Ji G, Kroll MH. von Willebrand factor binding to platelet glycoprotein Ib-IX-V stimulates the assembly of an alpha-actinin-based signaling complex. J Thromb Haemost 2004 ;2:161-9.. 15 Resendiz JC, Feng S, Ji G, Francis KA, Berndt MC, Kroll MH.Purinergic P2Y12 receptor blockade inhibits shear- induced platelet phosphatidylinositol 3-kinase activation. Mol Pharmacol 2003 ;63:639-45. 16 Kroll MH, Feng S. Targeting shear stress-induced platelet activation: is lesion-specific antiplatelet therapy a realistic clinical goal? Expert Rev Cardiovasc Ther 2005 ;3:941-51. 17 Varon D, Dardik R, Shenkman B, Kotev-Emeth S, Farzame N, Tamarin I, Savion N.A new method for quantitative analysis of whole blood platelet interaction with extracellular matrix under flow conditions. Thromb Res 1997 ;85:283-94. 18 Kenet G, Lubetsky A, Shenkman B, Tamarin I, Dardik R, Rechavi G, Barzilai A, Martinowitz U, Savion N, Varon D. Cone and platelet analyzer (CPA): a new test for the prediction of bleeding among thrombocytopenic patients. Br J Haematol 1998 ;101:255-9. 19 Levy Y, Shenkman B, Tamarin I, Pauzner R, Shoenfeld Y, Langevitz P, Savion N, Varon D.Increased platelet deposition on extracellular matrix under flow conditions in patients with antiphospholipid syndrome who experience thrombotic events. Arthritis Rheum 2005 ;52:4011-7. 20 Knobler H, Savion N, Shenkman B, Kotev-Emeth S, Varon D. Shear-induced platelet adhesion and aggregation on subendothelium are increased in diabetic patients. Thromb Res 1998 ;90:181-90. 21 Kroll MH, Feng S. Targeting shear stress-induced platelet activation: is lesion-specific antiplatelet therapy a realistic clinical goal? Expert Rev Cardiovasc Ther 2005 ;3:941-51. 22 Spectre G, Brill A, Gural A, Shenkman B, Touretsky N, Mosseri E, Savion N, Varon D. A new point-of-care method for monitoring anti-platelet therapy: application of the cone and plate(let) analyzer. Platelets 2005 ;16:293-9. 23 Matetzky S, Shenkman B, Guetta V, Shechter M, Bienart R, Goldenberg I, Novikov I, Pres H, Savion N, Varon D, Hod H Clopidogrel resistance is associated with increased risk of recurrent atherothrombotic events in patients with acute myocardial infarction. Circulation 2004 ;109:3171-5. 24 Feng S, Lu X, Kroll MH. Filamin A binding stabilizes nascent glycoprotein Ibalpha trafficking and thereby enhances its surface expression. J Biol Chem 2005 ;280:6709-15. 25 Shenkman B, Savion N, Dardik R, Tamarin I, Varon D.Testing of platelet deposition on polystyrene surface under flow conditions by the cone and plate(let) analyzer: role of platelet activation, fibrinogen and von Willebrand factor. Thromb Res 2000 ;99:353-61. 26 Shenkman B, Schneiderman J, Tamarin I, Kotev-Emeth S, Savion N, Varon D Testing the effect of GPIIb-IIIa antagonist in patients undergoing carotid stenting: correlation between standard aggregometry, flow cytometry and the cone and plate(let) analyzer (CPA) methods. Thromb Res 2001 ;102:311-7. 27. Wang X, Dorsam RT, Lauver A, Wang H, Barbera FA, Gibbs S, Varon D, Savion N, Friedman SM, Feuerstein GZ.Comparative analysis of various platelet glycoprotein IIb/IIIa antagonists on shear-induced platelet activation and adhesion. J Pharmacol Exp Ther 2002 ;303:1114-20. 28 Peerschke EI, Silver RT, Weksler B, Grigg SE, Savion N, Varon D. Ex vivo evaluation of erythrocytosis-enhanced platelet thrombus formation using the cone and plate(let) analyzer: effect of platelet antagonists. Br J Haematol 2004 ;127:195-203. 29 Chang HM and Robertson CR. Platelet aggregation by laminar shear and Brownian motion. Ann Biomed Eng 1976; 4: 151-83. 30 Frojmovic MM. Platelet aggregation in flow: Differential roles for adhesive receptors and ligands. Am Heart J Suppl 1998; 135: 5119-5131. 