Ncounter Human Inflammation V2 Panel Gene List
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Hydrogels and Dentin–Pulp Complex Regeneration: from the Benchtop to Clinical Translation
polymers Review Hydrogels and Dentin–Pulp Complex Regeneration: From the Benchtop to Clinical Translation Marwa M. S. Abbass 1,2 , Aiah A. El-Rashidy 2,3 , Khadiga M. Sadek 2,3 , Sara El Moshy 1,2, Israa Ahmed Radwan 1,2 , Dina Rady 1,2 , Christof E. Dörfer 4 and Karim M. Fawzy El-Sayed 2,4,5,* 1 Oral Biology Department, Faculty of Dentistry, Cairo University, Cairo 11562, Egypt; [email protected] (M.M.S.A.); [email protected] (S.E.M.); [email protected] (I.A.R.); [email protected] (D.R.) 2 Stem Cells and Tissue Engineering Research Group, Faculty of Dentistry, Cairo University, Cairo 11562, Egypt; [email protected] (A.A.E.-R.); [email protected] (K.M.S.) 3 Biomaterials Department, Faculty of Dentistry, Cairo University, Cairo 11562, Egypt 4 Clinic for Conservative Dentistry and Periodontology, School of Dental Medicine, Christian Albrechts University, 24105 Kiel, Germany; [email protected] 5 Oral Medicine and Periodontology Department, Faculty of Dentistry, Cairo University, Cairo 11562, Egypt * Correspondence: [email protected] Received: 22 October 2020; Accepted: 10 November 2020; Published: 9 December 2020 Abstract: Dentin–pulp complex is a term which refers to the dental pulp (DP) surrounded by dentin along its peripheries. Dentin and dental pulp are highly specialized tissues, which can be affected by various insults, primarily by dental caries. Regeneration of the dentin–pulp complex is of paramount importance to regain tooth vitality. The regenerative endodontic procedure (REP) is a relatively current approach, which aims to regenerate the dentin–pulp complex through stimulating the differentiation of resident or transplanted stem/progenitor cells. -
By Map44 Pathway Activation in a Manner Inhibitable Pattern
Co-Complexes of MASP-1 and MASP-2 Associated with the Soluble Pattern-Recognition Molecules Drive Lectin Pathway Activation in a Manner Inhibitable This information is current as by MAp44 of September 28, 2021. Søren E. Degn, Lisbeth Jensen, Tomasz Olszowski, Jens C. Jensenius and Steffen Thiel J Immunol 2013; 191:1334-1345; Prepublished online 19 June 2013; Downloaded from doi: 10.4049/jimmunol.1300780 http://www.jimmunol.org/content/191/3/1334 http://www.jimmunol.org/ Supplementary http://www.jimmunol.org/content/suppl/2013/06/19/jimmunol.130078 Material 0.DC1 References This article cites 43 articles, 23 of which you can access for free at: http://www.jimmunol.org/content/191/3/1334.full#ref-list-1 Why The JI? Submit online. by guest on September 28, 2021 • Rapid Reviews! 30 days* from submission to initial decision • No Triage! Every submission reviewed by practicing scientists • Fast Publication! 4 weeks from acceptance to publication *average Subscription Information about subscribing to The Journal of Immunology is online at: http://jimmunol.org/subscription Permissions Submit copyright permission requests at: http://www.aai.org/About/Publications/JI/copyright.html Email Alerts Receive free email-alerts when new articles cite this article. Sign up at: http://jimmunol.org/alerts The Journal of Immunology is published twice each month by The American Association of Immunologists, Inc., 1451 Rockville Pike, Suite 650, Rockville, MD 20852 Copyright © 2013 by The American Association of Immunologists, Inc. All rights reserved. Print ISSN: 0022-1767 Online ISSN: 1550-6606. The Journal of Immunology Co-Complexes of MASP-1 and MASP-2 Associated with the Soluble Pattern-Recognition Molecules Drive Lectin Pathway Activation in a Manner Inhibitable by MAp44 Søren E. -
Barriers to the Identification of Occupational Asthma
BARRIERS TO THE IDENTIFICATION OF OCCUPATIONAL ASTHMA By Gareth Iestyn Walters A thesis submitted to The University of Birmingham for the degree of Doctor of Medicine School of Health and Populations Sciences College of Medical and Dental Sciences The University of Birmingham August 2014 DEDICATION This is for my father Derek Walters (1940-2011)… who would have kept a copy on the bookshelf, but probably wouldn’t have read it unless it was about Frederick the Great or the Stuart monarchy… which unfortunately it isn’t. ABSTRACT Occupational asthma accounts for 1 in 6 cases of new-onset adult asthma and is associated with an estimated societal cost in the UK of £100 