The Experts below are selected from a list of 1611 Experts worldwide ranked by ideXlab platform

Soren Hansen - One of the best experts on this subject based on the ideXlab platform.

  • the Collectins cl l1 cl k1 and cl p1 and their roles in complement and innate immunity
    Immunobiology, 2016
    Co-Authors: Soren Hansen, Katsuki Ohtani, Nobutaka Wakamiya
    Abstract:

    Both the complement system and Collectins play important roles in our innate immune system. The Collectins, which are characterized by their inclusion of a collagen-like region and a calcium-dependent carbohydrate recognition domain, are pattern recognition molecules and include the well characterized proteins mannan-binding lectin (MBL) and the surfactant proteins SP-A/-D. Collectin liver 1 (CL-L1), Collectin kidney 1 (CL-K1) and Collectin placenta 1 (CL-P1) are the most recently discovered Collectins. Although their function is still under investigation, accumulating information suggests that CL-L1, CL-K1 and CL-P1 play important roles in host defense by recognizing a variety of microorganisms and interacting with effector proteins, including complement components. The recent establishment of the existence of CL-K1 in the circulation in form of heteromeric complexes with CL-L1 (known as CL-LK) and its activation of the lectin pathway via MASPs, drew new attention in the complement biology, which was further strengthened by the observed interactions between CL-P1 and CRP-C1q-factor H or properdin. Deficiency of either CL-K1 or MASP-3 has been demonstrated in 3MC syndrome patients with developmental abnormalities, showing that lectin pathway components, regulation and/or activation are essential during the embryonic development; another feature that they most likely share CL-P1. Herein, we discuss the recent characteristics and roles of the Collectins CL-L1, CL-K1 and CL-P1 in the complement system, in innate immunity and their possible association with disease development and pathogenesis.

  • the genes encoding bovine sp a sp d mbl a conglutinin cl 43 and cl 46 form a distinct Collectin locus on bos taurus chromosome 28 bta28 at position q 1 8 1 9
    Animal Genetics, 2004
    Co-Authors: Morten F Gjerstorff, Soren Hansen, B Jensen, B Dueholm, P Horn, Christian Bendixen, Uffe Holmskov
    Abstract:

    Summary Collectins are a group of C-type lectins involved in the innate immune system, where they mediate and modulate clearance of pathogens. The health status of cattle is of major economical and ethical concern; therefore, the study of bovine Collectins is of importance. The Collectins conglutinin, CL-43 and CL-46 are only present in Bovidae and the characterization of their genes indicates that they are structural descendants of another Collectin, lung surfactant protein D (SP-D). In this study, we assembled BAC clones into a contig spanning 330–1150 kb, which includes the bovine genes encoding the Collectins SP-A (SFTPA), SP-D (SFTPD), mannan-binding lectin A (MBL1), CL-43 (COLEC9), CL-46 (COLEC13) and conglutinin (COLEC8). In the same contig, we also identified a gene that potentially encodes a novel conglutinin-like Collectin (COLEC14). The arrangement of STFPA, SFTPD and MBL1 is homologous to the organization found in humans and mice, whereas the Bovidae-specific Collectin genes, COLEC8, COLEC9 and COLEC13, extend from SFTPD. Proximal to the Collectin locus at BTA28q1.8–1.9, and included in the contig, we found the microsatellite IDVGA8, which may be a valuable marker for tracking polymorphisms in the linked Collectin genes.

Nobutaka Wakamiya - One of the best experts on this subject based on the ideXlab platform.

  • the Collectins cl l1 cl k1 and cl p1 and their roles in complement and innate immunity
    Immunobiology, 2016
    Co-Authors: Soren Hansen, Katsuki Ohtani, Nobutaka Wakamiya
    Abstract:

    Both the complement system and Collectins play important roles in our innate immune system. The Collectins, which are characterized by their inclusion of a collagen-like region and a calcium-dependent carbohydrate recognition domain, are pattern recognition molecules and include the well characterized proteins mannan-binding lectin (MBL) and the surfactant proteins SP-A/-D. Collectin liver 1 (CL-L1), Collectin kidney 1 (CL-K1) and Collectin placenta 1 (CL-P1) are the most recently discovered Collectins. Although their function is still under investigation, accumulating information suggests that CL-L1, CL-K1 and CL-P1 play important roles in host defense by recognizing a variety of microorganisms and interacting with effector proteins, including complement components. The recent establishment of the existence of CL-K1 in the circulation in form of heteromeric complexes with CL-L1 (known as CL-LK) and its activation of the lectin pathway via MASPs, drew new attention in the complement biology, which was further strengthened by the observed interactions between CL-P1 and CRP-C1q-factor H or properdin. Deficiency of either CL-K1 or MASP-3 has been demonstrated in 3MC syndrome patients with developmental abnormalities, showing that lectin pathway components, regulation and/or activation are essential during the embryonic development; another feature that they most likely share CL-P1. Herein, we discuss the recent characteristics and roles of the Collectins CL-L1, CL-K1 and CL-P1 in the complement system, in innate immunity and their possible association with disease development and pathogenesis.

