Plasma Contact Activation: a Revised Hypothesis
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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. -
Role of Thrombin and Thromboxane A2 in Reocclusion Following Coronary
Proc. Natl. Acad. Sci. USA Vol. 86, pp. 7585-7589, October 1989 Medical Sciences Role of thrombin and thromboxane A2 in reocclusion following coronary thrombolysis with tissue-type plasminogen activator (thrombolytic therapy/coronary thrombosis/platelet activation/reperfusion) DESMOND J. FITZGERALD*I* AND GARRET A. FITZGERALD* Divisions of *Clinical Pharmacology and tCardiology, Vanderbilt University, Nashville, TN 37232 Communicated by Philip Needleman, June 28, 1989 (receivedfor review April 12, 1989) ABSTRACT Reocclusion of the coronary artery occurs against the prothrombinase formed on the platelet surface after thrombolytic therapy of acute myocardlal infarction (13) and the neutralization ofheparin by platelet factor 4 (14) despite routine use of the anticoagulant heparin. However, and thrombospondin (15), proteins released by activated heparin is inhibited by platelet activation, which is greatly platelets. enhanced in this setting. Consequently, it is unclear whether To address the role of thrombin during coronary throm- thrombin induces acute reocclusion. To address this possibility, bolysis, we have examined the effect of a specific thrombin we examined the effect of argatroban {MCI9038, (2R,4R)- inhibitor, argatroban {MCI9038, (2R,4R)-4-methyl-1-[N-(3- 4-methyl-l-[Na-(3-methyl-1,2,3,4-tetrahydro-8-quinolinesulfo- methyl-1,2,3,4-tetrahydro-8-quinolinesulfonyl)-L-arginyl]-2- nyl)-L-arginyl]-2-piperidinecarboxylic acid}, a specific throm- piperidinecarboxylic acid} on the response to tissue plasmin- bin inhibitor, on the response to tissue-type plasminogen ogen activator (t-PA) in a closed-chest canine model of activator in a dosed-chest canine model of coronary thrombo- coronary thrombosis. MCI9038, an argimine derivative which sis. MCI9038 prolonged the thrombin time and shortened the binds to a hydrophobic pocket close to the active site of time to reperfusion (28 + 2 min vs. -
Systemic Thrombolysis in a Patient with Massive Pulmonary Embolism and Recent Glioblastoma Multiforme Resection
Unusual presentation of more common disease/injury BMJ Case Reports: first published as 10.1136/bcr-2017-221578 on 29 November 2017. Downloaded from CASE REPORT Systemic thrombolysis in a patient with massive pulmonary embolism and recent glioblastoma multiforme resection Joshua Lampert,1 Behnood Bikdeli,2 Philip Green,3 Matthew R Baldwin4 1Department of Internal SUMMARY and 2013 American College of Cardiology Foun- Medicine, Columbia University While trials of systemic thrombolysis for submassive and dation/AHA Task Force on Practice Guidelines list Medical Center, New York City, massive pulmonary embolism (PE) report intracranial known malignant intracranial neoplasm and brain New York, USA haemorrhage (ICH) rates of 2%–3%, the risk of ICH or spinal canal surgery within 2 months as absolute 2Division of Cardiology, in patients with recent brain surgery or intracranial contraindications to thrombolysis for treatment Columbia University Medical 8 9 Center, New York, NY neoplasm is unknown since these patients were of PE and ST-elevation myocardial infarction. 3Division of Cardiology, excluded from these trials. We report a case of massive The Neurocritical Care Society does not provide Columbia University Medical PE treated with systemic thrombolysis in a patient with guidelines for treatment of venous thromboembo- Center, New York, NY recent neurosurgery for an intracranial neoplasm. We lism (VTE). While the ACCP guidelines note that 4Division of Pulmonary discuss the risks and benefits of systemic thrombolysis the more severe the hypotension, the more compel- and Critical Care Medicine, for massive PE in the context of previous case reports, ling the indication for systemic thrombolysis, there Columbia University College of prior cohort studies and trials, and current guidelines. -
A Novel Detection Method of Cleaved Plasma High-Molecular-Weight Kininogen Reveals Its Correlation with Alzheimer’S Pathology and Cognitive Impairment