million per annum. The cost is somewhat avoidable if workers with occupational asthma are identified quickly and removed from exposure to a sensitizing agent. However many workers with occupational asthma go undiagnosed or experience a lengthy delay in diagnosis. The aim of this work was to identify the barriers to diagnosis of occupational asthma on the part of the worker and of the healthcare professional. The first study evaluated current practice in assessing working-age asthmatics for occupational asthma in a West Midlands primary care population, using UK national guidelines as a reference standard. The recorded prevalence of occupational asthma was much lower than expected (0-0.8%) and there was poor enquiry regarding occupation (14% of cases) and the effect of work on asthma symptoms (2% of cases) by primary healthcare professionals. The second study used a qualitative methodology to explore and define health beliefs and behaviours in workers with occupational asthma symptoms. -
The Serine Protease Domain of MASP-3: Enzymatic Properties and Crystal Structure in Complex with Ecotin
The serine protease domain of MASP-3: enzymatic properties and crystal structure in complex with ecotin. Christine Gaboriaud, Rajesh Kumar Gupta, Lydie Martin, Monique Lacroix, Laurence Serre, Florence Teillet, Gérard J Arlaud, Véronique Rossi, Nicole Thielens To cite this version: Christine Gaboriaud, Rajesh Kumar Gupta, Lydie Martin, Monique Lacroix, Laurence Serre, et al.. The serine protease domain of MASP-3: enzymatic properties and crystal structure in complex with ecotin.. PLoS ONE, Public Library of Science, 2013, 8 (7), pp.e67962. 10.1371/journal.pone.0067962. inserm-00868926 HAL Id: inserm-00868926 https://www.hal.inserm.fr/inserm-00868926 Submitted on 2 Oct 2013 HAL is a multi-disciplinary open access L’archive ouverte pluridisciplinaire HAL, est archive for the deposit and dissemination of sci- destinée au dépôt et à la diffusion de documents entific research documents, whether they are pub- scientifiques de niveau recherche, publiés ou non, lished or not. The documents may come from émanant des établissements d’enseignement et de teaching and research institutions in France or recherche français ou étrangers, des laboratoires abroad, or from public or private research centers. publics ou privés. The Serine Protease Domain of MASP-3: Enzymatic Properties and Crystal Structure in Complex with Ecotin Christine Gaboriaud1,2,3*, Rajesh Kumar Gupta1,2,3¤a, Lydie Martin1,2,3, Monique Lacroix1,2,3, Laurence Serre3,1¤b, Florence Teillet1,2,3,Ge´rard J. Arlaud1,2,3,Ve´ronique Rossi1,2,3, Nicole M. Thielens1,2,3 1 Institut de Biologie Structurale (IBS), Direction des Sciences du Vivant, Commissariat a` l’Energie Atomique et aux Energies Alternatives, Grenoble, France, 2 IBS, Centre National de la Recherche Scientifique, Grenoble, France, 3 IBS, Universite´ Grenoble Alpes, Grenoble, France Abstract Mannan-binding lectin (MBL), ficolins and collectin-11 are known to associate with three homologous modular proteases, the MBL-Associated Serine Proteases (MASPs). -
On the Value of Therapeutic Interventions Targeting the Complement System in Acute Myocardial Infarction
UvA-DARE (Digital Academic Repository) The inflammatory response in myocarditis and acute myocardial infarction Emmens, R.W. Publication date 2016 Document Version Final published version Link to publication Citation for published version (APA): Emmens, R. W. (2016). The inflammatory response in myocarditis and acute myocardial infarction. General rights It is not permitted to download or to forward/distribute the text or part of it without the consent of the author(s) and/or copyright holder(s), other than for strictly personal, individual use, unless the work is under an open content license (like Creative Commons). Disclaimer/Complaints regulations If you believe that digital publication of certain material infringes any of your rights or (privacy) interests, please let the Library know, stating your reasons. In case of a legitimate complaint, the Library will make the material inaccessible and/or remove it from the website. Please Ask the Library: https://uba.uva.nl/en/contact, or a letter to: Library of the University of Amsterdam, Secretariat, Singel 425, 1012 WP Amsterdam, The Netherlands. You will be contacted as soon as possible. UvA-DARE is a service provided by the library of the University of Amsterdam (https://dare.uva.nl) Download date:02 Oct 2021 Chapter 5 On the value of therapeutic interventions targeting the complement system in acute myocardial infarction Reindert Emmens, Diana Wouters, Sacha Zeerleder, Marieke van Ham, Hans Niessen, Paul Krijnen Submitted for publication 81 SUMMARY The complement system plays an important role in the inflammatory response subsequent to acute myocardial infarction (AMI), by actively increasing cell death of cardiomyocytes beyond the primary infarcted area. -
