1,600 results match your criteria Haemostasis[Journal]
Haemostasis 2001 ;31 Suppl 1:1-110
Haemostasis 2001 ;31 Suppl 1:68-9
McMaster University, Faculty of Health Sciences, Hamilton, Ontario, Canada.
Haemostasis 2001 ;31 Suppl 1:67
Hammersmith Hospital, Imperial College, Thrombosis Research Institute, London, England, UK.
Haemostasis 2001 ;31 Suppl 1:64-6
Department of Hematology, Hadassah, Hebrew University Medical Center, Jerusalem, Israel.
Haemostasis 2001 ;31 Suppl 1:60-3
Department of Oncology, Hadassah-Hebrew University Hospital, Jerusalem, Israel.
Cleavage of heparan sulfate proteoglycans affects the integrity and functional state of tissues and thereby fundamental normal and pathological phenomena involving cell migration and response to changes in the extracellular microenvironment. Heparanase, degrading heparan sulfate (HS) at specific intrachain sites, is synthesized as a latent approximately 65 kDa protein that is processed at the N-terminus into a highly active approximately 50 kDa form. The heparanase enzyme is preferentially expressed in human tumors and its overexpression in low-metastatic tumor cells confers a highly invasive phenotype in experimental animals. Read More
Haemostasis 2001 ;31 Suppl 1:59
Dept. of Cell Biology and Functional Genetics, Università Vito-Salute San Raffaele, Milan, Italy.
Haemostasis 2001 ;31 Suppl 1:55-8
The Scripps Research Institute, La Jolla, CA 92037, USA.
Haemostasis 2001 ;31 Suppl 1:52-4
Department of Vascular Medicine and Pharmacology, Istituto di Ricerche Farmacologiche Mario Negri, Consorzio Mario Negri Sud, Santa Maria Imbaro, Italy.
Haemostasis 2001 ;31 Suppl 1:5-7
Department of Immunology and Vascular Biology, The Scripps Research Institute, La Jolla, CA 92037, USA.
TF expression is a hallmark of cancer progression. The procoagulant functions of TF that lead to thrombin generation are critically important to support metastasis, in part through the generation of fibrin that assures prolonged arrest of tumor cells in target organs. In addition, the coagulation initiation complex, i. Read More
Haemostasis 2001 ;31 Suppl 1:49-51
Hematology Department, San Bortolo Hospital, Vicenza, Italy.
Haemostasis 2001 ;31 Suppl 1:47-8
Academic Medical Center, Department of Internal Medicine, University of Amsterdam, The Netherlands.
Haemostasis 2001 ;31 Suppl 1:45-6
Angelo Bianchi Bonomi Hemophilia and Thrombosis Center, IRCCS Maggiore Hospital and University of Milan, Italy.
Haemostasis 2001 ;31 Suppl 1:43-4
Department of Hematology, Rambam Medical Center and Bruce Rappaport Faculty of Medicine, Technion, Haifa, Israel.
Haemostasis 2001 ;31 Suppl 1:40-2
Department of Internal Medicine, Academic Medical Center, Amsterdam, The Netherlands.
Haemostasis 2001 ;31 Suppl 1:37-9
Department of Medical and Surgical Sciences, University of Padua, Italy.
Since Trousseau's time it has been documented the strong two-way relationship between cancer and venous thromboembolism (VTE). Moreover it has been clearly demonstrated that patients with a first episode of idiopathic VTE exhibit a higher risk of newly discovered cancer during follow-up when compared to those suffering from secondary VTE. The performance of a selected diagnostic work-up for cancer detection at the time of referral for index VTE in these patients appears to be capable to identify most of these malignancies and the earlier detection is likely to be associated with improved treatment possibilities and thus prognosis. Read More
Haemostasis 2001 ;31 Suppl 1:34-6
Department of Clinical Epidemiology, Aarhus University Hospital, Denmark.
Haemostasis 2001 ;31 Suppl 1:32-3
Department of Internal Medicine, Academic Hospital Maastricht, University of Maastricht, The Netherlands.