31 Xia Z, Frojmovic MM. Aggregation efficiency of activated normal or fixed platelets in a simple shear field: effect of shear and fibrinogen occupancy. Biophys J 1994; 66: 2110-201. 32 Frojmovic MM, Kasirer-Friede A, Goldsmith H. and Brown E. Surface-secreted von Willebrand Factor mediates aggregation of ADP-activated platelets at moderate shear stress: Facilitated by GPIb but controlled by GPIIb-IIIa. Thrombos Haemost 1997; 76: 568-576. 33 Bonnefoy A, Hantgan R, Legrand C, Frojmovic MM. A model of platelet aggregation involving multiple ineteractions of thrombospondin-1, fibrinogen and GPIIbIIIa receptor.J Bio. Chem 2001; 276: 5605-12. 34 Bonnefoy A, Liu Q, Jerome W Gray, Legrand C, and Frojmovic MM. Platelets in suspension require preactivation to adhere to immobilized fibrinogen. Annals New York Acad. Sci 2001; 936: 459-63. 35 Frojmovic MM, Nash G, and Diamond SL. Definitions in biorheology: cell aggregation and cell adhesion in flow. Recommendation of the Scientific Subcommittee on Biorheology of the Scientific and Standardisation Committee of the International Society on Thrombosis and Haemostasis. Thromb Haemost 2002;87:771. 36 Frojmovic M and Zolotarova E. Both shear and temperature can profoundly alter antithrombotic drug efficacy: demonstration with the P2Y12 ADP receptor antagonist, ARC-69931MX. J Thromb Haemost 2003 ; 1772. 37 Labarthe B, Frojmovic M and Legrand C. Inhibition and Reversal of Platelet Aggregation by αIIbβ3 Antagonists Depends on Flow Conditions:-Differential effects of Abciximab and Lamifiban. Br J Haematol 2005 ;131:348-55. 38 Falati S. et al. Accumulation of tissue factor into developing thrombi in vivo is dependent upon microparticle P- selectin glycoprotein ligand 1 and platelet P-selectin. J Exp Med 2003; 197: 1585-98. 39 Ajzenberg N, Aubry P, Huisse M-G, Cachier A, ElAmara W, Feldman L, Himbert D, Baruch D, Guillin M-C, Steg G. Enhanced shear-induced platelet aggregation in patients who experience subacute stent thrombosis. A case- control study. J American College Cardiology 2005; 45:1753. 40 Turner NA, Moake JL, McIntire LV. Blockade of adenosine diphosphate receptors P2Y(12) and P2Y(1) is required to inhibit platelet aggregation in whole blood under flow. Blood 2001 ;98:3340-5. 41 Baumgartner HR, Haudenschild C. Adhesion of platelets to subendothelium. Ann NY Acad Sci 1972; 201: 22- 36. 42 Baumgartner HR. The role of blood flow in platelet adhesion, fibrin deposition and formation of mural thrombi. Microvasc Res 1973; 5: 167-79. 43 Baumgartner ER Effects of anticoagulation on the interaction of human platelets with subendothelium in flowing blood. Schweiz Med Wochenschr 1976; 106: 1367-8. 44 Sakariassen KS, Turitto VT, Baumgartner HR. Recollection on the development of flow devices for studying mechanisms of haemostasis and thrombosis in flowing whole blood. J Thromb Haemostas 2004; 2: 1681-90. 45 Sakariassen KS, Bolhuis PA, Sixma JJ. Human blood platelet adhesion to artery subendothelium is mediated by factor VIII-von Willebrand factor bound to subendothelium. Nature 1979; 279: 636-8. 46 Sakariassen KS, Hanson SR, Cadroy Y. Methods and models to evaluate shear-dependent and surface reactivity-dependent antithrombotic efficacy. Thromb Res 2001; 104: 149-73. 47 Sakariassen KS, Turitto VT, Baumgartner HR. Recollection of the development of flow devices for studying mechanisms of hemostasis and thrombosis in flowing whole blood. J Thromb Haemostas 2004; 2: 1681-90. 48 Baumgartner HR. The role of blood flow in platelet adhesion, fibrin deposition and formation of mural thrombi. Microvasc Res 1973; 5: 167-79. 49 Sakariassen KS, Aarts PAMM, de Groot PG, Houdijk WPM, Sixma JJ. A perfusion chamber developed to investigate platelet interaction in flowing blood with human vessel wall cells, their extracellular matrix and purified components. J Lab Clin Med 1983; 102: 522-35.
