Control of Lung Defence by Mucins and Macrophages: Ancient Defence Mechanisms with Modern Functions
Total Page:16
File Type:pdf, Size:1020Kb
Load more
Recommended publications
-
Expression and Preliminary Functional Analysis of Siglec-F on Mouse Macrophages*
386 Feng et al. / J Zhejiang Univ-Sci B (Biomed & Biotechnol) 2012 13(5):386-394 Journal of Zhejiang University-SCIENCE B (Biomedicine & Biotechnology) ISSN 1673-1581 (Print); ISSN 1862-1783 (Online) www.zju.edu.cn/jzus; www.springerlink.com E-mail: [email protected] Expression and preliminary functional analysis of * Siglec-F on mouse macrophages Yin-he FENG, Hui MAO†‡ (Department of Respiratory Medicine, West China Hospital, Sichuan University, Chengdu 610041, China) †E-mail: [email protected] Received Aug. 4, 2011; Revision accepted Jan. 18, 2012; Crosschecked Mar. 30, 2012 Abstract: Sialic acid-binding immunoglobulin-like lectin (Siglec)-F is a mouse functional paralog of human Siglec-8 that induces apoptosis in human eosinophils, and therefore may be useful as the basis of treatments for a variety of disorders associated with eosinophil hyperactivity, such as asthma. The expression pattern and functions of this protein in various cell types remain to be elucidated. The aim of this study was to determine the expression of Siglec-F on mouse macrophages by immunocytochemical staining, and also to investigate the effects of Siglec-F engagement by a Siglec-F antibody on phagocytic activity of macrophages. The results showed that Siglec-F expression was detected on mouse alveolar macrophages, but not on peritoneal macrophages. Furthermore, Siglec-F engagement did not affect the phagocytic activity of alveolar macrophages in the resting state or in the activated state following stimulation by the proinflammatory mediator tumor necrosis factor alpha (TNF-α) or lipopolysaccharide (LPS). Siglec-F expression on alveolar macrophages may be a result of adaptation. -
Development of a Quantitative Assay for the Characterization of Human Collectin-11 (CL-11, CL-K1)
Development of a Quantitative Assay for the Characterization of Human Collectin-11 (CL-11, CL-K1) Bayarri-Olmos, Rafael; Kirketerp-Moller, Nikolaj; Pérez-Alós, Laura; Skjodt, Karsten; Skjoedt, Mikkel Ole; Garred, Peter Published in: Frontiers in Immunology DOI: 10.3389/fimmu.2018.02238 Publication date: 2018 Document version Publisher's PDF, also known as Version of record Document license: CC BY Citation for published version (APA): Bayarri-Olmos, R., Kirketerp-Moller, N., Pérez-Alós, L., Skjodt, K., Skjoedt, M. O., & Garred, P. (2018). Development of a Quantitative Assay for the Characterization of Human Collectin-11 (CL-11, CL-K1). Frontiers in Immunology, 9, [2238]. https://doi.org/10.3389/fimmu.2018.02238 Download date: 01. Oct. 2021 ORIGINAL RESEARCH published: 28 September 2018 doi: 10.3389/fimmu.2018.02238 Development of a Quantitative Assay for the Characterization of Human Collectin-11 (CL-11, CL-K1) Rafael Bayarri-Olmos 1*, Nikolaj Kirketerp-Moller 1, Laura Pérez-Alós 1, Karsten Skjodt 2, Mikkel-Ole Skjoedt 1 and Peter Garred 1 1 Laboratory of Molecular Medicine, Department of Clinical Immunology, Faculty of Health and Medical Sciences, Rigshospitalet, University of Copenhagen, Copenhagen, Denmark, 2 Department of Cancer and Inflammation Research, University of Southern Denmark, Odense, Denmark Collectin-11 (CL-11) is a pattern recognition molecule of the lectin pathway of complement with diverse functions spanning from host defense to embryonic development. CL-11 is found in the circulation in heterocomplexes with the homologous collectin-10 (CL-10). Abnormal CL-11 plasma levels are associated with the presence Edited by: of disseminated intravascular coagulation, urinary schistosomiasis, and congenital Maciej Cedzynski, disorders. -
Recognition of Microbial Glycans by Soluble Human Lectins