Haemostasis 2001 ;31 Suppl 1:30-1
M.D. Anderson Cancer Center, University of Texas, Houston 77030, USA.
Haemostasis 2001 ;31 Suppl 1:25-9
Department of Cell Biology and Histology, Academic Medical Center, University of Amsterdam, The Netherlands.
Haemostasis 2001 ;31 Suppl 1:23-4
Mario Negri Institute for Pharmacological Research, Bergamo, Italy.
Haemostasis 2001 ;31 Suppl 1:21-2
Deportment of Applied BioSciences, Swiss Federal Institute of Technology, Zurich.
Haemostasis 2001 ;31 Suppl 1:16-20
The George Washington University Medical Center and the Children's National Medical Center, Washington, DC, USA.
Haemostasis 2001 ;31 Suppl 1:11-5
Division of Hematology/Oncology, Children's Hospital Research Foundation and University of Cincinnati College of Medicine, OH 45229-3039, USA.
Detailed studies tumor cell-associated procoagulants and fibrinolytic factors have strongly suggested that local thrombin and plasmin generation may be important in tumor progression. Given that one target for both these serine proteases is fibrinogen, a logical extension of this hypothesis is that local fibrin deposition and dissolution may be key determinants of tumor growth and/or dissemination. To directly test this concept, we initiated studies of tumor growth, experimental metastasis, and spontaneous metastasis in C57Bl/6-inbred mice with and without fibrinogen. Read More
Haemostasis 2001 ;31 Suppl 1:1-4
Dept. Hematology-Oncology, Ospedali Riuniti, Bergamo, Italy.
Thrombin generation and fibrin formation are constantly determined in patients with malignancy, who are at increased risk of thromboembolic complications. Most importantly, fibrin formation is also involved in the processes of tumor spread and metastasis. Activation of blood coagulation in cancer is a complex phenomenon, involving many different pathways of the hemostatic system and numerous interactions of the tumor cell with other blood cells, including platelet, monocyte and endothelial cell. Read More
Haemostasis 2001 May-Dec;31(3-6):294-305
Institute of Zoology, Slovak Academy of Sciences, SK-84206 Bratislava, Slovakia.
Anticoagulant activities against the extrinsic and intrinsic coagulation pathways were identified in salivary gland extracts (SGE) prepared from four tabanids (Hybomitra muehlfeldi, Tabanus autumnalis, Haematopota pluvialis, Heptatoma pellucens). All extracts prolonged human plasma clotting time in a dose-dependent manner and inhibited thrombin activity in the chromogenic substrate assay. Horsefly SGE did not inhibit factor Xa. Read More
Haemostasis 2001 May-Dec;31(3-6):288-93
Centro de Medicina Experimental, Laboratorio de Fisiopatologia, Instituto Venezolano de Investigaciones Científicas (IVIC), Apartado 21827, Caracas 1020A, Venezuela.
Persons who have been in contact with Lonomia achelous or Lonomia obliqua caterpillars present external and internal bleeding and opening of recently healed wounds. Hematological tests show normal platelet count, prolonged prothrombin time, activated partial thromboplastin time and thrombin time, totally corrected by normal plasma. Decreased fibrinogen (Fg), factor (F) V, FXIII, plasminogen and alpha(2)-antiplasmin with increased FVIII: C, von Willebrand factor, Fg degradation products and D dimers. Read More
Haemostasis 2001 May-Dec;31(3-6):279-87
Département de Biologie, Université de Cergy-Pontoise, Cergy-Pontoise, France.
Some venom and mammalian-secreted phospholipases A(2) (sPLA(2)) have been described to exert an anticoagulant effect. This review will discuss and compare phospholipid-dependent versus protein-dependent mechanisms of action of these sPLA(2) on the coagulation cascade. The importance of venom proteins, and of the study of their pharmacological effects, to explore the physiological functions of homologous mammalian proteins is also pointed out. Read More
Haemostasis 2001 May-Dec;31(3-6):273-8
Departamento de Bioquímica Médica/ICB/CCS, Bloco H-2o Andar-Ilha do Fundao, Universidade Federal do Rio de Janeiro, Rio de Janeiro, RJ 21941-590, Brazil.
