Structural Insight on the Recognition of Surface-Bound Opsonins by the Integrin I Domain of Complement Receptor 3
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Propranolol-Mediated Attenuation of MMP-9 Excretion in Infants with Hemangiomas
Supplementary Online Content Thaivalappil S, Bauman N, Saieg A, Movius E, Brown KJ, Preciado D. Propranolol-mediated attenuation of MMP-9 excretion in infants with hemangiomas. JAMA Otolaryngol Head Neck Surg. doi:10.1001/jamaoto.2013.4773 eTable. List of All of the Proteins Identified by Proteomics This supplementary material has been provided by the authors to give readers additional information about their work. © 2013 American Medical Association. All rights reserved. Downloaded From: https://jamanetwork.com/ on 10/01/2021 eTable. List of All of the Proteins Identified by Proteomics Protein Name Prop 12 mo/4 Pred 12 mo/4 Δ Prop to Pred mo mo Myeloperoxidase OS=Homo sapiens GN=MPO 26.00 143.00 ‐117.00 Lactotransferrin OS=Homo sapiens GN=LTF 114.00 205.50 ‐91.50 Matrix metalloproteinase‐9 OS=Homo sapiens GN=MMP9 5.00 36.00 ‐31.00 Neutrophil elastase OS=Homo sapiens GN=ELANE 24.00 48.00 ‐24.00 Bleomycin hydrolase OS=Homo sapiens GN=BLMH 3.00 25.00 ‐22.00 CAP7_HUMAN Azurocidin OS=Homo sapiens GN=AZU1 PE=1 SV=3 4.00 26.00 ‐22.00 S10A8_HUMAN Protein S100‐A8 OS=Homo sapiens GN=S100A8 PE=1 14.67 30.50 ‐15.83 SV=1 IL1F9_HUMAN Interleukin‐1 family member 9 OS=Homo sapiens 1.00 15.00 ‐14.00 GN=IL1F9 PE=1 SV=1 MUC5B_HUMAN Mucin‐5B OS=Homo sapiens GN=MUC5B PE=1 SV=3 2.00 14.00 ‐12.00 MUC4_HUMAN Mucin‐4 OS=Homo sapiens GN=MUC4 PE=1 SV=3 1.00 12.00 ‐11.00 HRG_HUMAN Histidine‐rich glycoprotein OS=Homo sapiens GN=HRG 1.00 12.00 ‐11.00 PE=1 SV=1 TKT_HUMAN Transketolase OS=Homo sapiens GN=TKT PE=1 SV=3 17.00 28.00 ‐11.00 CATG_HUMAN Cathepsin G OS=Homo -
Complement Component 3 (C3) Concentrations in Cancer Patients: a Systematic Review and Meta-Analysis
Complement Component 3 (C3) Concentrations in Cancer Patients: A Systematic Review and Meta-Analysis Zipeng Yang South China Agricultural University Zi-Guo Yuan ( [email protected] ) Anqun Yang Dapeng New District Nan'ao Peolple's Hospital of Shenzhen, Guangdong Province, China Xiu-Xiang Zhang South China Agricultural University College of Agriculture Xiaohu Wang Guangdong Academy of Agricultural Sciences, Guangzhou, Guangdong Province Miao Yu Dongfeng Xiyuan District, Stomatological Hospital Aliated to Guangzhou Medical University, Guangzhou Yasser S.Mahmmod Zagazig University Jorge A Hernandez University of Florida Zhaowen Ren South China Agricultural University Xirui Zhang South China Agricultural University Wei Cong Shandong University Research article Keywords: Complement Component 3, Cancer Patients, Meta-Analysis Posted Date: March 26th, 2020 DOI: https://doi.org/10.21203/rs.3.rs-18256/v1 License: This work is licensed under a Creative Commons Attribution 4.0 International License. Read Full License Page 1/17 Abstract Background The aim of this study was to investigate the association between the serum complement component 3 “C3” level and the patients with different types of cancer. Our study nding would ultimately provide reliable scientic conclusions to guide clinical practice. Methods PubMed, Embase, The Chorane Library and Google Scholar were systematically searched to identify all studies on serum C3 concentrations in cancer patients published as of September 2019. Additionally, we conducted a clinical study on serum C3 in lung cancer patients and healthy people. The levels of serum complement C3 in 84 lung cancer patients and 30 healthy people were examined by ELISA. We used standardized mean differences (SMD) to report the pooled estimation, and I² statistics were calculated to examine the heterogeneity. -