Load more

Recommended publications
  • Hemoglobin Interaction with Gp1ba Induces Platelet Activation And
    ARTICLE Platelet Biology & its Disorders Hemoglobin interaction with GP1bα induces platelet activation and apoptosis: a novel mechanism associated with intravascular hemolysis Rashi Singhal,1,2,* Gowtham K. Annarapu,1,2,* Ankita Pandey,1 Sheetal Chawla,1 Amrita Ojha,1 Avinash Gupta,1 Miguel A. Cruz,3 Tulika Seth4 and Prasenjit Guchhait1 1Disease Biology Laboratory, Regional Centre for Biotechnology, National Capital Region, Biotech Science Cluster, Faridabad, India; 2Biotechnology Department, Manipal University, Manipal, Karnataka, India; 3Thrombosis Research Division, Baylor College of Medicine, Houston, TX, USA, and 4Hematology, All India Institute of Medical Sciences, New Delhi, India *RS and GKA contributed equally to this work. ABSTRACT Intravascular hemolysis increases the risk of hypercoagulation and thrombosis in hemolytic disorders. Our study shows a novel mechanism by which extracellular hemoglobin directly affects platelet activation. The binding of Hb to glycoprotein1bα activates platelets. Lower concentrations of Hb (0.37-3 mM) significantly increase the phos- phorylation of signaling adapter proteins, such as Lyn, PI3K, AKT, and ERK, and promote platelet aggregation in vitro. Higher concentrations of Hb (3-6 mM) activate the pro-apoptotic proteins Bak, Bax, cytochrome c, caspase-9 and caspase-3, and increase platelet clot formation. Increased plasma Hb activates platelets and promotes their apoptosis, and plays a crucial role in the pathogenesis of aggregation and development of the procoagulant state in hemolytic disorders. Furthermore, we show that in patients with paroxysmal nocturnal hemoglobinuria, a chronic hemolytic disease characterized by recurrent events of intravascular thrombosis and thromboembolism, it is the elevated plasma Hb or platelet surface bound Hb that positively correlates with platelet activation.
