Activation of Factor VII Bound to Tissue Factor: a Key Early Step in the Tissue Factor Pathway of Blood Coagulation (Hemost/Factor X/Factor IX) L
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The Production of Coagulation Factor VII by Adipocytes Is Enhanced by Tumor Necrosis Factor-Α Or Isoproterenol
International Journal of Obesity (2015) 39, 747–754 © 2015 Macmillan Publishers Limited All rights reserved 0307-0565/15 www.nature.com/ijo ORIGINAL ARTICLE The production of coagulation factor VII by adipocytes is enhanced by tumor necrosis factor-α or isoproterenol N Takahashi1,2, T Yoshizaki3, N Hiranaka1, O Kumano1,4, T Suzuki1,4, M Akanuma5,TYui5, K Kanazawa6, M Yoshida7, S Naito7, M Fujiya2, Y Kohgo2 and M Ieko1 BACKGROUND: A relationship has been reported between blood concentrations of coagulation factor VII (FVII) and obesity. In addition to its role in coagulation, FVII has been shown to inhibit insulin signals in adipocytes. However, the production of FVII by adipocytes remains unclear. OBJECTIVE: We herein investigated the production and secretion of FVII by adipocytes, especially in relation to obesity-related conditions including adipose inflammation and sympathetic nerve activation. METHODS: C57Bl/6J mice were fed a low- or high-fat diet and the expression of FVII messenger RNA (mRNA) was then examined in adipose tissue. 3T3-L1 cells were used as an adipocyte model for in vitro experiments in which these cells were treated with tumor necrosis factor-α (TNF-α) or isoproterenol. The expression and secretion of FVII were assessed by quantitative real-time PCR, Western blotting and enzyme-linked immunosorbent assays. RESULTS: The expression of FVII mRNA in the adipose tissue of mice fed with high-fat diet was significantly higher than that in mice fed with low-fat diet. Expression of the FVII gene and protein was induced during adipogenesis and maintained in mature adipocytes. The expression and secretion of FVII mRNA were increased in the culture medium of 3T3-L1 adipocytes treated with TNF-α, and these effects were blocked when these cells were exposed to inhibitors of mitogen-activated kinases or NF-κB activation. -
The Rare Coagulation Disorders
Treatment OF HEMOPHILIA April 2006 · No. 39 THE RARE COAGULATION DISORDERS Paula HB Bolton-Maggs Department of Haematology Manchester Royal Infirmary Manchester, United Kingdom Published by the World Federation of Hemophilia (WFH) © World Federation of Hemophilia, 2006 The WFH encourages redistribution of its publications for educational purposes by not-for-profit hemophilia organizations. In order to obtain permission to reprint, redistribute, or translate this publication, please contact the Communications Department at the address below. This publication is accessible from the World Federation of Hemophilia’s web site at www.wfh.org. Additional copies are also available from the WFH at: World Federation of Hemophilia 1425 René Lévesque Boulevard West, Suite 1010 Montréal, Québec H3G 1T7 CANADA Tel. : (514) 875-7944 Fax : (514) 875-8916 E-mail: [email protected] Internet: www.wfh.org The Treatment of Hemophilia series is intended to provide general information on the treatment and management of hemophilia. The World Federation of Hemophilia does not engage in the practice of medicine and under no circumstances recommends particular treatment for specific individuals. Dose schedules and other treatment regimes are continually revised and new side effects recognized. WFH makes no representation, express or implied, that drug doses or other treatment recommendations in this publication are correct. For these reasons it is strongly recommended that individuals seek the advice of a medical adviser and/or to consult printed instructions provided by the pharmaceutical company before administering any of the drugs referred to in this monograph. Statements and opinions expressed here do not necessarily represent the opinions, policies, or recommendations of the World Federation of Hemophilia, its Executive Committee, or its staff. -
Coagulation Factors Directly Cleave SARS-Cov-2 Spike and Enhance Viral Entry