Bothrojaracin (BJC) is a 27-kD protein from Bothrops jararaca venom that interacts with alpha-thrombin (K(D) = 0.7 nM) through both anion-binding exosites I and II. Recently, it has been shown that BJC interacts with the exosite I precursor (proexosite I) on human prothrombin (K(D) = 75 nM), forming a 1:1 Ca(2+)-independent noncovalent complex with the zymogen. Read More
Haemostasis 2001 May-Dec;31(3-6):266-72
Pentapharm Ltd., Engelgasse 109, P.O. Box, CH-4002 Basel, Switzerland.
Proteinases converting the zymogen protein C (PC) of vertebrates into activated PC have been detected in several snake venoms. Most PC activators have been purified from venom of snake species belonging to the genera of the Agkistrodon complex. Unlike the physiological, thrombin-catalyzed PC activation reaction which requires thrombomodulin as a cofactor, most snake venom activators directly convert the zymogen PC into the catalytically active form which can easily be determined by means of coagulation or chromogenic substrate techniques. Read More
Haemostasis 2001 May-Dec;31(3-6):257-65
Laboratory of Biochemistry and Biophysics, Center for Applied Toxinology, CEPID-FAPESP, Butantan Institute, Av. Vital Brazil 1500, 05503-900 São Paulo-SP, Brazil.
Severe consumption coagulopathy has been detected in rats after Lopap (a prothrombin activator from Lonomia obliqua caterpillar bristles) infusion and in humans after accidental contact with L. obliqua bristles. However, platelet count and antithrombin (AT) levels were only modestly affected, suggesting that a different form of blood coagulation activation may be involved in this hemorrhagic syndrome. Read More
Haemostasis 2001 May-Dec;31(3-6):247-56
Venom Unit, Institut Pasteur, 25 rue du Docteur-Roux, F-75724 Paris Cedex 15, France.
Thrombin is a mammalian serine proteinase that plays a prominent role in the maintenance and regulation of hemostasis through its interaction with various substrates and/or ligands. The venoms of several snakes contain glycosylated serine proteinases that have been recognized to possess one or more of the essential activities of thrombin on fibrinogen (Fg) and/or platelets. These proteinases share about 60% sequence identity. Read More
Haemostasis 2001 May-Dec;31(3-6):241-6
Department of Biochemistry, Cardiovascular Research Institute, University of Maastricht, PO Box 616, NL-6200 MD Maastricht, The Netherlands.
Blood coagulation factor V is a single-chain glycoprotein with M(r) = 330,000 which plays an important role in the procoagulant and anticoagulant pathways. Thrombin activates factor V into factor Va, a two-chain molecule which is composed of a heavy (M(r) = 105,000) and a light chain (M(r) = 71,000/74,000). Factor Va accelerates factor Xa-catalysed prothrombin activation more than 1,000-fold and under physiological conditions the cofactor activity of factor Va in prothrombin activation is down-regulated by activated protein C. Read More
Haemostasis 2001 May-Dec;31(3-6):234-40
Department of Biochemistry, Faculty of Medicine, National University of Singapore, 14 Science Drive, Singapore 117543.
We have recently determined the complete amino acid sequence of trocarin, a group D prothrombin activator from the venom of Tropidechis carinatus (Australian rough-scaled snake). This proteinase is both functionally and structurally similar to mammalian blood coagulation factor Xa. It shows approximately 70% homology and possesses the characteristic Gla domain, two EGF domains and serine proteinase domain. Read More
Haemostasis 2001 May-Dec;31(3-6):225-33
Cardiovascular Research Institute Maastricht (CARIM), Maastricht University, PO Box 616, NL-6200 MD Maastricht, The Netherlands.