    [Show full text]
  • Common Gene Polymorphisms Associated with Thrombophilia
    Chapter 5 Common Gene Polymorphisms Associated with Thrombophilia Christos Yapijakis, Zoe Serefoglou and Constantinos Voumvourakis Additional information is available at the end of the chapter http://dx.doi.org/10.5772/61859 Abstract Genetic association studies have revealed a correlation between DNA variations in genes encoding factors of the hemostatic system and thrombosis-related disease. Certain var‐ iant alleles of these genes that affect either gene expression or function of encoded protein are known to be genetic risk factors for thrombophilia. The chapter presents the current genetics and molecular biology knowledge of the most important DNA polymorphisms in thrombosis-related genes encoding coagulation factor V (FV), coagulation factor II (FII), coagulation factor XII (FXII), coagulation factor XIII A1 subunit (FXIIIA1), 5,10- methylene tetrahydrofolate reductase (MTHFR), serpine1 (SERPINE1), angiotensin I-con‐ verting enzyme (ACE), angiotensinogen (AGT), integrin A2 (ITGA2), plasma carboxypeptidase B2 (CPB2), platelet glycoprotein Ib α polypeptide (GP1BA), thrombo‐ modulin (THBD) and protein Z (PROZ). The molecular detection methods of each DNA polymorphism is presented, in addition to the current knowledge regarding its influence on thrombophilia and related thrombotic events, including stroke, myocardial infarction, deep vein thrombosis, spontaneous abortion, etc. In addition, best thrombosis prevention strategies with a combination of genetic counseling and molecular testing are discussed. Keywords: Thrombophilia, coagulation
    [Show full text]
  • Therapeutic Antibody-Like Immunoconjugates Against Tissue Factor with the Potential to Treat Angiogenesis-Dependent As Well As Macrophage-Associated Human Diseases
    antibodies Review Therapeutic Antibody-Like Immunoconjugates against Tissue Factor with the Potential to Treat Angiogenesis-Dependent as Well as Macrophage-Associated Human Diseases Zhiwei Hu ID Department of Surgery Division of Surgical Oncology, The James Comprehensive Cancer Center, The Ohio State University College of Medicine, Columbus, OH 43210, USA; [email protected]; Tel.: +1-614-685-4606 Received: 10 October 2017; Accepted: 18 January 2018; Published: 23 January 2018 Abstract: Accumulating evidence suggests that tissue factor (TF) is selectively expressed in pathological angiogenesis-dependent as well as macrophage-associated human diseases. Pathological angiogenesis, the formation of neovasculature, is involved in many clinically significant human diseases, notably cancer, age-related macular degeneration (AMD), endometriosis and rheumatoid arthritis (RA). Macrophage is involved in the progression of a variety of human diseases, such as atherosclerosis and viral infections (human immunodeficiency virus, HIV and Ebola). It is well documented that TF is selectively expressed on angiogenic vascular endothelial cells (VECs) in these pathological angiogenesis-dependent human diseases and on disease-associated macrophages. Under physiology condition, TF is not expressed by quiescent VECs and monocytes but is solely restricted on some cells (such as pericytes) that are located outside of blood circulation and the inner layer of blood vessel walls. Here, we summarize TF expression on angiogenic VECs, macrophages and other diseased cell types in these human diseases. In cancer, for example, the cancer cells also overexpress TF in solid cancers and leukemia. Moreover, our group recently reported that TF is also expressed by cancer-initiating stem cells (CSCs) and can serve as a novel oncotarget for eradication of CSCs without drug resistance.
    [Show full text]
  • Supplementary Table 1: Adhesion Genes Data Set
    Supplementary Table 1: Adhesion genes data set PROBE Entrez Gene ID Celera Gene ID Gene_Symbol Gene_Name 160832 1 hCG201364.3 A1BG alpha-1-B glycoprotein 223658 1 hCG201364.3 A1BG alpha-1-B glycoprotein 212988 102 hCG40040.3 ADAM10 ADAM metallopeptidase domain 10 133411 4185 hCG28232.2 ADAM11 ADAM metallopeptidase domain 11 110695 8038 hCG40937.4 ADAM12 ADAM metallopeptidase domain 12 (meltrin alpha) 195222 8038 hCG40937.4 ADAM12 ADAM metallopeptidase domain 12 (meltrin alpha) 165344 8751 hCG20021.3 ADAM15 ADAM metallopeptidase domain 15 (metargidin) 189065 6868 null ADAM17 ADAM metallopeptidase domain 17 (tumor necrosis factor, alpha, converting enzyme) 108119 8728 hCG15398.4 ADAM19 ADAM metallopeptidase domain 19 (meltrin beta) 117763 8748 hCG20675.3 ADAM20 ADAM metallopeptidase domain 20 126448 8747 hCG1785634.2 ADAM21 ADAM metallopeptidase domain 