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  1. Article: Pentraxins: structure, function, and role in inflammation.

    Du Clos, Terry W

    ISRN inflammation

    2013  Volume 2013, Page(s) 379040

    Abstract: The pentraxins are an ancient family of proteins with a unique architecture found as far back in evolution as the Horseshoe crab. In humans the two members of this family are C-reactive protein and serum amyloid P. Pentraxins are defined by their ... ...

    Abstract The pentraxins are an ancient family of proteins with a unique architecture found as far back in evolution as the Horseshoe crab. In humans the two members of this family are C-reactive protein and serum amyloid P. Pentraxins are defined by their sequence homology, their pentameric structure and their calcium-dependent binding to their ligands. Pentraxins function as soluble pattern recognition molecules and one of the earliest and most important roles for these proteins is host defense primarily against pathogenic bacteria. They function as opsonins for pathogens through activation of the complement pathway and through binding to Fc gamma receptors. Pentraxins also recognize membrane phospholipids and nuclear components exposed on or released by damaged cells. CRP has a specific interaction with small nuclear ribonucleoproteins whereas SAP is a major recognition molecule for DNA, two nuclear autoantigens. Studies in autoimmune and inflammatory disease models suggest that pentraxins interact with macrophage Fc receptors to regulate the inflammatory response. Because CRP is a strong acute phase reactant it is widely used as a marker of inflammation and infection.
    Language English
    Publishing date 2013-09-14
    Publishing country United States
    Document type Journal Article ; Review
    ZDB-ID 2679170-5
    ISSN 2090-8695
    ISSN 2090-8695
    DOI 10.1155/2013/379040
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  2. Article ; Online: Pentraxins and Fc Receptor-Mediated Immune Responses.

    Lu, Jinghua / Mold, Carolyn / Du Clos, Terry W / Sun, Peter D

    Frontiers in immunology

    2018  Volume 9, Page(s) 2607

    Abstract: C-reactive protein (CRP) is a member of the pentraxin family of proteins. These proteins are highly conserved over the course of evolution being present as far back as 250 million years ago. Mammalian pentraxins are characterized by the presence of five ... ...

    Abstract C-reactive protein (CRP) is a member of the pentraxin family of proteins. These proteins are highly conserved over the course of evolution being present as far back as 250 million years ago. Mammalian pentraxins are characterized by the presence of five identical non-covalently linked subunits. Each subunit has a structurally conserved site for calcium-dependent ligand binding. The biological activities of the pentraxins established over many years include the ability to mediate opsonization for phagocytosis and complement activation. Pentraxins have an important role in protection from infection from pathogenic bacteria, and regulation of the inflammatory response. It was recognized early on that some of these functions are mediated by activation of the classical complement pathway through C1q. However, experimental evidence suggested that cellular receptors for pentraxins also play a role in phagocytosis. More recent experimental evidence indicates a direct link between pentraxins and Fc receptors. The Fc receptors were first identified as the major receptors for immunoglobulins. The avidity of the interaction between IgG complexes and Fc receptors is greatly enhanced when multivalent ligands interact with the IgG binding sites and activation of signaling pathways requires Fc receptor crosslinking. Human pentraxins bind and activate human and mouse IgG receptors, FcγRI and FcγRII, and the human IgA receptor, FcαRI. The affinities of the interactions between Fc receptors and pentraxins in solution and on cell surfaces are similar to antibody binding to low affinity Fc receptors. Crystallographic and mutagenesis studies have defined the structural features of these interactions and determined the stoichiometry of binding as one-to-one. Pentraxin aggregation or binding to multivalent ligands increases the avidity of binding and results in activation of these receptors for phagocytosis and cytokine synthesis. This review will discuss the structural and functional characteristics of pentraxin Fc receptor interactions and their implications for host defense and inflammation.
    MeSH term(s) Animals ; C-Reactive Protein/immunology ; Humans ; Immunoglobulin G/immunology ; Inflammation/immunology ; Phagocytosis/immunology ; Receptors, Fc/immunology ; Receptors, IgG/immunology
    Chemical Substances Immunoglobulin G ; Receptors, Fc ; Receptors, IgG ; C-Reactive Protein (9007-41-4)
    Language English
    Publishing date 2018-11-13
    Publishing country Switzerland
    Document type Journal Article ; Research Support, N.I.H., Intramural ; Research Support, Non-U.S. Gov't ; Review
    ZDB-ID 2606827-8
    ISSN 1664-3224 ; 1664-3224
    ISSN (online) 1664-3224
    ISSN 1664-3224
    DOI 10.3389/fimmu.2018.02607
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  3. Article ; Online: Pentraxins