Activators of blood coagulation factor X have been described in the venom of many snake species belonging to the genus Viperidae and Crotalidae as well as from a few Elapid species. Based on the structural and functional properties of purified activating principles, factor X activators are either metalloproteases or serine proteases. The best known activator is RVV-X from Russell's viper (Daboia russelli), a metalloprotease consisting of a heavy chain containing the catalytic domain and two light chains which share homology with C-type lectins and which are thought to exert a regulatory function in the Ca(2+)-dependent activation of factor X. Read More
Haemostasis 2001 May-Dec;31(3-6):218-24
Department of Biological Sciences, Faculty of Science, Block S2 Room 04-11, 14 Science Drive, National University of Singapore, Singapore 117543.
Several procoagulant proteins from snake venoms have been isolated and characterized. They are either serine proteinases or metalloproteinases, which activate specific zymogens of coagulation factors and initiate the coagulation cascade. These procoagulant proteins are useful in treating various thrombotic and hemostatic conditions and contribute to our understanding of molecular details in the activation of specific coagulation factors. Read More
Haemostasis 2001 May-Dec;31(3-6):211-7
School of Life Sciences, Queensland University of Technology, 2 George Street, GPO Box 2434, Brisbane, Qld. 4001, Australia.
Snake venom toxins are invaluable for the assay of coagulation factors and for the study of haemostasis generally. Thrombin-like enzymes (SVTLE) are used for fibrinogen and fibrinogen breakdown product assays as well as detecting dysfibrinogenaemias. Since SVTLE are not inhibited by heparin, they can be used for assaying antithrombin III in samples containing heparin. Read More
Haemostasis 2001 May-Dec;31(3-6):207-10
Laboratoire des Venins et Toxines, Institut Pasteur de Tunis, 13 Place Pasteur, BP 74, 1002 Tunis-Belvédère, Tunisia.
Lebetins from Macrovipera lebetina snake venom constitute a new class of inhibitors of platelet aggregation. There are two groups of peptides: lebetin 1 (L1; 11- to 13-mer) and lebetin 2 (L2; 37- to 38-mer). The short lebetins are identical to the N-terminal segments of the longer ones. Read More
Haemostasis 2001 May-Dec;31(3-6):192-206
Pharmacological Institute, College of Medicine, National Taiwan University, No. 1 Jen-Ai Road, Sec. 1, Taipei, Taiwan, ROC.
Angiogenesis is a complex process consisting of the proliferation, migration and differentiation of endothelial cells, and it is essential for the progression of malignant solid tumors. In this report, we examine the effects of disintegrins (e.g. Read More
Haemostasis 2001 May-Dec;31(3-6):183-91
Department of Biochemistry and Molecular Biology, University of Southern California, Keck School of Medicine, Los Angeles, CA, USA.
OVCAR-5 is a human epithelial carcinoma cell line of the ovary, established from the ascitic fluid of a patient with progressive ovarian adenocarcinoma without prior cytotoxic treatment. The unique growth pattern of ovarian carcinoma makes it an ideal model for examining the anticancer activity of contortrostatin (CN), a homodimeric disintegrin from southern copperhead venom. FACS analysis revealed that OVCAR-5 is integrin alphavbeta3 negative, but alphavbeta5 positive. Read More
Haemostasis 2001 May-Dec;31(3-6):177-82
Department of Medical Technology, McKinly Lab 057, University of Delaware, Newark, DE 19716, USA.
Viper venom disintegrins have been used frequently to study the cellular receptors which characterize various types of cells, including platelets, endothelial cells and cancer cells. While the majority of such analyses have pointed to involvement of integrin receptors alphavbeta3, alpha5beta1 or alphaIIbbeta3, this may not always be so. Eristostatin, from Eristocophis macmahoni, is a potent inhibitor of ADP-induced platelet aggregation as well as of human and murine melanoma metastases in mouse model systems. Read More
Haemostasis 2001 May-Dec;31(3-6):173-6
Laboratoire des Venins et Toxines, Institut Pasteur de Tunis, 13 Place Pasteur, BP 74, 1001 Tunis-Belvédère, Tunisia.