21 208981 8747 hCG1785634.2|hCG2042897 ADAM21 ADAM metallopeptidase domain 21 180903 53616 hCG17212.4 ADAM22 ADAM metallopeptidase domain 22 177272 8745 hCG1811623.1 ADAM23 ADAM metallopeptidase domain 23 102384 10863 hCG1818505.1 ADAM28 ADAM metallopeptidase domain 28 119968 11086 hCG1786734.2 ADAM29 ADAM metallopeptidase domain 29 205542 11085 hCG1997196.1 ADAM30 ADAM metallopeptidase domain 30 148417 80332 hCG39255.4 ADAM33 ADAM metallopeptidase domain 33 140492 8756 hCG1789002.2 ADAM7 ADAM metallopeptidase domain 7 122603 101 hCG1816947.1 ADAM8 ADAM metallopeptidase domain 8 183965 8754 hCG1996391 ADAM9 ADAM metallopeptidase domain 9 (meltrin gamma) 129974 27299 hCG15447.3 ADAMDEC1 ADAM-like,
    [Show full text]
  • Alternatively Spliced Tissue Factor Induces Angiogenesis Through Integrin Ligation
    Alternatively spliced tissue factor induces angiogenesis through integrin ligation Y. W. van den Berga, L. G. van den Hengela, H. R. Myersa, O. Ayachia, E. Jordanovab, W. Rufc, C. A. Spekd, P. H. Reitsmaa, V. Y. Bogdanove, and H. H. Versteega,1 aThe Einthoven Laboratory for Experimental Vascular Medicine and bDepartment of Pathology, Leiden University Medical Center, Albinusdreef 2, 2333 ZA, Leiden, The Netherlands; cDepartment of Immunology and Microbial Science, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037; dCenter for Experimental and Molecular Medicine, Academic Medical Center, Meibergdreef 9, 1105 AZ, Amsterdam, The Netherlands; and eDivision of Hematology/Oncology, Department of Internal Medicine, University of Cincinnati College of Medicine, 3125 Eden Avenue, Cincinnati, OH 45267 Edited by Charles T. Esmon, Oklahoma Medical Research Foundation, Oklahoma City, OK, and approved September 25, 2009 (received for review May 15, 2009) The initiator of coagulation, full-length tissue factor (flTF), in complex pancreatic cancer cells transfected to express asTF produce more with factor VIIa, influences angiogenesis through PAR-2. Recently, an blood vessels (20), but it remained mechanistically unclear if and alternatively spliced variant of TF (asTF) was discovered, in which part how angiogenesis is regulated by asTF. One possibility is that asTF of the TF extracellular domain, the transmembrane, and cytoplasmic stimulates cancer cells to produce angiogenic factors, but it is also domains are replaced by a unique C terminus. Subcutaneous tumors plausible that asTF enhances angiogenesis via paracrine stimulation produced by asTF-secreting cells revealed increased angiogenesis, but of endothelial cells. Moreover, the role of VIIa, PAR-2 activation it remained unclear if and how angiogenesis is regulated by asTF.
    [Show full text]
  • Datasheet: MCA740PE Product Details
    Datasheet: MCA740PE Description: MOUSE ANTI HUMAN CD42b:RPE Specificity: CD42b Other names: GPIB-ALPHA Format: RPE Product Type: Monoclonal Antibody Clone: AK2 Isotype: IgG1 Quantity: 100 TESTS Product Details Applications This product has been reported to work in the following applications. This information is derived from testing within our laboratories, peer-reviewed publications or personal communications from the originators. Please refer to references indicated for further information. For general protocol recommendations, please visit www.bio-rad-antibodies.com/protocols. Yes No Not Determined Suggested Dilution Flow Cytometry Neat Where this antibody has not been tested for use in a particular technique this does not necessarily exclude its use in such procedures. The suggested working dilution is given as a guide only. It is recommended that the user titrates the antibody for use in his/her own system using appropriate negative/positive controls. Target Species Human Product Form Purified IgG conjugated to R. Phycoerythrin (RPE) - lyophilized Reconstitution Reconstitute with 1 ml distilled water Max Ex/Em Fluorophore Excitation Max (nm) Emission Max (nm) RPE 488nm laser 496 578 Preparation Purified IgG prepared by affinity chromatography on Protein A from tissue culture supernatant Buffer Solution Phosphate buffered saline Preservative 0.09% Sodium Azide Stabilisers 1% Bovine Serum Albumin 5% Sucrose External Database Links UniProt: P07359 Related reagents Entrez Gene: 2811 GP1BA Related reagents Page 1 of 3 Specificity Mouse anti Human CD42b antibody, clone AK2 recognizes the human CD42b cell surface antigen, also known as platelet glycoprotein GP1B. CD42b is expressed by platelets and megakaryocytes. Clone AK2 has been reported to block the binding of von Willebrand Factor (VWF) to platelets Flow Cytometry Use 10ul of the suggested working dilution to label 100ul whole blood.