    Terry W. Du Clos

    ISRN Inflammation, Vol

    Structure, Function, and Role in Inflammation

    2013  Volume 2013

    Keywords Pathology ; RB1-214 ; Medicine ; R ; DOAJ:Pathology ; DOAJ:Medicine (General) ; DOAJ:Health Sciences
    Language English
    Publishing date 2013-01-01T00:00:00Z
    Publisher Hindawi Publishing Corporation
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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  4. Article ; Online: C-reactive protein inhibits plasmacytoid dendritic cell interferon responses to autoantibody immune complexes.

    Mold, Carolyn / Clos, Terry W Du

    Arthritis and rheumatism

    2013  Volume 65, Issue 7, Page(s) 1891–1901

    Abstract: Objective: C-reactive protein (CRP) is a serum pattern recognition molecule that binds to apoptotic cells and nucleoprotein autoantigens and Fcγ receptors (FcγR). In systemic lupus erythematosus (SLE), immune complexes (ICs) containing nucleoprotein ... ...

    Abstract Objective: C-reactive protein (CRP) is a serum pattern recognition molecule that binds to apoptotic cells and nucleoprotein autoantigens and Fcγ receptors (FcγR). In systemic lupus erythematosus (SLE), immune complexes (ICs) containing nucleoprotein autoantigens activate plasmacytoid dendritic cells (PDCs) to produce type I interferon (IFN), which contributes to disease pathogenesis. Autoantibody ICs are taken up by PDCs through FcγR type IIa into endosomes, where the nucleic acid components activate Toll-like receptor 7 (TLR-7) or TLR-9. The objective of this study was to investigate the effect of CRP on PDC and monocyte responses to nucleoprotein autoantigens and ICs.
    Methods: Peripheral blood mononuclear cells (PBMCs), purified monocytes, and PDCs were isolated from healthy volunteers and stimulated with autoantibody ICs containing apoptotic cells, small nuclear RNPs (snRNPs), or DNA, or directly with TLR-7 and TLR-9 agonists. Supernatants were analyzed for IFNα and cytokine levels by enzyme-linked immunosorbent assay and multiplex assay. Small nuclear RNPs were fluorescence-labeled, and the effect of CRP on binding, uptake, and intracellular localization of autoantibody snRNP complexes was measured by flow cytometry and confocal microscopy.
    Results: CRP bound to autoantigen did not induce IFNα in PBMCs or PDCs, whereas complexes formed with autoantibody did. Significantly, CRP inhibited the IFNα response to both anti-U1 RNP-snRNP complexes and anti-DNA-DNA complexes, but not to other TLR-7 and TLR-9 agonists. CRP directly inhibited PDC IFNα release, promoted PDC differentiation, and increased late endosome localization of autoantigen in PDCs and monocytes.
    Conclusion: CRP is a regulator of the type I IFN response to SLE ICs. CRP increased the intracellular processing of ICs in late endosomes, which is associated with decreased synthesis of type I IFN after intracellular TLR activation.
    MeSH term(s) Antibodies, Antinuclear/immunology ; Antigen-Antibody Complex/immunology ; C-Reactive Protein/immunology ; Cytokines/immunology ; Dendritic Cells/immunology ; Humans ; Interferon Type I/immunology ; Interferon-alpha/immunology ; Leukocytes, Mononuclear ; Lupus Erythematosus, Systemic/immunology ; Toll-Like Receptor 7/agonists ; Toll-Like Receptor 7/immunology ; Toll-Like Receptor 9/agonists ; Toll-Like Receptor 9/immunology ; U937 Cells
    Chemical Substances Antibodies, Antinuclear ; Antigen-Antibody Complex ; Cytokines ; Interferon Type I ; Interferon-alpha ; TLR7 protein, human ; TLR9 protein, human ; Toll-Like Receptor 7 ; Toll-Like Receptor 9 ; C-Reactive Protein (9007-41-4)
    Language English
    Publishing date 2013-04-11
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, U.S. Gov't, Non-P.H.S.
    ZDB-ID 127294-9
    ISSN 1529-0131 ; 0004-3591 ; 2326-5191
    ISSN (online) 1529-0131
    ISSN 0004-3591 ; 2326-5191
    DOI 10.1002/art.37968
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  5. Article: C-reactive protein as a regulator of autoimmunity and inflammation.

