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  1. Article ; Online: C1q/TNF-Related Protein 6 Is a Pattern Recognition Molecule That Recruits Collectin-11 from the Complement System to Ligands.

    Kirketerp-Møller, Nikolaj / Bayarri-Olmos, Rafael / Krogfelt, Karen Angeliki / Garred, Peter

    Journal of immunology (Baltimore, Md. : 1950)

    2020  Volume 204, Issue 6, Page(s) 1598–1606

    Abstract: C1q/TNF-related protein (CTRP) 6 is a member of the CTRP protein family associated with the regulation of cellular and endocrine processes. CTRP6 contains collagen and globular structures, resembling the pattern recognition molecules (PRMs) of the ... ...

    Abstract C1q/TNF-related protein (CTRP) 6 is a member of the CTRP protein family associated with the regulation of cellular and endocrine processes. CTRP6 contains collagen and globular structures, resembling the pattern recognition molecules (PRMs) of the classical and lectin complement pathways. We expressed human CTRP6 in Chinese hamster ovary cells and investigated the binding to different putative ligands (acetylated BSA [AcBSA], zymosan, mannan, and LPS from
    MeSH term(s) Animals ; Antigens, Bacterial/immunology ; Antigens, Bacterial/metabolism ; CHO Cells ; Collagen/genetics ; Collagen/isolation & purification ; Collagen/metabolism ; Collectins/metabolism ; Complement Activation ; Complement C4/metabolism ; Complement Pathway, Mannose-Binding Lectin/immunology ; Cricetulus ; Escherichia coli/immunology ; Escherichia coli/metabolism ; Ligands ; Mannose-Binding Protein-Associated Serine Proteases/metabolism ; Pseudomonas aeruginosa/immunology ; Pseudomonas aeruginosa/metabolism ; Recombinant Proteins/genetics ; Recombinant Proteins/isolation & purification ; Recombinant Proteins/metabolism
    Chemical Substances Antigens, Bacterial ; C1qTNF6 protein, human ; Colec11 protein, human ; Collectins ; Complement C4 ; Ligands ; Recombinant Proteins ; Collagen (9007-34-5) ; MASP2 protein, human (EC 3.4.21.-) ; Mannose-Binding Protein-Associated Serine Proteases (EC 3.4.21.-)
    Language English
    Publishing date 2020-02-10
    Publishing country United States
    Document type Journal Article
    ZDB-ID 3056-9
    ISSN 1550-6606 ; 0022-1767 ; 1048-3233 ; 1047-7381
    ISSN (online) 1550-6606
    ISSN 0022-1767 ; 1048-3233 ; 1047-7381
    DOI 10.4049/jimmunol.1901316
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Ud II Zs.37: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 2021: Bestellungen von Artikeln über das Online-Bestellformular
    ab Jg. 2022: Lesesaal (EG)
    Zs.MG 28: Show issues

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  2. Article: The ficolin response to LPS challenge in mice

    Jarlhelt, Ida / Garred, Peter / Genster, Ninette / Kirketerp-Møller, Nikolaj / Skjoedt, Mikkel-Ole

    Molecular immunology. 2019 Apr., v. 108

    2019  

    Abstract: The ficolins belong to an important family of pattern recognition molecules, which contributes to complement activation via the lectin pathway. How the ficolins respond to inflammatory stimuli remains only partly understood. In the present study, we ... ...