    [Show full text]
  • Endotoxin Enhances Tissue Factor and Suppresses Thrombomodulin Expression of Human Vascular Endothelium in Vitro Kevin L
    Endotoxin Enhances Tissue Factor and Suppresses Thrombomodulin Expression of Human Vascular Endothelium In Vitro Kevin L. Moore,* Sharon P. Andreoli,* Naomi L. Esmon,1 Charles T. Esmon,l and Nils U. Bang1l Department ofMedicine, Section ofHematology/Oncology,* and Department ofPediatrics, Section ofNephrology,t Indiana University School ofMedicine, Indianapolis, Indiana 46223; Oklahoma Medical Research Foundation,§ Oklahoma City, Oklahoma 73104; and Lilly Laboratory for Clinical Research,1' Indianapolis, Indiana 46202 Abstract to support the assembly of clotting factor complexes on their surfaces (13, 14). Endotoxemia is frequently associated clinically with disseminated Under physiologic conditions the thromboresistant properties intravascular coagulation (DIC); however, the mechanism of en- ofthe endothelium are predominant. In some pathological states, dotoxin action in vivo is unclear. Modulation of tissue factor however, this may not be the case. Gram-negative sepsis is fre- (TF) and thrombomodulin (TM) expression on the endothelial quently associated with varying degrees of disseminated intra- surface may be relevant pathophysiologic mechanisms. Stimu- vascular coagulation (DIC),' which is thought to be triggered by lation of human umbilical vein endothelial cells with endotoxin endotoxemia. The pathophysiology of DIC in gram-negative (1 ,ug/ml) increased surface TF activity from 1.52±0.84 to sepsis is complex and the mechanism(s) by which endotoxemia 11.89±8.12 mU/ml-106 cells at 6 h (n = 11) which returned to promotes intravascular coagulation in vivo is unclear. Recently, baseline by 24 h. Repeated stimulation at 24 h resulted in renewed reports by several investigators provide evidence that the throm- TF expression. Endotoxin (1 ,tg/ml) also caused a decrease in boresistance of the endothelial cell is diminished after exposure TM expression to 55.0±6.4% of control levels at 24 h (n = 10) to endotoxin in the absence of other cell types.