Genetic Susceptibility to Chronic Wasting Disease in Free-Ranging White-Tailed Deer: Complement Component C1q and Prnp Polymorphisms Julie A
Natural Resource Ecology and Management Natural Resource Ecology and Management Publications 12-2009 Genetic susceptibility to chronic wasting disease in free-ranging white-tailed deer: Complement component C1q and Prnp polymorphisms Julie A. Blanchong Iowa State University, [email protected] Dennis M. Heisey United States Geological Survey Kim T. Scribner Michigan State University Scot V. Libants Michigan State University Chad Johnson UFonilvloerwsit ythi of sW aiscondn asiddn - itMionadisoaln works at: http://lib.dr.iastate.edu/nrem_pubs Part of the Animal Diseases Commons, Genetics Commons, Natural Resources Management See next page for additional authors and Policy Commons, Veterinary Infectious Diseases Commons, and the Zoology Commons The ompc lete bibliographic information for this item can be found at http://lib.dr.iastate.edu/ nrem_pubs/84. For information on how to cite this item, please visit http://lib.dr.iastate.edu/ howtocite.html. This Article is brought to you for free and open access by the Natural Resource Ecology and Management at Iowa State University Digital Repository. It has been accepted for inclusion in Natural Resource Ecology and Management Publications by an authorized administrator of Iowa State University Digital Repository. For more information, please contact [email protected]. Genetic susceptibility to chronic wasting disease in free-ranging white- tailed deer: Complement component C1q and Prnp polymorphisms Abstract The eg netic basis of susceptibility to chronic wasting disease (CWD) in free-ranging cervids is of great interest. Association studies of disease susceptibility in free-ranging populations, however, face considerable challenges including: the need for large sample sizes when disease is rare, animals of unknown pedigree create a risk of spurious results due to population admixture, and the inability to control disease exposure or dose. -
Neutrophil Chemoattractant Receptors in Health and Disease: Double-Edged Swords
Cellular & Molecular Immunology www.nature.com/cmi REVIEW ARTICLE Neutrophil chemoattractant receptors in health and disease: double-edged swords Mieke Metzemaekers1, Mieke Gouwy1 and Paul Proost 1 Neutrophils are frontline cells of the innate immune system. These effector leukocytes are equipped with intriguing antimicrobial machinery and consequently display high cytotoxic potential. Accurate neutrophil recruitment is essential to combat microbes and to restore homeostasis, for inflammation modulation and resolution, wound healing and tissue repair. After fulfilling the appropriate effector functions, however, dampening neutrophil activation and infiltration is crucial to prevent damage to the host. In humans, chemoattractant molecules can be categorized into four biochemical families, i.e., chemotactic lipids, formyl peptides, complement anaphylatoxins and chemokines. They are critically involved in the tight regulation of neutrophil bone marrow storage and egress and in spatial and temporal neutrophil trafficking between organs. Chemoattractants function by activating dedicated heptahelical G protein-coupled receptors (GPCRs). In addition, emerging evidence suggests an important role for atypical chemoattractant receptors (ACKRs) that do not couple to G proteins in fine-tuning neutrophil migratory and functional responses. The expression levels of chemoattractant receptors are dependent on the level of neutrophil maturation and state of activation, with a pivotal modulatory role for the (inflammatory) environment. Here, we provide an overview -