Human Map44 HK359
Human MAp44 HK359 Edition 05-13 ELISA KIT PRODUCT INFORMATION & MANUAL Read carefully prior to starting procedures! For use in laboratory research only Not for clinical or diagnostic use Note that this user protocol is not lot-specific and is representative for the current specifications of this product. Please consult the vial label and the Certificate of Analysis for information on specific lots. Also note that shipping conditions may differ from storage conditions. For research use only. Not for use in or on humans or animals or for diagnostics. It is the responsibility of the user to comply with all local/state and federal rules in the use of this product. Hycult Biotech is not responsible for any patent infringements that might result from the use or derivation of this product. TABLE OF CONTENTS Page 1. Intended use ..................................................................................................................2 2. Introduction ....................................................................................................................2 3. Kit features ....................................................................................................................2 4. Protocol overview ..........................................................................................................3 5. Kit components and storage instructions .......................................................................4 Materials required but not provided 4 6. Warnings and precautions .............................................................................................5 -
Amino Acid-Based Polymeric Scaffold Fabrication And
AMINO ACID-BASED POLYMERIC SCAFFOLD FABRICATION AND MODIFICATION FOR BONE REGENERATION APPLICATIONS A Dissertation Presented to The Graduate Faculty of The University of Akron In Partial Fulfillment of the Requirements for the Degree Doctor of Philosophy Shan Li May, 2018 i AMINO ACID-BASED POLYMERIC SCAFFOLD FABRICATION AND MODIFICATION FOR BONE REGENERATION APPLICATIONS Shan Li Dissertation Approved: Accepted: Advisor Department Chair Dr. Matthew L Becker Dr. Coleen Pugh Committee Member Dean of the College Dr. Yu Zhu Dr. Eric J. Amis Committee Member Dean of the Graduate School Dr. Darrell H. Reneker Dr. Chand Midha Committee Member Date Dr. Toshikazu Miyoshi Committee Member Dr. Rebecca Kuntz Willits ii ABSTRACT Bone tissue engineering has evolved into an inter-disciplinary field of chemistry, engineering, and biology to regenerate defective tissues or organs since its emergence. Polymeric scaffolds represent one of the key components in bone tissue engineering and are widely used due to the low cost, unlimited supply, biointegrity, biodegradability, bioresorbability, tunable mechanical properties, non-toxicity and processability. It is designed to act as a 3D template to provide mechanical support and guide cells to form new tissue by mimicking ECM. Amino acid based poly(ester urea)s (PEUs) are high modulus, biodegradable, and non-toxic thermoplastic polymers, which have been synthesized and characterized by the Becker lab for their applications in tissue engineering. However, their inherent radiolucent and bioinert properties limit clinical application. Efforts have been made to modify PEUs with radiopacity for in vivo detection with X-rays and osteoinductivity via growth factor delivery for bone inducement. The advances in new technologies bring 3D printing to the scaffold fabrication. -
An Investigation of the Properties of Mixtures of Starches with Mono-Myristic Acid Triglyceride As Potential Selectively Digestible Films