    [Show full text]
  • Path Ggf 5 2020.Pdf
    Hemostasis Hemostasis and Thrombosis Normal hemostasis is a consequence of tightly regulated processes that maintain blood in a fluid state in normal vessels, yet also permit the rapid formation of a hemostatic clot at the site of a vascular injury. Thrombosis involves blood clot formation within intact vessels. Both hemostasis and thrombosis involve three components: the vascular wall, platelets and the coagulation cascade. Elements of the Hemostatic process • Endothelium • Anti-thrombosis • Pro-thrombosis • Platelets • Platelet-endothelial cell interaction • Coagulation cascade http://www.as.miami.edu/chemistry/2086/chapter_21/NEW-Chap21_class_part1_files/image002.jpg After initial injury there is a brief period of arteriolar vasoconstriction mediated by reflex neurogenic mechanisms and augmented by the local secretion of factors such as endothelin (a potent endothelium-derived vasoconstrictor) The effect is transient, however, and bleeding would resume if not for activation of the platelet and coagulation systems. Endothelial injury exposes highly thrombogenic subendothelial extracellular matrix (ECM), facilitating platelet adherence and activation. Activation of platelets results in a dramatic shape change (from small rounded discs to flat plates with markedly increased surface area), as well as the release of secretory granules. Within minutes the secreted products recruit additional platelets (aggregation) to form a hemostatic plug; this process is referred to as primary hemostasis. http://www.ouhsc.edu/platelets/Platelet%20Pic s/Platelets3.jpg http://medcell.med.yale.edu/histology/blood_bone_marr ow_lab/images/platelets_em.jpg Tissue factor is also exposed at the site of injury. Also known as factor III and thromboplastin, tissue factor is a membrane-bound procoagulant glycoprotein synthesized by endothelial cells. It acts in conjunction with factor VII (see below) as the major in vivo initiator of the coagulation cascade, eventually culminating in thrombin generation.
    [Show full text]
  • 63Rd Annual SSC Meeting, in Conjunction with the 2017 ISTH Congress in Berlin, Germany Meeting Minutes
    63rd Annual SSC meeting, in conjunction with the 2017 ISTH Congress in Berlin, Germany Meeting Minutes Standing Committees Coagulation Standards Committee ............................................................... 3 Subcommittees Animal, Cellular and Molecular Models ........................................................ 5 Biorheology .................................................................................................. 7 Control of Anticoagulation ............................................................................ 10 Disseminated Intravascular Coagulation ...................................................... 12 Factor VIII, Factor IX and Rare Coagulation Disorders ................................ 14 Factor XI and the Contact System ................................................................ 19 Factor XIII and Fibrinogen ............................................................................ 21 Fibrinolysis ................................................................................................... 27 Genomics in Thrombosis and Hemostasis ................................................... 33 Hemostasis and Malignancy......................................................................... 46 Lupus Anticoagulant/Phospholipid Dependent Antibodies ........................... 49 Pediatric and Neonatal Hemostasis and Thrombosis ................................... 54 Perioperative Thrombosis and Hemostasis .................................................. 59 Plasma Coagulation Inhibitors .....................................................................
    [Show full text]
  • Biomechanical Thrombosis: the Dark Side of Force and Dawn of Mechano-­ Medicine
    Open access Review Stroke Vasc Neurol: first published as 10.1136/svn-2019-000302 on 15 December 2019. Downloaded from Biomechanical thrombosis: the dark side of force and dawn of mechano- medicine Yunfeng Chen ,1 Lining Arnold Ju 2 To cite: Chen Y, Ju LA. ABSTRACT P2Y12 receptor antagonists (clopidogrel, pras- Biomechanical thrombosis: the Arterial thrombosis is in part contributed by excessive ugrel, ticagrelor), inhibitors of thromboxane dark side of force and dawn platelet aggregation, which can lead to blood clotting and A2 (TxA2) generation (aspirin, triflusal) or of mechano- medicine. Stroke subsequent heart attack and stroke. Platelets are sensitive & Vascular Neurology 