Available online at www.sciencedirect.com ScienceDirect Recognition of microbial glycans by soluble human lectins 3 1 1,2 Darryl A Wesener , Amanda Dugan and Laura L Kiessling Human innate immune lectins that recognize microbial glycans implicated in the regulation of microbial colonization and can conduct microbial surveillance and thereby help prevent in protection against infection. Seminal research on the infection. Structural analysis of soluble lectins has provided acute response to bacterial infection led to the identifica- invaluable insight into how these proteins recognize their tion of secreted factors that include C-reactive protein cognate carbohydrate ligands and how this recognition gives (CRP) and mannose-binding lectin (MBL) [1,3]. Both rise to biological function. In this opinion, we cover the CRP and MBL can recognize carbohydrate antigens on structural features of lectins that allow them to mediate the surface of pathogens, including Streptococcus pneumo- microbial recognition, highlighting examples from the collectin, niae and Staphylococcus aureus and then promote comple- Reg protein, galectin, pentraxin, ficolin and intelectin families. ment-mediated opsonization and cell killing [4]. Since These analyses reveal how some lectins (e.g., human intelectin- these initial observations, other lectins have been impli- 1) can recognize glycan epitopes that are remarkably diverse, cated in microbial recognition. Like MBL some of these yet still differentiate between mammalian and microbial proteins are C-type lectins, while others are members of glycans. We additionally discuss strategies to identify lectins the ficolin, pentraxin, galectin, or intelectin families. that recognize microbial glycans and highlight tools that Many of the lectins that function in microbial surveillance facilitate these discovery efforts. -
Review Sialic Acid-Specific Lectins: Occurrence, Specificity and Function
Cell. Mol. Life Sci. 63 (2006) 1331–1354 1420-682X/06/121331-24 DOI 10.1007/s00018-005-5589-y Cellular and Molecular Life Sciences © Birkhäuser Verlag, Basel, 2006 Review Sialic acid-specific lectins: occurrence, specificity and function F. Lehmanna, *, E. Tiralongob and J. Tiralongoa a Institute for Glycomics, Griffith University (Gold Coast Campus), PMB 50 Gold Coast Mail Centre Australia 9726 (Australia), Fax: +61 7 5552 8098; e-mail: [email protected] b School of Pharmacy, Griffith University (Gold Coast Campus), PMB 50 Gold Coast Mail Centre Australia 9726 (Australia) Received 13 December 2005; received after revision 9 February 2006; accepted 15 February 2006 Online First 5 April 2006 Abstract. Sialic acids consist of a family of acidic nine- through specific interactions with lectins, a family of carbon sugars that are typically located at the terminal po- proteins that recognise and bind sugars. This review will sitions of a variety of glycoconjugates. Naturally occur- present a detailed overview of our current knowledge re- ring sialic acids show an immense diversity of structure, garding the occurrence, specificity and function of sialic and this reflects their involvement in a variety of biologi- acid-specific lectins, particularly those that occur in vi- cally important processes. One such process involves the ruses, bacteria and non-vertebrate eukaryotes. direct participation of sialic acids in recognition events Keywords. Sialic acid, lectin, sialoglycoconjugate, sialic acid-specific lectin, adhesin, infectious disease, immunology. Introduction [1, 2]. The largest structural variations of naturally occurring Sia are at carbon 5, which can be substituted with either an Sialic acids (Sia) are a family of nine-carbon a-keto acids acetamido, hydroxyacetamido or hydroxyl moiety to form (Fig. -
Human Lectins, Their Carbohydrate Affinities and Where to Find Them
biomolecules Review Human Lectins, Their Carbohydrate Affinities and Where to Review HumanFind Them Lectins, Their Carbohydrate Affinities and Where to FindCláudia ThemD. Raposo 1,*, André B. Canelas 2 and M. Teresa Barros 1 1, 2 1 Cláudia D. Raposo * , Andr1 é LAQVB. Canelas‐Requimte,and Department M. Teresa of Chemistry, Barros NOVA School of Science and Technology, Universidade NOVA de Lisboa, 2829‐516 Caparica, Portugal; [email protected] 12 GlanbiaLAQV-Requimte,‐AgriChemWhey, Department Lisheen of Chemistry, Mine, Killoran, NOVA Moyne, School E41 of ScienceR622 Co. and Tipperary, Technology, Ireland; canelas‐ [email protected] NOVA de Lisboa, 2829-516 Caparica, Portugal; [email protected] 2* Correspondence:Glanbia-AgriChemWhey, [email protected]; Lisheen Mine, Tel.: Killoran, +351‐212948550 Moyne, E41 R622 Tipperary, Ireland; [email protected] * Correspondence: [email protected]; Tel.: +351-212948550 Abstract: Lectins are a class of proteins responsible for several biological roles such as cell‐cell in‐ Abstract:teractions,Lectins signaling are pathways, a class of and proteins several responsible innate immune for several responses biological against roles pathogens. such as Since cell-cell lec‐ interactions,tins are able signalingto bind to pathways, carbohydrates, and several they can innate be a immuneviable target responses for targeted against drug pathogens. delivery Since sys‐ lectinstems. In are fact, able several to bind lectins to carbohydrates, were approved they by canFood be and a viable Drug targetAdministration for targeted for drugthat purpose. delivery systems.Information In fact, about several specific lectins carbohydrate were approved recognition by Food by andlectin Drug receptors Administration was gathered for that herein, purpose. plus Informationthe specific organs about specific where those carbohydrate lectins can recognition be found by within lectin the receptors human was body. -