An Anticomplement Agent That Homes to the Damaged Brain and Promotes Recovery After Traumatic Brain Injury in Mice
An anticomplement agent that homes to the damaged brain and promotes recovery after traumatic brain injury in mice Marieta M. Rusevaa,1,2, Valeria Ramagliab,1, B. Paul Morgana, and Claire L. Harrisa,3 aInstitute of Infection and Immunity, School of Medicine, Cardiff University, Cardiff CF14 4XN, United Kingdom; and bDepartment of Genome Analysis, Academic Medical Center, Amsterdam 1105 AZ, The Netherlands Edited by Douglas T. Fearon, Cornell University, Cambridge, United Kingdom, and approved September 29, 2015 (received for review July 15, 2015) Activation of complement is a key determinant of neuropathology to rapidly and specifically inhibit MAC at sites of complement and disability after traumatic brain injury (TBI), and inhibition is activation, and test its therapeutic potential in experimental TBI. neuroprotective. However, systemic complement is essential to The construct, termed CD59-2a-CRIg, comprises CD59a linked fight infections, a critical complication of TBI. We describe a to CRIg via the murine IgG2a hinge. CD59a prevents assembly targeted complement inhibitor, comprising complement receptor of MAC in cell membranes (16), whereas CRIg binds C3b/iC3b of the Ig superfamily (CRIg) fused with complement regulator CD59a, deposited at sites of complement activation (17). The IgG2a designed to inhibit membrane attack complex (MAC) assembly at hinge promotes dimerization to increase ligand avidity. CD59- sites of C3b/iC3b deposition. CRIg and CD59a were linked via the 2a-CRIg protected in the TBI model, demonstrating that site- IgG2a hinge, yielding CD59-2a-CRIg dimer with increased iC3b/C3b targeted anti-MAC therapeutics may be effective in prevention binding avidity and MAC inhibitory activity. CD59-2a-CRIg inhibited of secondary neuropathology and improve neurologic recovery MAC formation and prevented complement-mediated lysis in vitro. -
Complement Component 4 Genes Contribute Sex-Specific Vulnerability in Diverse Illnesses
bioRxiv preprint doi: https://doi.org/10.1101/761718; this version posted September 9, 2019. The copyright holder for this preprint (which was not certified by peer review) is the author/funder, who has granted bioRxiv a license to display the preprint in perpetuity. It is made available under aCC-BY-ND 4.0 International license. Complement component 4 genes contribute sex-specific vulnerability in diverse illnesses Nolan Kamitaki1,2, Aswin Sekar1,2, Robert E. Handsaker1,2, Heather de Rivera1,2, Katherine Tooley1,2, David L. Morris3, Kimberly E. Taylor4, Christopher W. Whelan1,2, Philip Tombleson3, Loes M. Olde Loohuis5,6, Schizophrenia Working Group of the Psychiatric Genomics Consortium7, Michael Boehnke8, Robert P. Kimberly9, Kenneth M. Kaufman10, John B. Harley10, Carl D. Langefeld11, Christine E. Seidman1,12,13, Michele T. Pato14, Carlos N. Pato14, Roel A. Ophoff5,6, Robert R. Graham15, Lindsey A. Criswell4, Timothy J. Vyse3, Steven A. McCarroll1,2 1 Department of Genetics, Harvard Medical School, Boston, Massachusetts 02115, USA 2 Stanley Center for Psychiatric Research, Broad Institute of MIT and Harvard, Cambridge, Massachusetts 02142, USA 3 Department of Medical and Molecular Genetics, King’s College London, London WC2R 2LS, UK 4 Rosalind Russell / Ephraim P Engleman Rheumatology Research Center, Division of Rheumatology, UCSF School of Medicine, San Francisco, California 94143, USA 5 Department of Human Genetics, David Geffen School of Medicine, University of California, Los Angeles, California 90095, USA 6 Center for Neurobehavioral Genetics, Semel Institute for Neuroscience and Human Behavior, University of California, Los Angeles, California 90095, USA 7 A full list of collaborators is in Supplementary Information. -