bioRxiv preprint doi: https://doi.org/10.1101/2021.03.31.437960; this version posted April 1, 2021. The copyright holder for this preprint (which was not certified by peer review) is the author/funder. All rights reserved. No reuse allowed without permission. Coagulation factors directly cleave SARS-CoV-2 spike and enhance viral entry. Edward R. Kastenhuber1, Javier A. Jaimes2, Jared L. Johnson1, Marisa Mercadante1, Frauke Muecksch3, Yiska Weisblum3, Yaron Bram4, Robert E. Schwartz4,5, Gary R. Whittaker2 and Lewis C. Cantley1,* Affiliations 1. Meyer Cancer Center, Department of Medicine, Weill Cornell Medical College, New York, NY, USA. 2. Department of Microbiology and Immunology, Cornell University, Ithaca, New York, USA. 3. Laboratory of Retrovirology, The Rockefeller University, New York, NY, USA. 4. Division of Gastroenterology and Hepatology, Department of Medicine, Weill Cornell Medicine, New York, NY, USA. 5. Department of Physiology, Biophysics and Systems Biology, Weill Cornell Medicine, New York, NY, USA. *Correspondence: [email protected] bioRxiv preprint doi: https://doi.org/10.1101/2021.03.31.437960; this version posted April 1, 2021. The copyright holder for this preprint (which was not certified by peer review) is the author/funder. All rights reserved. No reuse allowed without permission. Summary Coagulopathy is recognized as a significant aspect of morbidity in COVID-19 patients. The clotting cascade is propagated by a series of proteases, including factor Xa and thrombin. Other host proteases, including TMPRSS2, are recognized to be important for cleavage activation of SARS-CoV-2 spike to promote viral entry. Using biochemical and cell-based assays, we demonstrate that factor Xa and thrombin can also directly cleave SARS-CoV-2 spike, enhancing viral entry. -
Blood Coagulation Factor X Exerts Differential Effects on Adenovirus Entry Into Human Lymphocytes
viruses Article Blood Coagulation Factor X Exerts Differential Effects on Adenovirus Entry into Human Lymphocytes James S. Findlay 1, Graham P. Cook 2 and G. Eric Blair 1,* ID 1 School of Molecular and Cellular Biology, University of Leeds, Leeds LS2 9JT, UK; jsfi[email protected] 2 Leeds Institute of Cancer and Pathology, University of Leeds, St. James’s University Hospital, Leeds LS9 7TF, UK; [email protected] * Correspondence: [email protected]; Tel.: +44-113-343-3128 Received: 5 December 2017; Accepted: 30 December 2017; Published: 3 January 2018 Abstract: It has been proposed that blood coagulation factors, principally factor X (FX), enhance the uptake of human adenovirus type 5 (Ad5) into cultured epithelial cells by bridging the viral hexon capsid protein and cell-surface heparan sulphate proteoglycans (HSPGs). We studied the effects of FX on Ad transduction of lymphoid cell lines (NK92MI, a natural killer cell line; Daudi, a B-cell line and Jurkat, a T-cell line) as well as primary peripheral blood lymphocytes (PBL) and HeLa epithelial cells using either replication-deficient Ad5, or a derivative in which the Ad5 fiber was replaced with that of another Ad type, Ad35, termed Ad5F35. PBL and NK92MI were resistant to Ad5 transduction. Transduction of Jurkat and Daudi cells by Ad5 was reduced by FX but without discernible effects on cell-surface Ad5 binding. FX reduced virus binding and transduction of all lymphoid cell lines by Ad5F35, as well as transduction of the T- and Natural Killer (NK)-cell populations of PBL. Flow cytometry analysis showed that all lymphoid cell lines were negative for HSPG components, in contrast to HeLa cells. -
Urokinase and Urokinase Receptor in the Urinary Tract of the Dog Trina Racquel Bailey Louisiana State University and Agricultural and Mechanical College
Louisiana State University LSU Digital Commons LSU Master's Theses Graduate School 2005 Urokinase and urokinase receptor in the urinary tract of the dog Trina Racquel Bailey Louisiana State University and Agricultural and Mechanical College Follow this and additional works at: https://digitalcommons.lsu.edu/gradschool_theses Part of the Veterinary Medicine Commons Recommended Citation Bailey, Trina Racquel, "Urokinase and urokinase receptor in the urinary tract of the dog" (2005). LSU Master's Theses. 1457. https://digitalcommons.lsu.edu/gradschool_theses/1457 This Thesis is brought to you for free and open access by the Graduate School at LSU Digital Commons. It has been accepted for inclusion in LSU Master's Theses by an authorized graduate school editor of LSU Digital Commons. For more information, please contact [email protected]. UROKINASE AND UROKINASE RECEPTOR IN THE URINARY TRACT OF THE DOG A Thesis Submitted to the Graduate Faculty of the Louisiana State University and Agricultural and Mechanical College in partial fulfillment of the requirements for the degree of Master of Science In The Interdepartmental Program in Veterinary Medical Sciences through the Department of Veterinary Clinical Sciences by Trina Racquel Bailey BSc, Doctor of Veterinary Medicine Atlantic Veterinary College, University of Prince Edward Island, 2000 December 2005 To my husband John, who has been there to help me through it all. To my son Ewan, who makes everything worthwhile. To my family and family in law for all their love, help and support. To Dude, Bailey, Sarah, Scamp, Ellie, Abby, and all the other wonderful animals who have been there for me to love and have allowed me to learn. -