Myelin-Associated Glycoprotein Gene
CHAPTER 17 Myelin-Associated Glycoprotein Gene John Georgiou, Michael B. Tropak, and John C. Roder MAG INTRODUCTION Specialized glial cells, oligodendrocytes in the central nervous system (CNS), and Schwann cells in the peripheral nervous system (PNS) elaborate cytoplasmic wrappings known as myelin around axons. The myelination process requires a complex series of interactions between the glial cells and axons, which remain poorly understood. Myelin functions to insulate neurons and facilitates the rapid signal conduction required in organisms with complex nervous systems. Myelin-associated glycoprotein (MAG) is a relatively minor constituent of both CNS and PNS myelin that has been implicated in the formation and maintenance of myelin. However, it is also a cell recognition molecule involved in neuron- glial interactions, including regulation of axonal outgrowth and nerve regeneration. Discovery of Myelin-Associated Glycoprotein, MAG Prior to the discovery of MAG in 1973, the major proteins in compact myelin such as myelin basic protein (MBP) and proteolipid protein (PLP) were known. During the early 1970s it became clear that proteins on the surface which mediate adhesion are generally glycosylated. Consequently, Quarles and colleagues used radiolabeled fucose to identify MAG (Quarles et al., 1973), a myelin glycoprotein that might mediate adhesive inter- actions between glial and neuronal cells that are important for the formation of the myelin sheath. MAG was cloned in 1987 (Arquint et al., 1987), and DNA sequence analysis revealed that the MAG cDNA that was isolated was derived from the same mRNA as clone p1B236, a randomly selected, brain-speciWc, partial cDNA isolated previously in 1983 (SutcliVe et al., 1983). -
Siglec-15 As an Emerging Target for Next-Generation Cancer Immunotherapy 2 Jingwei Sun1,*, Qiao Lu2,3, Miguel F
Author Manuscript Published OnlineFirst on September 21, 2020; DOI: 10.1158/1078-0432.CCR-19-2925 Author manuscripts have been peer reviewed and accepted for publication but have not yet been edited. 1 Siglec-15 as an emerging target for next-generation cancer immunotherapy 2 Jingwei Sun1,*, Qiao Lu2,3, Miguel F. Sanmanmed4, Jun Wang2,3# 3 4 1Department of Immunobiology, Yale University School of Medicine, New Haven, CT, USA. 5 2Department of Pathology, New York University Grossman School of Medicine, New York, NY, USA. 6 3The Laura and Isaac Perlmutter Cancer Center, New York University Langone Health, New York, NY, 7 USA. 8 4Program of Immunology and Immunotherapy, CIMA, University of Navarra, Pamplona 31008, Spain. 9 10 *Current Address: Grit Biotechnology, Shanghai, China. 11 #Correspondence, Dr. Jun Wang, 550 First Avenue, Smilow Research Building 316, New York, NY 10016. 12 Tel: 212-263-1506, E-mail: [email protected]. 13 14 Running title: Siglec-15 in cancer immunotherapy 15 16 Funding support: This work was supported in part by the NCI Cancer Center Support Grant (CCSG) 17 P30CA016087-39 at NYU Perlmutter Cancer Center. 18 19 20 Abstract 21 Immunomodulatory agents blocking the PD-1/PD-L1 pathway have shown a new way to treat cancer. The 22 explanation underlying the success of these agents may be the selective expression of PD-L1 with 23 dominant immune-suppressive activities in the tumor microenvironment (TME), supporting a more 24 favorable tumor response-to-toxicity ratio. However, despite the big success of these drugs, most cancer 25 patients show primary or acquired resistance, calling for the identification of new immune modulators in 26 the TME. -
Scavenger Receptor Collectin Placenta 1 Is a Novel Receptor Involved in The
