Activation of Human Factor VII in Plasma and in Purified Systems
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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. -
Guideline on Clinical Investigation of Recombinant and Human Plasma-Derived 9 Factor IX Products’ (EMA/CHMP/BPWP/144552/2009 Rev
1 15 November 2018 2 EMA/CHMP/BPWP/144552/2009 rev. 2 Corr. 1 3 Committee for medicinal products for human use (CHMP) 4 Guideline on clinical investigation of recombinant and 5 human plasma-derived factor IX products 6 Draft Draft Agreed by Blood Products Working Party (BPWP) August 2018 Adopted by Committee for Medicinal Products for Human Use (CHMP) 15 November 2018 Start of public consultation 3 December 2018 End of public consultation 30 June 2019 7 8 This guideline replaces ‘Guideline on clinical investigation of recombinant and human plasma-derived 9 factor IX products’ (EMA/CHMP/BPWP/144552/2009 Rev. 1, Corr. 1) 10 Comments should be provided using this template. The completed comments form should be sent to [email protected] 11 Keywords Recombinant factor IX, plasma-derived factor IX, efficacy, safety, immunogenicity, inhibitor, thrombogenicity, anaphylactic reactions, potency assays 30 Churchill Place ● Canary Wharf ● London E14 5EU ● United Kingdom Telephone +44 (0)20 3660 6000 Facsimile +44 (0)20 3660 5555 Send a question via our website www.ema.europa.eu/contact An agency of the European Union © European Medicines Agency, 2019. Reproduction is authorised provided the source is acknowledged. 12 Guideline on the clinical investigation of recombinant and 13 human plasma-derived factor IX products 14 Table of contents 15 Executive summary ..................................................................................... 4 16 1. Introduction (background) ..................................................................... -
Role of the Renin–Angiotensin–Aldosterone and Kinin–Kallikrein Systems in the Cardiovascular Complications of COVID-19 and Long COVID
International Journal of Molecular Sciences Review Role of the Renin–Angiotensin–Aldosterone and Kinin–Kallikrein Systems in the Cardiovascular Complications of COVID-19 and Long COVID Samantha L. Cooper 1,2,*, Eleanor Boyle 3, Sophie R. Jefferson 3, Calum R. A. Heslop 3 , Pirathini Mohan 3, Gearry G. J. Mohanraj 3, Hamza A. Sidow 3, Rory C. P. Tan 3, Stephen J. Hill 1,2 and Jeanette Woolard 1,2,* 1 Division of Physiology, Pharmacology and Neuroscience, School of Life Sciences, University of Nottingham, Nottingham NG7 2UH, UK; [email protected] 2 Centre of Membrane Proteins and Receptors (COMPARE), School of Life Sciences, University of Nottingham, Nottingham NG7 2UH, UK 3 School of Medicine, Queen’s Medical Centre, University of Nottingham, Nottingham NG7 2UH, UK; [email protected] (E.B.); [email protected] (S.R.J.); [email protected] (C.R.A.H.); [email protected] (P.M.); [email protected] (G.G.J.M.); [email protected] (H.A.S.); [email protected] (R.C.P.T.) * Correspondence: [email protected] (S.L.C.); [email protected] (J.W.); Tel.: +44-115-82-30080 (S.L.C.); +44-115-82-31481 (J.W.) Abstract: Severe Acute Respiratory Syndrome Coronavirus 2 (SARS-CoV-2) is the virus responsible Citation: Cooper, S.L.; Boyle, E.; for the COVID-19 pandemic. Patients may present as asymptomatic or demonstrate mild to severe Jefferson, S.R.; Heslop, C.R.A.; and life-threatening symptoms. Although COVID-19 has a respiratory focus, there are major cardio- Mohan, P.; Mohanraj, G.G.J.; Sidow, vascular complications (CVCs) associated with infection. -
MONONINE (“Difficulty ® Monoclonal Antibody Purified in Concentrating”; Subject Recovered)
CSL Behring IU/kg (n=38), 0.98 ± 0.45 K at doses >95-115 IU/kg (n=21), 0.70 ± 0.38 K at doses >115-135 IU/kg (n=2), 0.67 K at doses >135-155 IU/kg (n=1), and 0.73 ± 0.34 K at doses >155 IU/kg (n=5). Among the 36 subjects who received these high doses, only one (2.8%) Coagulation Factor IX (Human) reported an adverse experience with a possible relationship to MONONINE (“difficulty ® Monoclonal Antibody Purified in concentrating”; subject recovered). In no subjects were thrombo genic complications MONONINE observed or reported.4 only The manufacturing procedure for MONONINE includes multiple processing steps that DESCRIPTION have been designed to reduce the risk of virus transmission. Validation studies of the Coagulation Factor IX (Human), MONONINE® is a sterile, stable, lyophilized concentrate monoclonal antibody (MAb) immunoaffinity chromatography/chemical treatment step and of Factor IX prepared from pooled human plasma and is intended for use in therapy nanofiltration step used in the production of MONONINE doc ument the virus reduction of Factor IX deficiency, known as Hemophilia B or Christmas disease. MONONINE is capacity of the processes employed. These studies were conducted using the rel evant purified of extraneous plasma-derived proteins, including Factors II, VII and X, by use of enveloped and non-enveloped viruses. The results of these virus validation studies utilizing immunoaffinity chromatography. A murine monoclonal antibody to Factor IX is used as an a wide range of viruses with different physicochemical properties are summarized in Table affinity ligand to isolate Factor IX from the source material. -
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. -
Gene Therapy Expression Vectors Based on the Clotting Factor IX Promoter