Alzheimer’s& Dementia: Diagnosis, Assessment & Disease Monitoring 10 (2018) 480-489 Blood-Based Biomarkers A novel detection method of cleaved plasma high-molecular-weight kininogen reveals its correlation with Alzheimer’s pathology and cognitive impairment Hitomi Yamamoto-Imotoa,b, Daria Zamolodchikova, Zu-Lin Chena, S. Lloyd Bournec, Syeda Rizvic, Pradeep Singha, Erin H. Norrisa, Frances Weis-Garciac, Sidney Stricklanda,* aPatricia and John Rosenwald Laboratory of Neurobiology and Genetics, The Rockefeller University, New York, NY, USA bResearch fellow of Japan Society for the Promotion of Science, Chiyoda-ku, Tokyo, Japan cAntibody and Bioresource Core Facility, Memorial Sloan Kettering Cancer Center, New York, NY, USA Abstract Introduction: Accumulation of b-amyloid is a pathological hallmark of Alzheimer’s disease (AD). b-Amyloid activates the plasma contact system leading to kallikrein-mediated cleavage of intact high-molecular-weight kininogen (HKi) to cleaved high-molecular-weight kininogen (HKc). Increased HKi cleavage is observed in plasma of AD patients and mouse models by Western blot. For potential diagnostic purposes, a more quantitative method that can measure HKc levels in plasma with high sensitivity and specificity is needed. Methods: HKi/c, HKi, and HKc monoclonal antibodies were screened from hybridomas using direct ELISA with a fluorescent substrate. Results: We generated monoclonal antibodies recognizing HKi or HKc specifically and developed sand- wich ELISAs that can quantitatively detect HKi and HKc levels in human. These new assays show that decreased HKi and increased HKc levels in AD plasma correlate with dementia and neuritic plaque scores. Discussion: High levels of plasma HKc could be used as an innovative biomarker for AD. -
High Molecular Weight Kininogen Contributes to Early Mortality and Kidney Dysfunction in a Mouse Model of Sickle Cell Disease
DR ERICA SPARKENBAUGH (Orcid ID : 0000-0002-5529-7847) DR NIGEL KEY (Orcid ID : 0000-0002-8930-4304) Article type : Original Article High molecular weight kininogen contributes to early mortality and kidney dysfunction in a mouse model of sickle cell disease. Erica M Sparkenbaugh1, Malgorzata Kasztan2, Michael W Henderson1, Patrick Ellsworth1, Parker Ross Davis2, Kathryn J Wilson1, Brandi Reeves1, Nigel S Key1,5, Sidney Strickland3, Keith McCrae4, David M. Pollock2, Rafal Pawlinski1* 1UNC Blood Research Center, Division of Hematology & Oncology, Department of Medicine, University of North Carolina at Chapel Hill, Chapel Hill, NC; 2Section of Cardio-Renal Physiology and Medicine, Division of Nephrology, Department of Medicine, University of Alabama at Birmingham, Birmingham, AL; 3Patricia and John Rosenwald Laboratory of Neurobiology and Genetics, The Rockefeller University, New York, NY; 4Taussig Cancer Institute, Department of Hematology Oncology, Cleveland Clinic, Cleveland, OH; and 5Department of Pathology and Laboratory Medicine, University of North Carolina at Chapel Hill, Chapel Hill, NC. *Address for correspondence Rafal Pawlinski 8008B Mary Ellen Jones Bldg, CB 7035 This article has been accepted for publication and undergone full peer review but has not been throughAccepted Article the copyediting, typesetting, pagination and proofreading process, which may lead to differences between this version and the Version of Record. Please cite this article as doi: 10.1111/JTH.14972 This article is protected by copyright. All rights reserved 116 Manning Drive Chapel Hill, NC 27599-7025 Ph: 919-843-8387 Fax: 919-843-4896 Email: [email protected] Word Counts Abstract: 179 Main Text: 3691 Figures: Main manuscript has 6 figures, 2 tables; supplement has 4 tables and 3 figures. -
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. -
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 -
T-Kininogen 1/2 (F-12): Sc-103886