www.nature.com/scientificreports OPEN Scavenger receptor collectin placenta 1 is a novel receptor involved in the uptake of myelin Received: 20 June 2016 Accepted: 14 February 2017 by phagocytes Published: 20 March 2017 Jeroen F. J. Bogie1,*, Jo Mailleux1,*, Elien Wouters1, Winde Jorissen1, Elien Grajchen1, Jasmine Vanmol1, Kristiaan Wouters2,3, Niels Hellings1, Jack van Horssen4, Tim Vanmierlo1 & Jerome J. A. Hendriks1 Myelin-containing macrophages and microglia are the most abundant immune cells in active multiple sclerosis (MS) lesions. Our recent transcriptomic analysis demonstrated that collectin placenta 1 (CL-P1) is one of the most potently induced genes in macrophages after uptake of myelin. CL-P1 is a type II transmembrane protein with both a collagen-like and carbohydrate recognition domain, which plays a key role in host defense. In this study we sought to determine the dynamics of CL-P1 expression on myelin-containing phagocytes and define the role that it plays in MS lesion development. We show that myelin uptake increases the cell surface expression of CL-P1 by mouse and human macrophages, but not by primary mouse microglia in vitro. In active demyelinating MS lesions, CL-P1 immunoreactivity was localized to perivascular and parenchymal myelin-laden phagocytes. Finally, we demonstrate that CL-P1 is involved in myelin internalization as knockdown of CL-P1 markedly reduced myelin uptake. Collectively, our data indicate that CL-P1 is a novel receptor involved in myelin uptake by phagocytes and likely plays a role in MS lesion development. Multiple sclerosis (MS) is a chronic, inflammatory, neurodegenerative disease of the central nervous system (CNS). -
Collectins and Galectins in the Abomasum of Goats Susceptible and Resistant T to Gastrointestinal Nematode Infection ⁎ Bárbara M.P.S
Veterinary Parasitology: Regional Studies and Reports 12 (2018) 99–105 Contents lists available at ScienceDirect Veterinary Parasitology: Regional Studies and Reports journal homepage: www.elsevier.com/locate/vprsr Original article Collectins and galectins in the abomasum of goats susceptible and resistant T to gastrointestinal nematode infection ⁎ Bárbara M.P.S. Souzaa, , Sabrina M. Lamberta, Sandra M. Nishia, Gustavo F. Saldañab, Geraldo G.S. Oliveirac, Luis S. Vieirad, Claudio R. Madrugaa, Maria Angela O. Almeidaa a Laboratory of Cellular and Molecular Biology, School of Veterinary Medicine and Animal Science, Federal University of Bahia, Salvador, BA, Brazil b Institute for Research on Genetic Engineering and Molecular Biology (INGEBI-CONICET), Laboratory of Molecular Biology of Chagas Disease, Buenos Aires, Argentina c Laboratory of Cellular and Molecular Immunology, Research Center of Gonçalo Muniz, Fiocruz, BA, Brazil d National Research Center of Goats and Sheep, Embrapa, Sobral, CE, Brazil ARTICLE INFO ABSTRACT Keywords: Originally described in cattle, conglutinin belongs to the collectin family and is involved in innate immune Innate immunity defense. It is thought that conglutinin provides the first line of defense by maintaining a symbiotic relationship Lectins with the microbes in the rumen while inhibiting inflammatory reactions caused by antibodies leaking into the Helminth bloodstream. Due to the lack of information on the similar lectins and sequence detection in goats, we char- Ruminants acterized the goat conglutinin gene using RACE and evaluated the differences in its gene expression profile, as PCR well as in the gene expression profiles for surfactant protein A, galectins 14 and 11, interleukin 4 and interferon- gamma in goats. -
Mannan-Binding Lectin Directly Interacts with Toll-Like Receptor 4 and Suppresses Lipopolysaccharide-Induced Inflammatory Cytokine Secretion from THP-1 Cells
Cellular & Molecular Immunology (2011) 8, 265–275 ß 2011 CSI and USTC. All rights reserved 1672-7681/11 $32.00 www.nature.com/cmi RESEARCH ARTICLE Mannan-binding lectin directly interacts with Toll-like receptor 4 and suppresses lipopolysaccharide-induced inflammatory cytokine secretion from THP-1 cells Mingyong Wang1,2, Yue Chen1, Yani Zhang1, Liyun Zhang1, Xiao Lu1 and Zhengliang Chen1 Mannan-binding lectin (MBL) plays a key role in the lectin pathway of complement activation and can influence cytokine expression. Toll-like receptor 4 (TLR4) is expressed extensively and has been demonstrated to be involved in lipopolysaccharide (LPS)-induced signaling. We first sought to determine whether MBL exposure could modulate LPS-induced inflammatory cytokine secretion and nuclear factor-kB (NF-kB) activity by using the monocytoid cell line THP-1. We then investigated the possible mechanisms underlying any observed regulatory