360 BCBSA Reference Number: 2.01.13
Pharmacy Medical Policy Human Anti-hemophilic Factor Table of Contents • Policy: Commercial • Policy History • Endnotes • Policy: Medicare • Information Pertaining to All Policies • Forms • Coding Information • References Policy Number: 360 BCBSA Reference Number: 2.01.13 Related Policies None Policy Commercial Members: Managed Care (HMO and POS), PPO, and Indemnity Note: All requests for indications listed and not listed on the medical policy guidelines may be submitted to BCBSMA Pharmacy Operations by completing the Prior Authorization Form on the last page of this document. This medication is not covered by the pharmacy benefit. It is covered by the Medical Benefit or as a Home Infusion Therapy. We may cover: Factor VII • Coagulation factor indicated for the treatment of bleeding episodes and perioperative management in adults and children with hemophilia A or B with inhibitors, congenital Factor VII (FVII) deficiency, and Glanzmann’s thrombasthenia with refractoriness to platelet transfusions, with or without antibodies to platelets & Treatment of bleeding episodes and perioperative management in adults with acquired hemophilia. Factor VIII • Human anti-hemophilic factor (AHF) maintenance therapy (prophylaxis) as needed to maintain trough levels at 1% or greater in patients with severe Hemophilia A (AHF activity less than 1% of normal).1 • Human anti-hemophilic factor (AHF) for treatment and/or management of bleeding episodes in surgical patients with mild hemophilia (AHF activity 5%-30%) or moderately severe hemophilia (AHF activity -
1 Elevated Protein Levels and Altered Cellular Expression of Factor VII
Thorax Online First, published on May 4, 2007 as 10.1136/thx.2006.069658 Elevated protein levels and altered cellular expression of factor VII-activating protease Thorax: first published as 10.1136/thx.2006.069658 on 4 May 2007. Downloaded from (FSAP) in the lungs of patients with acute respiratory distress syndrome (ARDS) Malgorzata Wygrecka1*, Philipp Markart2*, Ludger Fink3, Andreas Guenther2, and Klaus T. Preissner1 Departments of 1Biochemistry, 2Internal Medicine, and 3Pathology, Faculty of Medicine, University of Giessen Lung Center, Giessen, Germany Corresponding author: Malgorzata Wygrecka, PhD Department of Biochemistry, Faculty of Medicine, University of Giessen Lung Center, Friedrichstrasse 24, 35392 Giessen, Germany Phone: +49-641-99-47501 Fax: +49-641-99-47509 [email protected] http://thorax.bmj.com/ on September 27, 2021 by guest. Protected copyright. Keywords: acute lung injury, acute respiratory distress syndrome, factor VII and single-chain plasminogen activator-activating protease, hemostasis, hyaluronan binding protein 2 Word count: 4040 * both authors contributed equally to the manuscript 1 Copyright Article author (or their employer) 2007. Produced by BMJ Publishing Group Ltd (& BTS) under licence. ABSTRACT Thorax: first published as 10.1136/thx.2006.069658 on 4 May 2007. Downloaded from Background: ARDS is characterized by inflammation of the lung parenchyma and alterations of the alveolar haemostasis with extravascular fibrin deposition. Factor VII-activating protease (FSAP) is a recently described serine protease in plasma and tissues, known to be involved in haemostasis, cell proliferation and migration. Methods: We investigated FSAP protein (western blotting/ELISA/immunohistochemistry) and activity (coagulation/fibrinolysis assays) in plasma, bronchoalveolar lavage (BAL) fluids and lung tissue of mechanically ventilated patients with early ARDS as compared to patients with cardiogenic pulmonary oedema and healthy controls. -
Factor IX Complex (Human - Bebulin, Profilnine) Reference Number: ERX.SPMN.201 Effective Date: 01/17 Coding Implications Last Review Date: Revision Log