    Du Clos, Terry W

    Arthritis and rheumatism

    2003  Volume 48, Issue 6, Page(s) 1475–1477

    MeSH term(s) Animals ; Autoimmunity/immunology ; Biomarkers/blood ; C-Reactive Protein/immunology ; C-Reactive Protein/metabolism ; Humans ; Inflammation/blood ; Inflammation/immunology ; Mice ; Models, Animal
    Chemical Substances Biomarkers ; C-Reactive Protein (9007-41-4)
    Language English
    Publishing date 2003-06
    Publishing country United States
    Document type Comment ; Editorial ; Review
    ZDB-ID 127294-9
    ISSN 1529-0131 ; 0004-3591 ; 2326-5191
    ISSN (online) 1529-0131
    ISSN 0004-3591 ; 2326-5191
    DOI 10.1002/art.11025
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  6. Article ; Online: Pentraxins (CRP, SAP) in the process of complement activation and clearance of apoptotic bodies through Fcγ receptors.

    Du Clos, Terry W / Mold, Carolyn

    Current opinion in organ transplantation

    2010  Volume 16, Issue 1, Page(s) 15–20

    Abstract: Purpose of review: Ischemia/reperfusion injury and organ allograft rejection both entail excessive cell and tissue destruction. A number of innate immune proteins, including the pentraxins, participate in the removal of this potentially inflammatory and ...

    Abstract Purpose of review: Ischemia/reperfusion injury and organ allograft rejection both entail excessive cell and tissue destruction. A number of innate immune proteins, including the pentraxins, participate in the removal of this potentially inflammatory and autoimmunogenic material. The classical pentraxins, C-reactive protein (CRP) and serum amyloid P component (SAP) are serum opsonins, which bind to damaged membranes and nuclear autoantigens. Understanding the role of pentraxins in inflammation has been advanced by the recent identification and structural analysis of their receptor interactions.
    Recent findings: The ligand-binding, complement-activating and opsonic properties of pentraxins have been known for some time. However, the establishment of Fcγ receptors as the primary receptors for pentraxins is a recent finding with important implications for CRP and SAP functions. The crystal structure of SAP in complex with FcγRIIa was recently solved, leading to new insights into function and new opportunities for pentraxin-based therapeutics. In addition, new approaches to inhibit CRP synthesis or binding are being developed based on clinical associations between CRP levels and cardiovascular disease.
    Summary: This review will summarize data on the function of pentraxins in clearance of injured tissue and cells and discuss the implications of this clearance pathway for autoimmunity and ischemia/reperfusion injury.
    MeSH term(s) Animals ; Apoptosis/immunology ; C-Reactive Protein/immunology ; C-Reactive Protein/metabolism ; Complement Activation/immunology ; Humans ; Ischemia/immunology ; Ischemia/pathology ; Models, Molecular ; Receptors, IgG/immunology ; Receptors, IgG/metabolism ; Reperfusion Injury/immunology ; Reperfusion Injury/pathology ; Serum Amyloid P-Component/immunology ; Serum Amyloid P-Component/metabolism
    Chemical Substances Receptors, IgG ; Serum Amyloid P-Component ; C-Reactive Protein (9007-41-4)
    Language English
    Publishing date 2010-09-01
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, U.S. Gov't, Non-P.H.S. ; Review
    ZDB-ID 1390429-2
    ISSN 1531-7013 ; 1087-2418
    ISSN (online) 1531-7013
    ISSN 1087-2418
    DOI 10.1097/MOT.0b013e32834253c7
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  7. Article ; Online: Pentraxins and IgA share a binding hot-spot on FcαRI.