Supplementary Table 1: Adhesion Genes Data Set
Supplementary Table 1: Adhesion genes data set PROBE Entrez Gene ID Celera Gene ID Gene_Symbol Gene_Name 160832 1 hCG201364.3 A1BG alpha-1-B glycoprotein 223658 1 hCG201364.3 A1BG alpha-1-B glycoprotein 212988 102 hCG40040.3 ADAM10 ADAM metallopeptidase domain 10 133411 4185 hCG28232.2 ADAM11 ADAM metallopeptidase domain 11 110695 8038 hCG40937.4 ADAM12 ADAM metallopeptidase domain 12 (meltrin alpha) 195222 8038 hCG40937.4 ADAM12 ADAM metallopeptidase domain 12 (meltrin alpha) 165344 8751 hCG20021.3 ADAM15 ADAM metallopeptidase domain 15 (metargidin) 189065 6868 null ADAM17 ADAM metallopeptidase domain 17 (tumor necrosis factor, alpha, converting enzyme) 108119 8728 hCG15398.4 ADAM19 ADAM metallopeptidase domain 19 (meltrin beta) 117763 8748 hCG20675.3 ADAM20 ADAM metallopeptidase domain 20 126448 8747 hCG1785634.2 ADAM21 ADAM metallopeptidase domain 21 208981 8747 hCG1785634.2|hCG2042897 ADAM21 ADAM metallopeptidase domain 21 180903 53616 hCG17212.4 ADAM22 ADAM metallopeptidase domain 22 177272 8745 hCG1811623.1 ADAM23 ADAM metallopeptidase domain 23 102384 10863 hCG1818505.1 ADAM28 ADAM metallopeptidase domain 28 119968 11086 hCG1786734.2 ADAM29 ADAM metallopeptidase domain 29 205542 11085 hCG1997196.1 ADAM30 ADAM metallopeptidase domain 30 148417 80332 hCG39255.4 ADAM33 ADAM metallopeptidase domain 33 140492 8756 hCG1789002.2 ADAM7 ADAM metallopeptidase domain 7 122603 101 hCG1816947.1 ADAM8 ADAM metallopeptidase domain 8 183965 8754 hCG1996391 ADAM9 ADAM metallopeptidase domain 9 (meltrin gamma) 129974 27299 hCG15447.3 ADAMDEC1 ADAM-like, -
High-Throughput Proteomic Profiling of the Fish Liver Following Bacterial
Causey et al. BMC Genomics (2018) 19:719 https://doi.org/10.1186/s12864-018-5092-0 RESEARCH ARTICLE Open Access High-throughput proteomic profiling of the fish liver following bacterial infection Dwight R Causey1, Moritz A N Pohl1, David A Stead2, Samuel A M Martin1, Christopher J Secombes1 and Daniel J Macqueen1* Abstract Background: High-throughput proteomics was used to determine the role of the fish liver in defense responses to bacterial infection. This was done using a rainbow trout (Oncorhynchus mykiss) model following infection with Aeromonas salmonicida, the causative agent of furunculosis. The vertebrate liver has multifaceted functions in innate immunity, metabolism, and growth; we hypothesize this tissue serves a dual role in supporting host defense in parallel to metabolic adjustments that promote effectiveimmunefunction.Whilepaststudieshavereported mRNA responses to A. salmonicida in salmonids, the impact of bacterial infection on the liver proteome remains uncharacterized in fish. Results: Rainbow trout were injected with A. salmonicida or PBS (control) and liver extracted 48 h later for analysis on a hybrid quadrupole-Orbitrap mass spectrometer. A label-free method was used for protein abundance profiling, which revealed a strong innate immune response along with evidence to support parallel rewiring of metabolic and growth systems. 3076 proteins were initially identified against all proteins (n = 71,293 RefSeq proteins) annotated in a single high-quality rainbow trout reference genome, of which 2433 were maintained for analysis post-quality filtering. Among the 2433 proteins, 109 showed significant differential abundance following A. salmonicida challenge, including many upregulated complement system and acute phase response proteins, in addition to molecules with putative functions that may support metabolic re-adjustments. -