SANTA CRUZ BIOTECHNOLOGY, INC. T-kininogen 1/2 (F-12): sc-103886 The Power to Question BACKGROUND SOURCE In rats, four types of kininogens are produced, two of which are classical T-kininogen 1/2 (F-12) is an affinity purified goat polyclonal antibody raised high and low molecular weight kininogens and two of which are low molec- against a peptide mapping within an internal region of T-kininogen 2 of rat ular weight-like kininogens, designated T-kininogen 1 and T-kininogen 2. origin. T-kininogen 1 and T-kininogen 2 are 430 amino acid secreted rat proteins that each contain three cystatin domains and have nearly identical functions. PRODUCT Existing in plasma, both T-kininogen 1 and T-kininogen 2 are glycoproteins Each vial contains 200 µg IgG in 1.0 ml of PBS with < 0.1% sodium azide that act as thiol protease inhibitors and also play a role in blood coagulation, and 0.1% gelatin. specifically by helping to optimally position blood coagulation factors. Additionally, T-kininogen 1 and T-kininogen 2 act as precursors of the active Blocking peptide available for competition studies, sc-103886 P, (100 µg peptide Bradykinin and, as such, effect vascular permeability, hypotension peptide in 0.5 ml PBS containing < 0.1% sodium azide and 0.2% BSA). and smooth muscle contraction. APPLICATIONS REFERENCES T-kininogen 1/2 (F-12) is recommended for detection of full length and heavy 1. Furuto-Kato, S., Matsumoto, A., Kitamura, N. and Nakanishi, S. 1985. chain of T-kininogen 1 and 2 of rat origin by Western Blotting (starting dilu- Primary structures of the mRNAs encoding the rat precursors for tion 1:200, dilution range 1:100-1:1000), immunofluorescence (starting dilu- bradykinin and T-kinin. -
Coagulation Factor XII Genetic Variation, Ex Vivo Thrombin Generation, and Stroke Risk in the Elderly: Results from the Cardiovascular Health Study
HHS Public Access Author manuscript Author ManuscriptAuthor Manuscript Author J Thromb Manuscript Author Haemost. Author Manuscript Author manuscript; available in PMC 2016 October 01. Published in final edited form as: J Thromb Haemost. 2015 October ; 13(10): 1867–1877. doi:10.1111/jth.13111. Coagulation factor XII genetic variation, ex vivo thrombin generation, and stroke risk in the elderly: results from the Cardiovascular Health Study N. C. Olson*, S. Butenas†, L. A. Lange‡, E. M. Lange‡,§, M. Cushman*,¶, N. S. Jenny*, J. Walston**, J. C. Souto††, J. M. Soria‡‡, G. Chauhan§§,¶¶, S. Debette§§,¶¶,***,†††, W.T. Longstreth‡‡‡,§§§, S. Seshadri†††, A.P. Reiner§§§, and R. P. Tracy*,† *Department of Pathology and Laboratory Medicine, University of Vermont College of Medicine, Burlington, VT †Department of Biochemistry, University of Vermont College of Medicine, Burlington, VT ¶Department of Medicine, University of Vermont College of Medicine, Burlington, VT ‡Department of Genetics, University of North Carolina School of Medicine, Chapel Hill, NC §Department of Biostatistics, University of North Carolina School of Medicine, Chapel Hill, NC **Division of Geriatric Medicine and Gerontology, Johns Hopkins University School of Medicine, Baltimore, MD ††Department of Haematology, Institute of Biomedical Research, (IIB-Sant Pau), Hospital de la Santa Creu i Sant Pau, Barcelona, Spain ‡‡Unit of Genomic of Complex Diseases, Institute of Biomedical Research, (IIB-Sant Pau), Hospital de la Santa Creu i Sant Pau, Barcelona, Spain §§INSERM U897, University of Bordeaux, Bordeaux, France ¶¶University of Bordeaux, Bordeaux, France ***Bordeaux University Hospital, Bordeaux, France †††Department of Neurology, Boston University School of Medicine, Boston, MA ‡‡‡Department of Neurology, University of Washington, Seattle, WA §§§Department of Epidemiology, University of Washington, Seattle, WA Correspondence: Russell P. -
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Florida State University Libraries Faculty Publications The Department of Biomedical Sciences 2010 Functional Intersection of the Kallikrein- Related Peptidases (KLKs) and Thrombostasis Axis Michael Blaber, Hyesook Yoon, Maria Juliano, Isobel Scarisbrick, and Sachiko Blaber Follow this and additional works at the FSU Digital Library. For more information, please contact [email protected] Article in press - uncorrected proof Biol. Chem., Vol. 391, pp. 311–320, April 2010 • Copyright ᮊ by Walter de Gruyter • Berlin • New York. DOI 10.1515/BC.2010.024 Review Functional intersection of the kallikrein-related peptidases (KLKs) and thrombostasis axis Michael Blaber1,*, Hyesook Yoon1, Maria A. locus (Gan et al., 2000; Harvey et al., 2000; Yousef et al., Juliano2, Isobel A. Scarisbrick3 and Sachiko I. 2000), as well as the adoption of a commonly accepted Blaber1 nomenclature (Lundwall et al., 2006), resolved these two fundamental issues. The vast body of work has associated 1 Department of Biomedical Sciences, Florida State several cancer pathologies with differential regulation or University, Tallahassee, FL 32306-4300, USA expression of individual members of the KLK family, and 2 Department of Biophysics, Escola Paulista de Medicina, has served to elevate the importance of the KLKs in serious Universidade Federal de Sao Paulo, Rua Tres de Maio 100, human disease and their diagnosis (Diamandis et al., 2000; 04044-20 Sao Paulo, Brazil Diamandis and Yousef, 2001; Yousef and Diamandis, 2001, 3 Program for Molecular Neuroscience and Departments of 2003; -