    Lu, Jinghua / Marjon, Kristopher D / Mold, Carolyn / Marnell, Lorraine / Du Clos, Terry W / Sun, Peter

    Protein science : a publication of the Protein Society

    2014  Volume 23, Issue 4, Page(s) 378–386

    Abstract: The pentraxins, C-reactive protein (CRP), and serum amyloid P component (SAP) have previously been shown to function as innate opsonins through interactions with Fcγ receptors. The molecular details of these interactions were elucidated by the crystal ... ...

    Abstract The pentraxins, C-reactive protein (CRP), and serum amyloid P component (SAP) have previously been shown to function as innate opsonins through interactions with Fcγ receptors. The molecular details of these interactions were elucidated by the crystal structure of SAP in complex with FcγRIIA. More recently, pentraxins were shown to bind and activate FcαRI (CD89), the receptor for IgA. Here, we used mutations of the receptor based on a docking model to further examine pentraxin recognition by FcαRI. The solution binding of pentraxins to six FcαRI alanine cluster mutants revealed that mutations Y35A and R82A, on the C-and F-strands of the D1 domain, respectively, markedly reduced receptor binding to CRP and SAP. These residues are in the IgA-binding site of the receptor, and thus, significantly affected receptor binding to IgA. The shared pentraxin and IgA-binding site on FcαRI is further supported by the results of a solution binding competition assay. In addition to the IgA-binding site, pentraxins appear to interact with a broader region of the receptor as the mutation in the C'-strand (R48A/E49A) enhanced pentraxin binding. Unlike Fcγ receptors, the H129A/I130A and R178A mutations on the BC- and FG-loops of D2 domain, respectively, had little effect on FcαRI binding to the pentraxins. In conclusion, our data suggest that the pentraxins recognize a similar site on FcαRI as IgA.
    MeSH term(s) Antigens, CD/chemistry ; Antigens, CD/genetics ; Antigens, CD/metabolism ; Binding Sites ; C-Reactive Protein/chemistry ; Humans ; Immunoglobulin A/chemistry ; Mutation ; Neutrophils/metabolism ; Receptors, Fc/chemistry ; Receptors, Fc/genetics ; Receptors, Fc/metabolism ; Serum Amyloid P-Component/chemistry
    Chemical Substances Antigens, CD ; Fc(alpha) receptor ; Immunoglobulin A ; Receptors, Fc ; Serum Amyloid P-Component ; C-Reactive Protein (9007-41-4)
    Language English
    Publishing date 2014-01-28
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, N.I.H., Intramural ; Research Support, U.S. Gov't, Non-P.H.S.
    ZDB-ID 1106283-6
    ISSN 1469-896X ; 0961-8368
    ISSN (online) 1469-896X
    ISSN 0961-8368
    DOI 10.1002/pro.2419
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  8. Article ; Online: Transforming growth factor-β, macrophage colony-stimulating factor and C-reactive protein levels correlate with CD14(high)CD16+ monocyte induction and activation in trauma patients.