effect. Using ELISA and reverse transcriptase polymerase chain reaction (RT-PCR) analysis, we found that at both the protein and mRNA levels, treatment with MBL suppresses LPS-induced tumor-necrosis factor (TNF)-a and IL-12 production in THP-1 cells. An electrophoretic mobility shift assay and western blot analysis revealed that MBL treatment can inhibit LPS-induced NF-kB DNA binding and translocation in THP-1 cells. While the binding of MBL to THP-1 cells was evident at physiological calcium concentrations, this binding occurred optimally in response to supraphysiological calcium concentrations. This binding can be partly inhibited by treatment with either a soluble form of recombinant TLR4 extracellular domain or anti-TLR4 monoclonal antibody (HTA125). Activation of THP-1 cells by LPS treatment resulted in increased MBL binding. -
An Extracatalytic Function of CD45 in B Cells Is Mediated by CD22
An extracatalytic function of CD45 in B cells is PNAS PLUS mediated by CD22 Sarah Coughlina,b, Mark Noviskia, James L. Muellera, Ammarina Chuwonpada, William C. Raschkec, Arthur Weissa,b,1, and Julie Zikhermana,1 aDivision of Rheumatology, Rosalind Russell and Ephraim P. Engleman Arthritis Research Center, Department of Medicine, University of California, San Francisco, CA 94143; bHoward Hughes Medical Institute, University of California, San Francisco, CA 94143; and cVirogenics Inc., San Diego, CA 92121 Contributed by Arthur Weiss, October 12, 2015 (sent for review July 15, 2015; reviewed by Lars Nitschke and Shiv Pillai) The receptor-like tyrosine phosphatase CD45 regulates antigen segment that contains tandem protein tyrosine phosphatase do- receptor signaling by dephosphorylating the C-terminal inhibitory mains, the more membrane-distal of which is enzymatically inactive. tyrosine of the src family kinases. However, despite its abundance, Although CD45 is the most abundantly expressed protein on the the function of the large, alternatively spliced extracellular domain surface of nucleated hematopoietic cells, the function of its EC of CD45 has remained elusive. We used normally spliced CD45 trans- domain remains unknown. Alternative splicing of this domain gen- genes either incorporating a phosphatase-inactivating point mutation erates multiple CD45 isoforms whose expression is tightly regulated or lacking the cytoplasmic domain to uncouple the enzymatic and in a cell-type, activation, and developmental stage-specific manner noncatalytic functions of CD45 in lymphocytes. Although these trans- (6, 13). A genetic polymorphism that alters splicing, but not amino genes did not alter T-cell signaling or development irrespective of acid sequence, is associated with human autoimmune disease (14). -
Myelin-Associated Glycoprotein/Fc Chimera from Rat (M5063)
Myelin Associated Glycoprotein/Fc Chimera Rat, Recombinant Expressed in mouse NSO cells Product Number M 5063 Storage Temperature −20 °C Synonyms: MAG Although MAG may encounter haempoietic cells and lymphocytes under pathologic conditions, it would Product Description normally interact with neuronal cells. It has been Myelin Associated Glycoprotein (MAG)/Fc chimera shown that MAG promotes axonal growth from was prepared from a cDNA sequence encoding the neonatal dorsal root ganglion (DRG) neurons and extracellular domain of rat MAG1 that was fused by embryonic spinal neurons, but is a potent inhibitor of means of a polypeptide linker to the carboxyl-terminal axonal re-growth from adult DRG and postnatal Fc region of human IgG1. The chimeric protein was cerebellar neurons. MAG plays an important role in expressed in NSO mouse myeloma cells. Mature the interaction between axons and myelin. A soluble recombinant rat MAG/Fc chimera is a disulfide-linked form of MAG containing the extracellular domain is homodimer. Based on amino-terminal sequencing the released from myelin in large quantities and identified amino terminus is Gly20. Reduced rat MAG/Fc in normal human tissues and in tissues from patients chimera monomer has a calculated molecular mass of with neurological disorders. This soluble MAG may approximately 81 kDa. As a result of glycosylation, the contribute to the lack of neuronal regeneration after recombinant protein migrates as a 120 kDa protein in injury.3-6 SDS-PAGE. Reagent MAG is a type I transmembrane glycoprotein Recombinant mouse MAG/Fc chimera is lyophilized containing five Ig-like domains in its extracellular from a 0.2 µm-filtered solution in phosphate buffered domain.