    Abstract The ficolins belong to an important family of pattern recognition molecules, which contributes to complement activation via the lectin pathway. How the ficolins respond to inflammatory stimuli remains only partly understood. In the present study, we investigated the ficolin A and ficolin B expression and protein distribution patterns in a mouse model of LPS-induced inflammation. The time- and tissue-specific expression of ficolin A and B was determined by real time PCR. Furthermore, ficolin protein levels in serum and bone marrow extracts from LPS challenged mice were determined by novel in-house developed sandwich ELISAs. Ficolin A was mainly expressed in liver and spleen. However, our data also suggested that ficolin A is expressed in bone marrow, which is the main site of ficolin B expression. The level of ficolin A and B expression was increased after stimulation with LPS in the investigated tissues. This was followed by a downregulation of expression, causing mRNA levels to return to baseline 24 h post LPS challenge. Protein levels appeared to follow the same pattern as the expression profiles, with an exception of ficolin B levels in serum, which kept increasing for 24 h. Ficolin A was likewise significantly increased in bronchoalveolar lavage fluid from mice infected with the fungi A. fumigatus, pointing towards a similar effect of the ficolins in non-sterile mouse models of inflammation. The results demonstrate that LPS-induced inflammation can induce a significant ficolin response, suggesting that the murine ficolins are acute phase reactants with increase in both mRNA expression and protein levels during systemic inflammation.
    Keywords acute phase proteins ; animal models ; blood serum ; bone marrow ; enzyme-linked immunosorbent assay ; fungi ; gene expression ; gene expression regulation ; inflammation ; lectins ; liver ; messenger RNA ; mice ; protein content ; quantitative polymerase chain reaction ; spleen
    Language English
    Dates of publication 2019-04
    Size p. 121-127.
    Publishing place Elsevier Ltd
    Document type Article
    ZDB-ID 424427-8
    ISSN 1872-9142 ; 0161-5890
    ISSN (online) 1872-9142
    ISSN 0161-5890
    DOI 10.1016/j.molimm.2019.02.013
    Database NAL-Catalogue (AGRICOLA)

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 166: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
    Jg. 1995 - 2021: Lesesall (1.OG)
    ab Jg. 2022: Lesesaal (EG)

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  3. Article ; Online: The ficolin response to LPS challenge in mice.

    Jarlhelt, Ida / Genster, Ninette / Kirketerp-Møller, Nikolaj / Skjoedt, Mikkel-Ole / Garred, Peter

    Molecular immunology

    2019  Volume 108, Page(s) 121–127

    Abstract: The ficolins belong to an important family of pattern recognition molecules, which contributes to complement activation via the lectin pathway. How the ficolins respond to inflammatory stimuli remains only partly understood. In the present study, we ... ...

    Abstract The ficolins belong to an important family of pattern recognition molecules, which contributes to complement activation via the lectin pathway. How the ficolins respond to inflammatory stimuli remains only partly understood. In the present study, we investigated the ficolin A and ficolin B expression and protein distribution patterns in a mouse model of LPS-induced inflammation. The time- and tissue-specific expression of ficolin A and B was determined by real time PCR. Furthermore, ficolin protein levels in serum and bone marrow extracts from LPS challenged mice were determined by novel in-house developed sandwich ELISAs. Ficolin A was mainly expressed in liver and spleen. However, our data also suggested that ficolin A is expressed in bone marrow, which is the main site of ficolin B expression. The level of ficolin A and B expression was increased after stimulation with LPS in the investigated tissues. This was followed by a downregulation of expression, causing mRNA levels to return to baseline 24 h post LPS challenge. Protein levels appeared to follow the same pattern as the expression profiles, with an exception of ficolin B levels in serum, which kept increasing for 24 h. Ficolin A was likewise significantly increased in bronchoalveolar lavage fluid from mice infected with the fungi A. fumigatus, pointing towards a similar effect of the ficolins in non-sterile mouse models of inflammation. The results demonstrate that LPS-induced inflammation can induce a significant ficolin response, suggesting that the murine ficolins are acute phase reactants with increase in both mRNA expression and protein levels during systemic inflammation.
    MeSH term(s) Animals ; Aspergillosis/immunology ; Aspergillosis/microbiology ; Aspergillus fumigatus/pathogenicity ; Biological Assay ; Bone Marrow/drug effects ; Bone Marrow/metabolism ; Bronchoalveolar Lavage Fluid ; Disease Models, Animal ; Lectins/blood ; Lectins/metabolism ; Lipopolysaccharides/pharmacology ; Mice ; Organ Specificity/drug effects ; Reproducibility of Results ; Ficolins
    Chemical Substances Lectins ; Lipopolysaccharides
    Language English
    Publishing date 2019-02-26
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 424427-8
    ISSN 1872-9142 ; 0161-5890
    ISSN (online) 1872-9142
    ISSN 0161-5890
    DOI 10.1016/j.molimm.2019.02.013
    Database MEDical Literature Analysis and Retrieval System OnLINE

    Full text online

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 166: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
    Jg. 1995 - 2021: Lesesall (1.OG)
    ab Jg. 2022: Lesesaal (EG)

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  4. Article ; Online: Chimeric Proteins Containing MAP-1 and Functional Domains of C4b-Binding Protein Reveal Strong Complement Inhibitory Capacities.