    West, Sonlee D / Goldberg, Daniel / Ziegler, Anna / Krencicki, Michael / Du Clos, Terry W / Mold, Carolyn

    PloS one

    2012  Volume 7, Issue 12, Page(s) e52406

    Abstract: Severe injury remains a leading cause of death and morbidity in patients under 40, with the number of annual trauma-related deaths approaching 160,000 in the United States. Patients who survive the initial trauma and post-traumatic resuscitation are at ... ...

    Abstract Severe injury remains a leading cause of death and morbidity in patients under 40, with the number of annual trauma-related deaths approaching 160,000 in the United States. Patients who survive the initial trauma and post-traumatic resuscitation are at risk for immune dysregulation, which contributes to late mortality and accounts for approximately 20% of deaths after traumatic injury. This post-traumatic immunosuppressed state has been attributed to over-expression of anti-inflammatory mediators in an effort to restore host homeostasis. We measured a panel of monocyte markers and cytokines in 50 severely injured trauma patients for 3 days following admission. We made the novel observation that the subpopulation of monocytes expressing high levels of CD14 and CD16 was expanded in the majority of patients. These cells also expressed CD163 consistent with differentiation into alternatively activated macrophages with potential regulatory or wound-healing activity. We examined factors in trauma plasma that may contribute to the generation and activation of these cells. The percentage of CD14(high)CD16(+) monocytes after trauma correlated strongly with plasma C-reactive protein (CRP) transforming growth factor-β (TGF-β), and macrophage colony-stimulating factor (M-CSF) levels. We demonstrate a role for TGF-β and M-CSF, but not CRP in generating these cells using monocytes from healthy volunteers incubated with plasma from trauma patients. CD16 is a receptor for CRP and IgG, and we showed that monocytes differentiated to the CD14(high)CD16(+) phenotype produced anti-inflammatory cytokines in response to acute phase concentrations of CRP. The role of these cells in immunosuppression following trauma is an area of ongoing investigation.
    MeSH term(s) Adolescent ; Adult ; Aged ; C-Reactive Protein/metabolism ; Case-Control Studies ; Female ; Flow Cytometry ; Heme Oxygenase-1/metabolism ; Humans ; Lipopolysaccharide Receptors/metabolism ; Macrophage Colony-Stimulating Factor/blood ; Macrophage Colony-Stimulating Factor/pharmacology ; Male ; Middle Aged ; Monocytes/drug effects ; Monocytes/metabolism ; Receptors, IgG/metabolism ; Statistics, Nonparametric ; Transforming Growth Factor beta/blood ; Treatment Outcome ; Wounds and Injuries/blood ; Wounds and Injuries/enzymology ; Wounds and Injuries/immunology ; Young Adult
    Chemical Substances Lipopolysaccharide Receptors ; Receptors, IgG ; Transforming Growth Factor beta ; Macrophage Colony-Stimulating Factor (81627-83-0) ; C-Reactive Protein (9007-41-4) ; Heme Oxygenase-1 (EC 1.14.14.18)
    Language English
    Publishing date 2012-12-28
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
    ISSN 1932-6203
    ISSN (online) 1932-6203
    DOI 10.1371/journal.pone.0052406
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  9. Article ; Online: Pentraxins and Fc receptors.

    Lu, Jinghua / Marjon, Kristopher D / Mold, Carolyn / Du Clos, Terry W / Sun, Peter D

    Immunological reviews

    2012  Volume 250, Issue 1, Page(s) 230–238

    Abstract: Pentraxins are innate pattern recognition molecules whose major function is to bind microbial pathogens or cellular debris during infection and inflammation and, by doing so, contribute to the clearance of necrotic cells as well as pathogens through ... ...