An Investigation of the Properties of Mixtures of Starches with Mono-Myristic Acid Triglyceride as Potential Selectively Digestible Films. A dissertation submitted for the degree of Doctor of Philosophy by Christiane Charlotte Fertig at The School of Pharmacy Faculty of Medicine University of London October 2002 ProQuest Number: 10104897 All rights reserved INFORMATION TO ALL USERS The quality of this reproduction is dependent upon the quality of the copy submitted. In the unlikely event that the author did not send a complete manuscript and there are missing pages, these will be noted. Also, if material had to be removed, a note will indicate the deletion. uest. ProQuest 10104897 Published by ProQuest LLC(2016). Copyright of the Dissertation is held by the Author. All rights reserved. This work is protected against unauthorized copying under Title 17, United States Code. Microform Edition © ProQuest LLC. ProQuest LLC 789 East Eisenhower Parkway P.O. Box 1346 Ann Arbor, Ml 48106-1346 Abstract Abstract The aim of this work was the production of melt-films based on a mixture of unprocessed starch and a mono-myristic acid triglyceride for use as a coating on colon delivery formulations. The starches were embedded in the triglyceride-matrix during a melting process and drug release across the films was obtained by the digestion of the starch fraction through colonic a-amylases. During the first part of this study, the physicochemical properties of 7 starches, whose amylose content ranged from 0 % to nearly 100 %, were investigated and sub sequently correlated by statistical analysis. The second part comprised the identification of the optimum film formula with respect to film-forming temperature, starch content and film thickness. -
Strategies of Targeting Alternative and Lectin Pathway Components in Complement- Mediated Diseases
REVIEW published: 08 August 2018 doi: 10.3389/fimmu.2018.01851 Be on Target: Strategies of Targeting Alternative and Lectin Pathway Components in Complement- Mediated Diseases József Dobó, Andrea Kocsis and Péter Gál* Institute of Enzymology, Research Centre for Natural Sciences, Hungarian Academy of Sciences, Budapest, Hungary The complement system has moved into the focus of drug development efforts in the last decade, since its inappropriate or uncontrolled activation has been recognized in many diseases. Some of them are primarily complement-mediated rare diseases, such as paroxysmal nocturnal hemoglobinuria, C3 glomerulonephritis, and atypical hemolytic uremic syndrome. Complement also plays a role in various multifactorial diseases that affect millions of people worldwide, such as ischemia reperfusion injury (myocardial infarction, stroke), age-related macular degeneration, and several neurodegenerative disorders. In this review, we summarize the potential advantages of targeting various Edited by: complement proteins with special emphasis on the components of the lectin (LP) and Nicole Thielens, UMR5075 Institut de Biologie the alternative pathways (AP). The serine proteases (MASP-1/2/3, factor D, factor B), Structurale (IBS), France which are responsible for the activation of the cascade, are straightforward targets of Reviewed by: inhibition, but the pattern recognition molecules (mannose-binding lectin, other collectins, Cordula M. Stover, and ficolins), the regulatory components (factor H, factor I, properdin), and C3 are also University of Leicester, United Kingdom subjects of drug development. Recent discoveries about cross-talks between the LP Maciej Cedzynski, and AP offer new approaches for clinical intervention. Mannan-binding lectin-associated Institute for Medical Biology (PAN), Poland serine proteases (MASPs) are not just responsible for LP activation, but they are also Christian Drouet, indispensable for efficient AP activation. -
Role of Complement in Diabetes
This is a repository copy of Role of complement in diabetes. White Rose Research Online URL for this paper: http://eprints.whiterose.ac.uk/151783/ Version: Accepted Version Article: Ajjan, RA and Schroeder, V (2019) Role of complement in diabetes. Molecular Immunology, 114. pp. 270-277. ISSN 0161-5890 https://doi.org/10.1016/j.molimm.2019.07.031 (c) 2019, Elsevier Ltd. This manuscript version is made available under the CC-BY-NC-ND 4.0 license https://creativecommons.org/licenses/by-nc-nd/4.0/ Reuse This article is distributed under the terms of the Creative Commons Attribution-NonCommercial-NoDerivs (CC BY-NC-ND) licence. This licence only allows you to download this work and share it with others as long as you credit the authors, but you can’t change the article in any way or use it commercially. More information and the full terms of the licence here: https://creativecommons.org/licenses/ Takedown If you consider content in White Rose Research Online to be in breach of UK law, please notify us by emailing [email protected] including the URL of the record and the reason for the withdrawal request. [email protected] https://eprints.whiterose.ac.uk/ Molecular Immunology, Special Issue EMCHD 2019 Review Article Role of Complement in Diabetes Ramzi A. Ajjan a, Verena Schroeder b* a Leeds Institute for Cardiovascular and Metabolic Medicine, School of Medicine, University of Leeds, Leeds, United Kingdom b Experimental Haemostasis Group, Department for BioMedical Research (DBMR), University of Bern, Bern, Switzerland * Corresponding author: Verena Schroeder Experimental Haemostasis Group Department for BioMedical Research (DBMR) University of Bern Murtenstrasse 40 3008 Bern Switzerland Tel.: +41 31 632 9618 E-mail: [email protected] 1 Abstract Accumulating evidence suggests a role for the complement system in the pathogenesis of diabetes and the vascular complications that characterise this condition. -
MASP-1 and MASP-2 Do Not Activate Pro-FD in Resting Human
MASP-1 and MASP-2 do not activate pro-FD in resting human blood, while MASP-3 is a potential activator: kinetic analysis involving specific MASP-1 and MASP-2 inhibitors Gábor Oroszlán *, Elod Kortvely †, Dávid Szakács ‡, Andrea Kocsis *, Sascha Dammeier §, Anne Zeck ¶, Marius Ueffing †,§, Péter Závodszky *, Gábor Pál ‡ , Péter Gál *2, József Dobó *2 * Institute of Enzymology, Research Centre for Natural Sciences, Hungarian Academy of Sciences, Magyar tudósok krt. 2, H-1117, Budapest, Hungary † Institute for Ophthalmic Research, University of Tübingen, Röntgenweg 11, 72076 Tübingen, Germany ‡ Department of Biochemistry, Eötvös Loránd University, 1/C Pázmány Péter street, H-1117, Budapest, Hungary § Institute for Ophthalmic Research, Medical Proteome Center, University of Tübingen, Nägelestrasse 5, 72074 Tübingen, Germany ¶ Natural and Medical Sciences Institute at the University of Tübingen, Department of Bioanalytics, Markwiesenstrasse 55, 72770 Reutlingen, Germany 2 Address correspondence and reprint request to J. Dobó, and/or P. Gál, Institute of Enzymology, Research Centre for Natural Sciences, Hungarian Academy of Sciences, Magyar tudósok krt. 2, H- 1117, Budapest, Hungary, e-mail: [email protected] (J.D.), or [email protected] (P.G.), phone: +36-1-3826768, fax: +36-1-3826295 Running title: Kinetics of pro-FD activation Keywords (not in the title): lectin pathway; innate immunity; mannan-binding lectin; MBL- associated serine protease; thrombin; trypsin 1 Abstract It had been thought that complement factor D (FD) is activated at the site of synthesis and only FD lacking a propeptide is present in blood. The serum of MASP-1/3(-/-) mice contains pro-FD and has markedly reduced alternative pathway activity. -
Targeting of Liver Mannan-Binding Lectin
Targeting of Liver Mannan-Binding Lectin−Associated Serine Protease-3 with RNA Interference Ameliorates Disease in a Mouse Model of Rheumatoid Arthritis Downloaded from Nirmal K. Banda, Dhruv Desai, Robert I. Scheinman, Rasmus Pihl, Hideharu Sekine, Teizo Fujita, Vibha Sharma, Annette G. Hansen, Peter Garred, Steffen Thiel, Anna Borodovsky and V. Michael Holers http://www.immunohorizons.org/ ImmunoHorizons 2018, 2 (8) 274-295 http://www.immunohorizons.org/ doi: https://doi.org/10.4049/immunohorizons.1800053 http://www.immunohorizons.org/content/2/8/274 This information is current as of September 25, 2021. Supplementary http://www.immunohorizons.org/content/suppl/2018/09/14/2.8.274.DCSupp Material lemental by guest on September 25, 2021 References This article cites 60 articles, 25 of which you can access for free at: by guest on September 25, 2021 http://www.immunohorizons.org/content/2/8/274.full#ref-list-1 Email Alerts Receive free email-alerts when new articles cite this article. Sign up at: http://www.immunohorizons.org/alerts ImmunoHorizons is an open access journal published by The American Association of Immunologists, Inc., 1451 Rockville Pike, Suite 650, Rockville, MD 20852 All rights reserved. ISSN 2573-7732. RESEARCH ARTICLE Innate Immunity Targeting of Liver Mannan-Binding Lectin–Associated Serine Protease-3 with RNA Interference Ameliorates Disease in a Mouse Model of Rheumatoid Arthritis Nirmal K. Banda,*,1 Dhruv Desai,† Robert I. Scheinman,‡ Rasmus Pihl,§ Hideharu Sekine,{ Teizo Fujita,{ Vibha Sharma,|| Downloaded from Annette