    Hertz, Cecilie E / Bayarri-Olmos, Rafael / Kirketerp-Møller, Nikolaj / van Putten, Sander / Pilely, Katrine / Skjoedt, Mikkel-Ole / Garred, Peter

    Frontiers in immunology

    2018  Volume 9, Page(s) 1945

    Abstract: The complement system is a tightly regulated network of proteins involved in defense against pathogens, inflammatory processes, and coordination of the innate and adaptive immune responses. Dysregulation of the complement cascade is associated with many ... ...

    Abstract The complement system is a tightly regulated network of proteins involved in defense against pathogens, inflammatory processes, and coordination of the innate and adaptive immune responses. Dysregulation of the complement cascade is associated with many inflammatory disorders. Thus, inhibition of the complement system has emerged as an option for treatment of a range of different inflammatory diseases. MAP-1 is a pattern recognition molecule (PRM)-associated inhibitor of the lectin pathway of the complement system, whereas C4b-binding protein (C4BP) regulates both the classical and lectin pathways. In this study we generated chimeric proteins consisting of MAP-1 and the first five domains of human C4BP (C4BP
    MeSH term(s) Adaptor Proteins, Signal Transducing/chemistry ; Adaptor Proteins, Signal Transducing/genetics ; Adaptor Proteins, Signal Transducing/immunology ; Animals ; Apoptosis Regulatory Proteins/chemistry ; Apoptosis Regulatory Proteins/genetics ; Apoptosis Regulatory Proteins/immunology ; CHO Cells ; Complement C4b-Binding Protein/chemistry ; Complement C4b-Binding Protein/genetics ; Complement C4b-Binding Protein/immunology ; Complement Pathway, Mannose-Binding Lectin/immunology ; Cricetulus ; Enzyme-Linked Immunosorbent Assay ; Humans ; Recombinant Fusion Proteins
    Chemical Substances Adaptor Proteins, Signal Transducing ; Apoptosis Regulatory Proteins ; Complement C4b-Binding Protein ; MOAP1 protein, human ; Recombinant Fusion Proteins
    Language English
    Publishing date 2018-08-28
    Publishing country Switzerland
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2606827-8
    ISSN 1664-3224 ; 1664-3224
    ISSN (online) 1664-3224
    ISSN 1664-3224
    DOI 10.3389/fimmu.2018.01945
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  5. Article ; Online: 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

    Frontiers in immunology

    2018  Volume 9, Page(s) 2238

    Abstract: 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 ( ... ...

    Abstract 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 of disseminated intravascular coagulation, urinary schistosomiasis, and congenital disorders. Although there has been a marked development in the characterization of CL-11 there is still a scarcity of clinical tools for its analysis. Thus, we generated monoclonal antibodies and developed a quantitative ELISA to measure CL-11 in the circulation. The antibodies were screened against recombinant CL-11 and validated by ELISA and immunoprecipitation of serum and plasma. The best candidates were pairwise compared to develop a quantitative ELISA. The assay was validated regarding its sensitivity, reproducibility, and dilution linearity, demonstrating a satisfactory variability over a working range of 0.29-18.75 ng/ml. The mean plasma concentration of CL-11 in healthy controls was determined to be 289.4 ng/ml (range 143.2-459.4 ng/ml), highly correlated to the levels of CL/10/11 complexes (
    MeSH term(s) Analysis of Variance ; Animals ; Antibodies, Monoclonal/immunology ; CHO Cells ; Chromatography, Gel ; Collectins/blood ; Collectins/chemistry ; Collectins/immunology ; Collectins/metabolism ; Complement C4/metabolism ; Cricetulus ; Enzyme-Linked Immunosorbent Assay/methods ; Freezing ; Humans ; Lectins/metabolism ; Mannose-Binding Protein-Associated Serine Proteases/metabolism ; Protein Binding ; Statistics, Nonparametric ; Systemic Inflammatory Response Syndrome/blood ; Zymosan/chemistry
    Chemical Substances Antibodies, Monoclonal ; Colec11 protein, human ; Collectins ; Complement C4 ; Lectins ; Zymosan (9010-72-4) ; MASP2 protein, human (EC 3.4.21.-) ; Mannose-Binding Protein-Associated Serine Proteases (EC 3.4.21.-)
    Language English
    Publishing date 2018-09-28
    Publishing country Switzerland
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Validation Study
    ZDB-ID 2606827-8
    ISSN 1664-3224 ; 1664-3224
    ISSN (online) 1664-3224
    ISSN 1664-3224
    DOI 10.3389/fimmu.2018.02238
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  6. Article ; Online: Adipokinetic hormones and their G protein-coupled receptors emerged in Lophotrochozoa.