Gene Therapy (1999) 6, 1584–1589 1999 Stockton Press All rights reserved 0969-7128/99 $15.00 http://www.stockton-press.co.uk/gt Gene therapy expression vectors based on the clotting Factor IX promoter H Hoag, J Gore, D Barry and CR Mueller Department of Biochemistry and Cancer Research Laboratories, Queen’s University, Kingston, Ontario, Canada The liver is one of the prime targets for gene therapy, and moter. Introduction of this element increases promoter the correction of defects in a variety of clotting factor genes activity at least 20-fold over the proximal promoter alone is one of the main goals of liver-directed therapies. The use when assayed in the human liver cell line Hep G2. This of transcriptional regulatory elements derived from these optimized promoter is significantly more active than the genes may provide for the optimal expression of trans- SV40 enhancer/early promoter. The expression of the opti- duced genes. We have applied our knowledge of the pro- mized Factor IX promoter is also more persistent in the moter structure of the clotting Factor IX gene to design short term. The inclusion of a liver-specific locus control optimized expression vectors for use in gene therapy. The region, derived from the apolipoprotein E/C locus, did not activity of the proximal promoter has been augmented by further augment expression levels. These Factor IX vectors the introduction of a multimerized upstream site which we also exhibit a high degree of tissue specificity, as meas- have previously shown to be a prime regulator of the pro- ured by transfection into breast and muscle cell lines. -
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. -
Studies on a Complex Mechanism for the Activation of Plasminogen by Kaolin and by Chloroform: the Participation of Hageman Factor and Additional Cofactors
Studies on a complex mechanism for the activation of plasminogen by kaolin and by chloroform: the participation of Hageman factor and additional cofactors Derek Ogston, … , Oscar D. Ratnoff, Charles D. Forbes J Clin Invest. 1969;48(10):1786-1801. https://doi.org/10.1172/JCI106145. Research Article As demonstrated by others, fibrinolytic activity was generated in diluted, acidified normal plasma exposed to kaolin, a process requiring Hageman factor (Factor XII). Generation was impaired by adsorbing plasma with glass or similar agents under conditions which did not deplete its content of Hageman factor or plasminogen. The defect could be repaired by addition of a noneuglobulin fraction of plasma or an agent or agents eluted from diatomaceous earth which had been exposed to normal plasma. The restorative agent, tentatively called Hageman factor-cofactor, was partially purified by chromatography and had an apparent molecular weight of approximately 165,000. It could be distinguished from plasma thromboplastin antecedent (Factor XI) and plasma kallikrein, other substrates of Hageman factor, and from the streptokinase-activated pro-activator of plasminogen. Evidence is presented that an additional component may be needed for the generation of fibrinolytic activity in mixtures containing Hageman factor, HF-cofactor, and plasminogen. The long-recognized generation of plasmin activity in chloroform-treated euglobulin fractions of plasma was found to be dependent upon the presence of Hageman factor. Whether chloroform activation of plasminogen requires Hageman factor-cofactor was not determined, but glass-adsorbed plasma, containing Hageman factor and plasminogen, did not generate appreciable fibrinolytic or caseinolytic activity. These studies emphasize the complex nature of the mechanisms which lead to the generation of plasmin in human plasma. -
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. -
Phenotypic Correction of Factor IX Deficiency in Skin Fibroblasts
Proc. Nati. Acad. Sci. USA Vol. 87, pp. 5173-5177, July 1990 Genetics Phenotypic correction of factor IX deficiency in skin fibroblasts of hemophilic dogs (molecular cloning/hemophilia B/retroviral vectors/endothelial cells/gene therapy) J. H. AXELROD*, M. S. READt, K. M. BRINKHOUSt, AND 1. M. VERMA*t *Molecular Biology and Virology Laboratory, Salk Institute, Post Office Box 85800, San Diego, CA 92138; and tDepartment of Pathology and Center for Thrombosis and Hemostasis, University of North Carolina, Chapel Hill, NC 27599 Contributed by K. M. Brinkhous, April 24, 1990 ABSTRACT Primary skin fibroblasts from hemophilic endothelial cells as potential targets for gene transfer in the dogs were transduced by recombinant retrovirus (LNCdF9L) treatment of hemophilia B. containing a canine factor IX cDNA. High levels of biologically active canine factor IX (1.0 ,ug per 106 cells per 24 hr) were secreted in the medium. The level of factor IX produced MATERIALS AND METHODS increased substantially if the cells were stimulated by basic Construction and Isolation of a Canine Factor IX cDNA. A fibroblast growth factor during infection. Additionally, we also canine liver cDNA library was constructed using total cel- report that endothelial cells transduced by this virus can lular poly(A)+ RNA isolated from mongrel dog liver. cDNA produce high levels ofbiologically active factor IX. We propose was prepared using a cDNA synthesis kit (Pharmacia) and that skin fibroblasts and endothelial cells from hemophilia B ligated in the vector AZAP (Stratagene), which was packaged dogs may serve as potential venues for the development and with Gigapack Plus (Stratagene) according to the manufac- testing of models for treatment of hemophilia B by retrovirally turer's instructions. -
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