Activation of the Plasma Kallikrein-Kinin System in Respiratory Distress Syndrome
003 I-3998/92/3204-043 l$03.00/0 PEDIATRIC RESEARCH Vol. 32. No. 4. 1992 Copyright O 1992 International Pediatric Research Foundation. Inc. Printed in U.S.A. Activation of the Plasma Kallikrein-Kinin System in Respiratory Distress Syndrome OLA D. SAUGSTAD, LAILA BUP, HARALD T. JOHANSEN, OLAV RPISE, AND ANSGAR 0. AASEN Department of Pediatrics and Pediatric Research [O.D.S.].Institute for Surgical Research. University of Oslo [L.B.. A.O.A.], Rikshospitalet, N-0027 Oslo 1, Department of Surgery [O.R.],Oslo City Hospital Ullev~il University Hospital, N-0407 Oslo 4. Department of Pharmacology [H. T.J.],Institute of Pharmacy, University of Oslo. N-0316 Oslo 3, Norway ABSTRAm. Components of the plasma kallikrein-kinin proteins that interact in a complicated way. When activated, the and fibrinolytic systems together with antithrombin 111 contact factors plasma prekallikrein, FXII, and factor XI are were measured the first days postpartum in 13 premature converted to serine proteases that are capable of activating the babies with severe respiratory distress syndrome (RDS). complement, fibrinolytic, coagulation, and kallikrein-kinin sys- Seven of the patients received a single dose of porcine tems (7-9). Inhibitors regulate and control the activation of the surfactant (Curosurf) as rescue treatment. Nine premature cascades. C1-inhibitor is the most important inhibitor of the babies without lung disease or any other complicating contact system (10). It exerts its regulatory role by inhibiting disease served as controls. There were no differences in activated FXII, FXII fragment, and plasma kallikrein (10). In prekallikrein values between surfactant treated and non- addition, az-macroglobulin and a,-protease inhibitor inhibit treated RDS babies during the first 4 d postpartum. -
High Molecular Weight Kininogen Is an Inhibitor of Platelet Calpain
High molecular weight kininogen is an inhibitor of platelet calpain. A H Schmaier, … , D Schutsky, R W Colman J Clin Invest. 1986;77(5):1565-1573. https://doi.org/10.1172/JCI112472. Research Article Recent studies from our laboratory indicate that a high concentration of platelet-derived calcium-activated cysteine protease (calpain) can cleave high molecular weight kininogen (HMWK). On immunodiffusion and immunoblot, antiserum directed to the heavy chain of HMWK showed immunochemical identity with alpha-cysteine protease inhibitor--a major plasma inhibitor of tissue calpains. Studies were then initiated to determine whether purified or plasma HMWK was also an inhibitor of platelet calpain. Purified alpha-cysteine protease inhibitor, alpha-2-macroglobulin, as well as purified heavy chain of HMWK or HMWK itself inhibited purified platelet calpain. Kinetic analysis revealed that HMWK inhibited platelet calpain noncompetitively (Ki approximately equal to 5 nM). Incubation of platelet calpain with HMWK, alpha-2- macroglobulin, purified heavy chain of HMWK, or purified alpha-cysteine protease inhibitor under similar conditions resulted in an IC50 of 36, 500, 700, and 1,700 nM, respectively. The contribution of these proteins in plasma towards the inhibition of platelet calpain was investigated next. Normal plasma contained a protein that conferred a five to sixfold greater IC50 of purified platelet calpain than plasma deficient in either HMWK or total kininogen. Reconstitution of total kininogen deficient plasma with purified HMWK to normal levels (0.67 microM) completely corrected the subnormal inhibitory activity. However, reconstitution of HMWK deficient plasma to normal levels of low molecular weight kininogen (2.4 microM) did not fully correct the subnormal calpain inhibitory capacity […] Find the latest version: https://jci.me/112472/pdf High Molecular Weight Kininogen Is an Inhibitor of Platelet Calpain Alvin H.