    Li, Shizhong / Hauser, Frank / Skadborg, Signe K / Nielsen, Stine V / Kirketerp-Møller, Nikolaj / Grimmelikhuijzen, Cornelis J P

    Scientific reports

    2016  Volume 6, Page(s) 32789

    Abstract: Most multicellular animals belong to two evolutionary lineages, the Proto- and Deuterostomia, which diverged 640-760 million years (MYR) ago. Neuropeptide signaling is abundant in animals belonging to both lineages, but it is often unclear whether there ... ...

    Abstract Most multicellular animals belong to two evolutionary lineages, the Proto- and Deuterostomia, which diverged 640-760 million years (MYR) ago. Neuropeptide signaling is abundant in animals belonging to both lineages, but it is often unclear whether there exist evolutionary relationships between the neuropeptide systems used by proto- or deuterostomes. An exception, however, are members of the gonadotropin-releasing hormone (GnRH) receptor superfamily, which occur in both evolutionary lineages, where GnRHs are the ligands in Deuterostomia and GnRH-like peptides, adipokinetic hormone (AKH), corazonin, and AKH/corazonin-related peptide (ACP) are the ligands in Protostomia. AKH is a well-studied insect neuropeptide that mobilizes lipids and carbohydrates from the insect fat body during flight. In our present paper, we show that AKH is not only widespread in insects, but also in other Ecdysozoa and in Lophotrochozoa. Furthermore, we have cloned and deorphanized two G protein-coupled receptors (GPCRs) from the oyster Crassostrea gigas (Mollusca) that are activated by low nanomolar concentrations of oyster AKH (pQVSFSTNWGSamide). Our discovery of functional AKH receptors in molluscs is especially significant, because it traces the emergence of AKH signaling back to about 550 MYR ago and brings us closer to a more complete understanding of the evolutionary origins of the GnRH receptor superfamily.
    MeSH term(s) Adipokines/metabolism ; Animals ; Biological Evolution ; CHO Cells ; Cloning, Molecular ; Computational Biology ; Crassostrea/metabolism ; Cricetinae ; Cricetulus ; Drosophila melanogaster ; Gonadotropin-Releasing Hormone/metabolism ; Humans ; Insect Hormones/metabolism ; Insect Proteins/metabolism ; Insecta ; Invertebrates/metabolism ; Ligands ; Neuropeptides/metabolism ; Oligopeptides/metabolism ; Peptides/metabolism ; Phylogeny ; Pyrrolidonecarboxylic Acid/analogs & derivatives ; Pyrrolidonecarboxylic Acid/metabolism ; Receptors, G-Protein-Coupled/metabolism ; Signal Transduction
    Chemical Substances Adipokines ; Insect Hormones ; Insect Proteins ; Ligands ; Neuropeptides ; Oligopeptides ; Peptides ; Receptors, G-Protein-Coupled ; adipokinetic hormone ; corazonin protein, insect (122984-73-0) ; Gonadotropin-Releasing Hormone (33515-09-2) ; Pyrrolidonecarboxylic Acid (SZB83O1W42)
    Language English
    Publishing date 2016--15
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2615211-3
    ISSN 2045-2322 ; 2045-2322
    ISSN (online) 2045-2322
    ISSN 2045-2322
    DOI 10.1038/srep32789
    Database MEDical Literature Analysis and Retrieval System OnLINE

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