2019;0. protease- activated receptor 1 (PAR1) antag- to the haemodynamic environment. Rapid haemodynamcis 1 doi:10.1136/svn-2019-000302 onists (vorapaxar). Increasing the dose of and disturbed blood flow, which occur in vessels with these agents, especially aspirin and clopi- growing thrombi and atherosclerotic plaques or is caused YC and LAJ contributed equally. dogrel, has been employed to dampen the by medical device implantation and intervention, promotes Received 12 November 2019 platelet thrombotic functions. However, this platelet aggregation and thrombus formation. In such 4 Accepted 14 November 2019 situations, conventional antiplatelet drugs often have also increases the risk of excessive bleeding. suboptimal efficacy and a serious side effect of excessive It has long been recognized that arterial bleeding. Investigating the mechanisms of platelet thrombosis
    [Show full text]
  • Tissue Factor Regulation, Signaling and Functions Beyond Coagulation with a Focus on Diabetes
    Digital Comprehensive Summaries of Uppsala Dissertations from the Faculty of Medicine 1626 Tissue Factor regulation, signaling and functions beyond coagulation with a focus on diabetes DESIRÉE EDÉN ACTA UNIVERSITATIS UPSALIENSIS ISSN 1651-6206 ISBN 978-91-513-0842-5 UPPSALA urn:nbn:se:uu:diva-399599 2020 Dissertation presented at Uppsala University to be publicly examined in Enghoffsalen, Akademiska sjukhuset, ing. 50, Uppsala, Friday, 21 February 2020 at 13:15 for the degree of Doctor of Philosophy (Faculty of Medicine). The examination will be conducted in Swedish. Faculty examiner: Docent, Universitetslektor Sofia Ramström (Örebro Universitet, Institutionen för medicinska vetenskaper). Abstract Edén, D. 2020. Tissue Factor regulation, signaling and functions beyond coagulation with a focus on diabetes. Digital Comprehensive Summaries of Uppsala Dissertations from the Faculty of Medicine 1626. 65 pp. Uppsala: Acta Universitatis Upsaliensis. ISBN 978-91-513-0842-5. Background: Tissue factor (TF) is a 47 kDa transmembrane glycoprotein best known for initiating the coagulation cascade upon binding of its ligand FVIIa. Apart from its physiological role in coagulation, TF and TF/FVIIa signaling has proved to be involved in diseases such as diabetes, cancer and cardiovascular diseases. Biological functions coupled to TF/FVIIa signaling include diet-induced obesity, apoptosis, angiogenesis and migration. Aim: The aim of this thesis was to investigate the role of TF/FVIIa in cells of importance in diabetes, to further investigate the mechanism behind TF/FVIIa anti-apoptotic signaling in cancer cells and lastly to examine the regulation of TF expression in monocytes by micro RNAs (miRNA). Results: In paper I we found that TF/FVIIa signaling augments cytokine-induced beta cell death and impairs glucose stimulated insulin secretion from human pancreatic islets.
    [Show full text]
  • Human Induced Pluripotent Stem Cell–Derived Podocytes Mature Into Vascularized Glomeruli Upon Experimental Transplantation
    BASIC RESEARCH www.jasn.org Human Induced Pluripotent Stem Cell–Derived Podocytes Mature into Vascularized Glomeruli upon Experimental Transplantation † Sazia Sharmin,* Atsuhiro Taguchi,* Yusuke Kaku,* Yasuhiro Yoshimura,* Tomoko Ohmori,* ‡ † ‡ Tetsushi Sakuma, Masashi Mukoyama, Takashi Yamamoto, Hidetake Kurihara,§ and | Ryuichi Nishinakamura* *Department of Kidney Development, Institute of Molecular Embryology and Genetics, and †Department of Nephrology, Faculty of Life Sciences, Kumamoto University, Kumamoto, Japan; ‡Department of Mathematical and Life Sciences, Graduate School of Science, Hiroshima University, Hiroshima, Japan; §Division of Anatomy, Juntendo University School of Medicine, Tokyo, Japan; and |Japan Science and Technology Agency, CREST, Kumamoto, Japan ABSTRACT Glomerular podocytes express proteins, such as nephrin, that constitute the slit diaphragm, thereby contributing to the filtration process in the kidney. Glomerular development has been analyzed mainly in mice, whereas analysis of human kidney development has been minimal because of limited access to embryonic kidneys. We previously reported the induction of three-dimensional primordial glomeruli from human induced pluripotent stem (iPS) cells. Here, using transcription activator–like effector nuclease-mediated homologous recombination, we generated human iPS cell lines that express green fluorescent protein (GFP) in the NPHS1 locus, which encodes nephrin, and we show that GFP expression facilitated accurate visualization of nephrin-positive podocyte formation in
    [Show full text]