Clinical Policy: Factor IX complex (Human - Bebulin, Profilnine) Reference Number: ERX.SPMN.201 Effective Date: 01/17 Coding Implications Last Review Date: Revision Log See Important Reminder at the end of this policy for important regulatory and legal information. Policy/Criteria It is the policy of health plans affiliated with Envolve Pharmacy SolutionsTM that factor IX complex (Bebulin®, Profilnine®) is medically necessary when the following criteria are met: I. Initial Approval Criteria A. Hemophilia B (must meet all): 1. Prescribed by or in consultation with a hematologist; 2. Diagnosis of hemophilia B; 3. Agent will used for prevention/control of bleeding episodes. Approval duration: 3 months B. Other diagnoses/indications: Refer to ERX.SPMN.16 - Global Biopharm Policy. II. Continued Approval A. Hemophilia B (must meet all): 1. Currently receiving medication via health plan benefit or member has previously met all initial approval criteria. Approval duration: 3 months B. Other diagnoses/indications (must meet 1 or 2): 1. Currently receiving medication via health plan benefit and documentation supports positive response to therapy; or 2. Refer to ERX.SPMN.16 - Global Biopharm Policy. Background Description/Mechanism of Action: Factor IX complex replaces deficient clotting factors including factor X. Hemophilia B, or Christmas disease, is an X-linked recessively inherited disorder of blood coagulation characterized by insufficient or abnormal synthesis of the clotting protein factor IX. Factor IX is a vitamin K-dependent coagulation factor which is synthesized in the liver. Factor IX is activated by factor XIa in the intrinsic coagulation pathway. Activated factor IX (IXa), in combination with factor VII: C, activates factor X to Xa, resulting ultimately in the conversion of prothrombin to thrombin and the formation of a fibrin clot. -
(12) United States Patent (10) Patent No.: US 9,370,583 B2 Oestergaard Et Al
US009370583B2 (12) United States Patent (10) Patent No.: US 9,370,583 B2 Oestergaard et al. (45) Date of Patent: Jun. 21, 2016 (54) COAGULATION FACTOR VII POLYPEPTIDES 2015,0105321 A1 4/2015 Oestergaard et al. 2015,0225711 A1 8, 2015 Behrens et al. (71) Applicant: Novo Nordisk HealthCare AG, Zurich 2015,0259665 A1 9/2015 Behrens et al. (CH) FOREIGN PATENT DOCUMENTS (72) Inventors: Henrik Oestergaard, Oelstykke (DK); WO O158935 A2 8, 2001 Prafull S. Gandhi, Ballerup (DK); Ole WO O2/22776 A2 3, 2002 Hvilsted Olsen, Broenshoe (DK); WO O3O31464 A2 4/2003 Carsten Behrens, Koebenhavn N (DK); WO 2005/O14035 A2 2, 2005 WO 2005, O75635 A2 8, 2005 Paul L. DeAngelis, Edmond, OK (US); WO 2006/127896 A2 11/2006 Friedrich Michael Haller, Norman, OK WO 2006,134174 A2 12/2006 (US) WO 2007022512 A2 2, 2007 WO 2007/031559 A2 3, 2007 (73) Assignee: NOVO NORDISK HEALTHCARE WO 2008/O25856 A2 3, 2008 WO 2008/074032 A1 6, 2008 AG, Zurich (CH) WO 20081277O2 A2 10, 2008 WO 2009 126307 A2 10, 2009 (*) Notice: Subject to any disclaimer, the term of this WO 2010/030342 A2 3, 2010 patent is extended or adjusted under 35 WO 2011092242 A1 8, 2011 U.S.C. 154(b) by 0 days. WO 2011 1 01277 A1 8, 2011 WO 2012/OO7324 A2 1, 2012 WO 2012O35050 A2 3, 2012 (21) Appl. No.: 14/936,224 WO 2014/060401 4/2014 WO 201406.0397 A1 4/2014 (22) Filed: Nov. 9, 2015 WO 2014140.103 A2 9, 2014 OTHER PUBLICATIONS (65) Prior Publication Data Agersoe.H. -
General Considerations of Coagulation Proteins
ANNALS OF CLINICAL AND LABORATORY SCIENCE, Vol. 8, No. 2 Copyright © 1978, Institute for Clinical Science General Considerations of Coagulation Proteins DAVID GREEN, M.D., Ph.D.* Atherosclerosis Program, Rehabilitation Institute of Chicago, Section of Hematology, Department of Medicine, and Northwestern University Medical School, Chicago, IL 60611. ABSTRACT The coagulation system is part of the continuum of host response to injury and is thus intimately involved with the kinin, complement and fibrinolytic systems. In fact, as these multiple interrelationships have un folded, it has become difficult to define components as belonging to just one system. With this limitation in mind, an attempt has been made to present the biochemistry and physiology of those factors which appear to have a dominant role in the coagulation system. Coagulation proteins in general are single chain glycoprotein molecules. The reactions which lead to their activation are usually dependent on the presence of an appropriate surface, which often is a phospholipid micelle. Large molecular weight cofactors are bound to the surface, frequently by calcium, and act to induce a favorable conformational change in the reacting molecules. These mole cules are typically serine proteases which remove small peptides from the clotting factors, converting the single chain species to two chain molecules with active site exposed. The sequence of activation is defined by the enzymes and substrates involved and eventuates in fibrin formation. Mul tiple alternative pathways and control mechanisms exist throughout the normal sequence to limit coagulation to the area of injury and to prevent interference with the systemic circulation. Introduction RatnofP4 eloquently indicates in an arti cle aptly entitled: “A Tangled Web. -