    Abstract Pentraxins are innate pattern recognition molecules whose major function is to bind microbial pathogens or cellular debris during infection and inflammation and, by doing so, contribute to the clearance of necrotic cells as well as pathogens through complement activations. Fc receptors are the cellular mediators of antibody functions. Although conceptually separated, both pentraxins and antibodies are important factors in controlling acute and chronic inflammation and infections. In recent years, increasing experimental evidence suggests a direct link between the innate pentraxins and humoral Fc receptors. Specifically, both human and mouse pentraxins recognize major forms of Fc receptors in solution and on cell surfaces with affinities similar to antibodies binding to their low affinity Fc receptors. Like immune complex, pentraxin aggregation and opsonization of pathogen result in Fc receptor and macrophage activation. The recently published crystal structure of human serum amyloid P (SAP) in complex with FcγRIIA further illustrated similarities to antibody recognition. These recent findings implicate a much broader role than complement activation for pentraxins in immunity. This review summarizes the structural and functional work that bridge the innate pentraxins and the adaptive Fc receptor functions. In many ways, pentraxins can be regarded as innate antibodies.
    MeSH term(s) Adaptive Immunity ; Animals ; Antibodies/chemistry ; Antibodies/immunology ; Antibodies/metabolism ; Antigens, Bacterial/chemistry ; Antigens, Bacterial/immunology ; Antigens, Bacterial/metabolism ; C-Reactive Protein/chemistry ; C-Reactive Protein/immunology ; C-Reactive Protein/metabolism ; Complement Activation ; Humans ; Immunity, Innate ; Inflammation/immunology ; Mice ; Models, Molecular ; Protein Binding ; Protein Structure, Tertiary ; Receptors, IgG/chemistry ; Receptors, IgG/immunology ; Receptors, IgG/metabolism ; Serum Amyloid P-Component/chemistry ; Serum Amyloid P-Component/immunology ; Serum Amyloid P-Component/metabolism
    Chemical Substances Antibodies ; Antigens, Bacterial ; Fc gamma receptor IIA ; Receptors, IgG ; Serum Amyloid P-Component ; C-Reactive Protein (9007-41-4)
    Language English
    Publishing date 2012-10-09
    Publishing country England
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, N.I.H., Intramural ; Review
    ZDB-ID 391796-4
    ISSN 1600-065X ; 0105-2896
    ISSN (online) 1600-065X
    ISSN 0105-2896
    DOI 10.1111/j.1600-065X.2012.01162.x
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  10. Article ; Online: C-reactive protein at the interface between innate immunity and inflammation.

    Peisajovich, Andres / Marnell, Lorraine / Mold, Carolyn / Du Clos, Terry W

    Expert review of clinical immunology

    2008  Volume 4, Issue 3, Page(s) 379–390

    Abstract: C-reactive protein (CRP), the prototypic acute-phase protein, increases rapidly in response to infection and inflammation. Although CRP was thought to be a passive, nonspecific marker of inflammation, recent studies indicate that CRP plays a key role in ... ...

    Abstract C-reactive protein (CRP), the prototypic acute-phase protein, increases rapidly in response to infection and inflammation. Although CRP was thought to be a passive, nonspecific marker of inflammation, recent studies indicate that CRP plays a key role in the innate immune system by recognizing pathogens and altered self determinants. Activation of complement and interaction with Fcgamma receptors by CRP provides a link between the innate and adaptive immune systems. Recent evidence suggests that CRP is a marker of atherosclerotic disease and may play a role in its induction. However, CRP has an anti-inflammatory role in autoimmune diseases, such as systemic lupus erythematosus. In this article, we review the biological mechanisms by which CRP exerts its effects on the immune system and discuss its role in infection, cardiovascular disease, malignancy and systemic lupus erythematosus.
    Language English
    Publishing date 2008-05
    Publishing country England
    Document type Journal Article
    ZDB-ID 2274260-8
    ISSN 1744-8409 ; 1744-666X
    ISSN (online) 1744-8409
    ISSN 1744-666X
    DOI 10.1586/1744666X.4.3.379
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