APC Anti-Human Cd11b (ICRF44) Catalog Number: 20-0118
TECHNICAL DATA SHEET APC Anti-Human CD11b (ICRF44) Catalog Number: 20-0118 PRODUCT INFORMATION Count Contents: APC Anti-Human CD11b (ICRF44) Isotype: Mouse IgG1, kappa 0 0 1 2 3 4 10 10 10 10 10 Human CD11b (ICRF44) APC Concentration: 5 uL (1 ug)/test Clone: ICRF44 Human peripheral blood monocytes were stained with 5 uL (1 ug) APC Anti-Human CD11b (20-0118) (solid line) or 1 ug APC Mouse Reactivity: Human IgG1 isotype control (dashed line). Formulation: 10 mM NaH2PO4, 150 mM NaCl, 0.09% NaN3, 0.1% gelatin, pH7.2 DESCRIPTION The ICRF44 antibody reacts with human CD11b, also known as integrin alpha M. This 165-170 kDa cell surface glycoprotein is part of a family of integrin receptors that mediate adhesion between cells (cell-cell) and components of the extracellular matrix, e.g. fibrinogen (cell-matrix). In addition, integrins are active signaling receptors which recruit leukocytes to inflammatory sites and promote cell activa- tion. Complete, functional integrin receptors consist of distinct combinations of integrin chains which are differentially expressed. Integrin alpha M (CD11b) assembles with Integrin beta-2 (CD18) into a receptor known as Macrophage Antigen-1 (Mac-1) or complement receptor type 3 (CR3). This receptor binds and induces intracellular signaling through ICAM-1, ICAM-2, ICAM-3 and ICAM-4 on endothelial cells and can also facilitate removal of iC3b bearing foreign cells.The ICRF44 antibody is widely used as a marker for CD11b expression on macrophages, granulocytes, and subsets of NK cells. It is reported to be cross-reactive with a number of non-human species including Baboon, Chimpanzee, Cynomolgus, Rhesus and Swine. -
CD Markers Are Routinely Used for the Immunophenotyping of Cells
ptglab.com 1 CD MARKER ANTIBODIES www.ptglab.com Introduction The cluster of differentiation (abbreviated as CD) is a protocol used for the identification and investigation of cell surface molecules. So-called CD markers are routinely used for the immunophenotyping of cells. Despite this use, they are not limited to roles in the immune system and perform a variety of roles in cell differentiation, adhesion, migration, blood clotting, gamete fertilization, amino acid transport and apoptosis, among many others. As such, Proteintech’s mini catalog featuring its antibodies targeting CD markers is applicable to a wide range of research disciplines. PRODUCT FOCUS PECAM1 Platelet endothelial cell adhesion of blood vessels – making up a large portion molecule-1 (PECAM1), also known as cluster of its intracellular junctions. PECAM-1 is also CD Number of differentiation 31 (CD31), is a member of present on the surface of hematopoietic the immunoglobulin gene superfamily of cell cells and immune cells including platelets, CD31 adhesion molecules. It is highly expressed monocytes, neutrophils, natural killer cells, on the surface of the endothelium – the thin megakaryocytes and some types of T-cell. Catalog Number layer of endothelial cells lining the interior 11256-1-AP Type Rabbit Polyclonal Applications ELISA, FC, IF, IHC, IP, WB 16 Publications Immunohistochemical of paraffin-embedded Figure 1: Immunofluorescence staining human hepatocirrhosis using PECAM1, CD31 of PECAM1 (11256-1-AP), Alexa 488 goat antibody (11265-1-AP) at a dilution of 1:50 anti-rabbit (green), and smooth muscle KD/KO Validated (40x objective). alpha-actin (red), courtesy of Nicola Smart. PECAM1: Customer Testimonial Nicola Smart, a cardiovascular researcher “As you can see [the immunostaining] is and a group leader at the University of extremely clean and specific [and] displays Oxford, has said of the PECAM1 antibody strong intercellular junction expression, (11265-1-AP) that it “worked beautifully as expected for a cell adhesion molecule.” on every occasion I’ve tried it.” Proteintech thanks Dr. -