A novel C-lectin protein, lebecetin, was purified and characterized from the venom of Macrovipera lebetina. It is a disulfide-linked heterodimer of 15 and 16 kD. The subunits are homologous to each other and to the other snake venom proteins of the C-type (Ca(2+)-dependent) lectin superfamily. Read More
Haemostasis 2001 May-Dec;31(3-6):155-72
Department of Pharmacology, University of Oxford, Mansfield Road, Oxford, OX1 3QT, UK.
A large proportion of the biologically active proteins and peptides present within snake venoms interact with components of the haemostatic system to promote or inhibit the normal sequence of events that lead to clot formation. The venom proteins achieve their effects through interaction with various components of the coagulation cascade, endothelial matrix and platelets. Within the latter group, a number of venom proteins target the interaction of platelets with the major adhesive proteins, von Willebrand factor and collagen. Read More
Haemostasis 2001 May-Dec;31(3-6):148-54
Theodor Kocher Institute, University of Berne, Freiestrasse 1, CH-3012 Berne, Switzerland.
Snake venoms contain a wide range of components, many of which affect haemostasis by activation or inhibition of platelets or coagulation factors. They can be classified into groups based on structure and mode of action. One group is the snake C-type lectins, so called because of the typical folding which closely resembles that found in classical C-type lectins, such as selectins and mannose-binding proteins. Read More
Haemostasis 2001 May-Dec;31(3-6):141-7
Product Development/Mailstop 27-5-A, Amgen Inc., 1 Amgen Center Drive, Thousand Oaks, CA 91320, USA.
Alfimeprase is a recombinantly produced, truncated form of fibrolase, a known directly fibrinolytic zinc metalloproteinase that was first isolated from the venom of the southern copperhead snake (Agkistrodon contortrix contortrix). Both fibrolase and alfimeprase have been shown to have direct proteolytic activity against the fibrinogen Aalpha chain. In vivo pharmacology studies have shown that thrombolysis with alfimeprase is up to 6 times more rapid than with plasminogen activators. Read More
Haemostasis 2001 May-Dec;31(3-6):133-40
Venoms Unit, Institut Pasteur, 27-28 rue du Docteur-Roux, F-75724 Paris Cedex 15, France.
Snake venom serine proteinases affect many steps of the blood coagulation cascade. Each of them usually acts selectively on one coagulation factor. They are therefore potentially useful components to study the mechanisms of action, the regulation and the structure-function relationships of human serine proteinase coagulation factors. Read More
Haemostasis 2001 May-Dec;31(3-6):123-32
National Institute of Chemical Physics and Biophysics, Akadeemia tee 23, 12618 Tallinn, Estonia.
Our studies of the venom from the Levantine viper Vipera lebetina have demonstrated the existence of both coagulants and anticoagulants in the same venom. We showed that V. lebetina venom contains: (1) proteases that degrade fibrinogen, but not fibrin; (2) fibrinolytic enzyme (lebetase); (3) factor X activator (VLFXA); (4) factor V activator (VLFVA). Read More
Haemostasis 2001 May-Dec;31(3-6):118-22
Paion GmbH, Research Center Berlin, Tegeler Weg 33, D-10589 Berlin, Germany.
Plasminogen activators are enzymes found in all vertebrate species investigated so far. Their physiological function is the generation of localized proteolysis in the context of tissue remodeling, wound healing and neuronal plasticity. The common vampire bat (Desmodus rotundus) is a New World species that feeds exclusively on blood. Read More
Haemostasis 2001 May-Dec;31(3-6):118-305
Haemostasis 2001 Mar-Apr;31(2):106-12
Department of Pediatrics, Nara Medical University Hospital, 840 Shijo-Cho, Kashihara, Nara 634-8522, Japan.
We report the arthroscopic treatment of pigmented villonodular synovitis (PVNS) in a 13-year-old Japanese boy with congenital partial deficiency of plasminogen activator inhibitor-1 (PAI-1). He was admitted to our hospital with recurrent haemarthrosis of his right knee. Characteristic abnormalities of fibrinolysis included shortened euglobulin lysis time, low PAI-1 activity and low PAI-1 antigen levels. Read More