Plasma Kallikrein Modulates Immune Cell Trafficking During Neuroinflammation Via PAR2 and Bradykinin Release
Plasma kallikrein modulates immune cell trafficking during neuroinflammation via PAR2 and bradykinin release Kerstin Göbela,1,2, Chloi-Magdalini Asaridoua,2, Monika Merkera, Susann Eichlera, Alexander M. Herrmanna, Eva Geußb, Tobias Rucka, Lisa Schüngela,c, Linda Groenewega, Venu Narayanana, Tilman Schneider-Hohendorfa, Catharina C. Grossa, Heinz Wiendla, Beate E. Kehrelc, Christoph Kleinschnitzd,3, and Sven G. Meutha,3 aClinic of Neurology, Institute of Translational Neurology, University of Münster, 48149 Münster, Germany; bDepartment of Neurology, University Hospital Würzburg, 97080 Würzburg, Germany; cClinic of Anesthesiology, Intensive Care and Pain Medicine, Experimental and Clinical Haemostasis, University of Münster, 48149 Münster, Germany; and dDepartment of Neurology, University Hospital Essen, 45147 Essen, Germany Edited by Lawrence Steinman, Stanford University School of Medicine, Stanford, CA, and approved November 19, 2018 (received for review June 11, 2018) Blood–brain barrier (BBB) disruption and transendothelial trafficking peptidebradykinin(BK).Atthesametime,KKcanactivateFXIIin of immune cells into the central nervous system (CNS) are pathophys- a positive feedback loop, thereby leading to both activation of the iological hallmarks of neuroinflammatory disorders like multiple scle- intrinsic coagulation cascade and the proinflammatory KKS (14, rosis (MS). Recent evidence suggests that the kallikrein-kinin and 15). Additionally, KK may interact with cell-surface–associated re- coagulation system might participate in this process. Here, we iden- ceptors, such as the protease-activated receptors 1 (PAR1) and 2 tify plasma kallikrein (KK) as a specific direct modulator of BBB in- (PAR2) (16). tegrity. Levels of plasma prekallikrein (PK), the precursor of KK, were As KK has this dual mode of action (inflammation and co- markedly enhanced in active CNS lesions of MS patients. -
Assessing Plasmin Generation in Health and Disease
International Journal of Molecular Sciences Review Assessing Plasmin Generation in Health and Disease Adam Miszta 1,* , Dana Huskens 1, Demy Donkervoort 1, Molly J. M. Roberts 1, Alisa S. Wolberg 2 and Bas de Laat 1 1 Synapse Research Institute, 6217 KD Maastricht, The Netherlands; [email protected] (D.H.); [email protected] (D.D.); [email protected] (M.J.M.R.); [email protected] (B.d.L.) 2 Department of Pathology and Laboratory Medicine and UNC Blood Research Center, University of North Carolina at Chapel Hill, Chapel Hill, NC 27599, USA; [email protected] * Correspondence: [email protected]; Tel.: +31-(0)-433030693 Abstract: Fibrinolysis is an important process in hemostasis responsible for dissolving the clot during wound healing. Plasmin is a central enzyme in this process via its capacity to cleave fibrin. The ki- netics of plasmin generation (PG) and inhibition during fibrinolysis have been poorly understood until the recent development of assays to quantify these metrics. The assessment of plasmin kinetics allows for the identification of fibrinolytic dysfunction and better understanding of the relationships between abnormal fibrin dissolution and disease pathogenesis. Additionally, direct measurement of the inhibition of PG by antifibrinolytic medications, such as tranexamic acid, can be a useful tool to assess the risks and effectiveness of antifibrinolytic therapy in hemorrhagic diseases. This review provides an overview of available PG assays to directly measure the kinetics of plasmin formation and inhibition in human and mouse plasmas and focuses on their applications in defining the role of plasmin in diseases, including angioedema, hemophilia, rare bleeding disorders, COVID- 19, or diet-induced obesity.