In Vitro Selection for Adhesion of Plasmodium Falciparum-Infected Erythrocytes to ABO Antigens Does Not Affect Pfemp1 and RIFIN
www.nature.com/scientificreports OPEN In vitro selection for adhesion of Plasmodium falciparum‑infected erythrocytes to ABO antigens does not afect PfEMP1 and RIFIN expression William van der Puije1,2, Christian W. Wang 4, Srinidhi Sudharson 2, Casper Hempel 2, Rebecca W. Olsen 4, Nanna Dalgaard 4, Michael F. Ofori 1, Lars Hviid 3,4, Jørgen A. L. Kurtzhals 2,4 & Trine Staalsoe 2,4* Plasmodium falciparum causes the most severe form of malaria in humans. The adhesion of the infected erythrocytes (IEs) to endothelial receptors (sequestration) and to uninfected erythrocytes (rosetting) are considered major elements in the pathogenesis of the disease. Both sequestration and rosetting appear to involve particular members of several IE variant surface antigens (VSAs) as ligands, interacting with multiple vascular host receptors, including the ABO blood group antigens. In this study, we subjected genetically distinct P. falciparum parasites to in vitro selection for increased IE adhesion to ABO antigens in the absence of potentially confounding receptors. The selection resulted in IEs that adhered stronger to pure ABO antigens, to erythrocytes, and to various human cell lines than their unselected counterparts. However, selection did not result in marked qualitative changes in transcript levels of the genes encoding the best-described VSA families, PfEMP1 and RIFIN. Rather, overall transcription of both gene families tended to decline following selection. Furthermore, selection-induced increases in the adhesion to ABO occurred in the absence of marked changes in immune IgG recognition of IE surface antigens, generally assumed to target mainly VSAs. Our study sheds new light on our understanding of the processes and molecules involved in IE sequestration and rosetting. -
Supplement 1A Steffensen Et
Liver Wild-type Knockout C T C T 1 2 4 7 8 9 1 2 4 5 7 9 1 1 1 1 1 1 C C C T T T C C C T T T W W W W W W K K K K K K IMAGE:793166 RIKEN cDNA 6720463E02 gene IMAGE:1447421 ESTs, Weakly similar to ZF37 MOUSE ZINC FINGER PROTEIN 37 [M.musculus] IMAGE:934291 RIKEN cDNA 2810418N01 gene IMAGE:1247525 small EDRK-rich f2actor IMAGE:1449402 expressed sequence AW321064 IMAGE:1279847 ESTs IMAGE:518737 expressed sequence AW049941 IMAGE:860231 a disintegrin and metalloproteinase domain 17 IMAGE:642836 CD86 antigen IMAGE:1003885 phosphoribosyl pyrophosphate sy1nthetase IMAGE:524862 RIKEN cDNA 5730469D23 gene IMAGE:1264473 protein inhibitor of activat1ed STAT IMAGE:847035 RIKEN cDNA 4833422F06 gene IMAGE:374550 requiem IMAGE:976520 nuclear receptor coact4ivator IMAGE:1264311 Unknown IMAGE:976735 expressed sequence AI987692 IMAGE:976659 cathepsLin IMAGE:1477580 RIKEN cDNA 1600010J02 gene IMAGE:1277168 ribosomal protein, large, P1 IMAGE:524842 RIKEN cDNA 0710008D09 gene IMAGE:373019 split hand/foot delete1d gene IMAGE:404428 expressed sequence AI413851 IMAGE:619810 RIKEN cDNA 1700003F10 gene IMAGE:1749558 caspase 3, apoptosis related cysteine protease IMAGE:718718 RIKEN cDNA 2810003F23 gene IMAGE:819789 Unknown IMAGE:524474 ATP-binding cassette, sub-family A ABC1, member IMAGE:804950 Mus musculus, Similar to ribosomal protein S20, clone MGC:6876 IMAGE:2651405, mRNA, complete cds IMAGE:806143 gap junction membrane channel prot2ein beta IMAGE:1745887 expressed sequence AI836376 IMAGE:779426 RIKEN cDNA 5230400G24 gene IMAGE:1125615 Unknown IMAGE:535025 DNA