  • biological functions of the novel Collectins cl l1 cl k1 and cl p1
    BioMed Research International, 2012
    Co-Authors: Katsuki Ohtani, Yasuhiko Suzuki, Nobutaka Wakamiya
    Abstract:

    Collectins are characterized by a collagen-like sequence and a carbohydrate recognition domain and are members of the vertebrate C-type lectin superfamily. Recently, “novel Collectins”, different from “classical Collectins” consisting of mannan-binding lectin (MBL) and surfactant proteins A and D (SP-A and SP-D), have been found by reverse genetics. These “novel Collectins” consist of Collectin liver 1 (CL-L1), Collectin kidney 1 (CL-K1), and Collectin placenta 1 (CL-P1) and are encoded by three separate genes. Experimental findings on human and animal Collectins have shown that both novel Collectins and classical Collectins play an important role in innate immunity. Based on our recent results and those of others, in this paper, we summarize the new biological functions of these novel Collectins in embryonic morphogenesis and development.

Uffe Holmskov - One of the best experts on this subject based on the ideXlab platform.

  • Collectins Collectin receptors and the lectin pathway of complement activation
    Clinical and Experimental Immunology, 2008
    Co-Authors: Rajneesh Malhotra, Jinhua Lu, Uffe Holmskov
    Abstract:

    The Collectins are a group of soluble multimeric lectins, which contain collagenous segments, and resemble the complement protein C1q in aspects of their structures and functions. This group of proteins, which includes MBP, SP-A, SP-D, conglutinin and CL-43, are known to act as opsonins in various circumstances, and are likely to have roles in innate immunity. The focus of current research is to pursue the hypothesis that the Collectins recognize and bind to non-host carbohydrate structures on microorganisms and particles, and participate in the processing or elimination of such material, either by direct interaction with phagocytic cell receptors, or by indirect routes such as complement activation .

  • the genes encoding bovine sp a sp d mbl a conglutinin cl 43 and cl 46 form a distinct Collectin locus on bos taurus chromosome 28 bta28 at position q 1 8 1 9
    Animal Genetics, 2004
    Co-Authors: Morten F Gjerstorff, Soren Hansen, B Jensen, B Dueholm, P Horn, Christian Bendixen, Uffe Holmskov
    Abstract:

    Summary Collectins are a group of C-type lectins involved in the innate immune system, where they mediate and modulate clearance of pathogens. The health status of cattle is of major economical and ethical concern; therefore, the study of bovine Collectins is of importance. The Collectins conglutinin, CL-43 and CL-46 are only present in Bovidae and the characterization of their genes indicates that they are structural descendants of another Collectin, lung surfactant protein D (SP-D). In this study, we assembled BAC clones into a contig spanning 330–1150 kb, which includes the bovine genes encoding the Collectins SP-A (SFTPA), SP-D (SFTPD), mannan-binding lectin A (MBL1), CL-43 (COLEC9), CL-46 (COLEC13) and conglutinin (COLEC8). In the same contig, we also identified a gene that potentially encodes a novel conglutinin-like Collectin (COLEC14). The arrangement of STFPA, SFTPD and MBL1 is homologous to the organization found in humans and mice, whereas the Bovidae-specific Collectin genes, COLEC8, COLEC9 and COLEC13, extend from SFTPD. Proximal to the Collectin locus at BTA28q1.8–1.9, and included in the contig, we found the microsatellite IDVGA8, which may be a valuable marker for tracking polymorphisms in the linked Collectin genes.

  • Antiviral activity of bovine Collectins against rotaviruses
    2004
    Co-Authors: Patrick C. Reading, Uffe Holmskov, Margot E. Anders
    Abstract:

    The antiviral activity against rotaviruses of three bovine Collectins, conglutinin, Collectin-43 (CL-43) and bovine SP-D, was examined. As shown by ELISA and Western blot, all three Collectins bound to the Nebraska calf diarrhoea virus bovine strain of rotavirus, and specifically to the VP7 glycoprotein. Inhibition by mannose or EDTA confirmed that binding was mediated through the lectin domains of the Collectins. Binding resulted in haemagglutin-ation inhibition and neutralization of rotavirus in-fectivity, CL-43 displaying the highest activity in both types of assay. In contrast, conglutinin was the most potent of the three Collectins against influenz

Rajneesh Malhotra - One of the best experts on this subject based on the ideXlab platform.

  • Collectins Collectin receptors and the lectin pathway of complement activation
    Clinical and Experimental Immunology, 2008
    Co-Authors: Rajneesh Malhotra, Jinhua Lu, Uffe Holmskov
    Abstract:

    The Collectins are a group of soluble multimeric lectins, which contain collagenous segments, and resemble the complement protein C1q in aspects of their structures and functions. This group of proteins, which includes MBP, SP-A, SP-D, conglutinin and CL-43, are known to act as opsonins in various circumstances, and are likely to have roles in innate immunity. The focus of current research is to pursue the hypothesis that the Collectins recognize and bind to non-host carbohydrate structures on microorganisms and particles, and participate in the processing or elimination of such material, either by direct interaction with phagocytic cell receptors, or by indirect routes such as complement activation .

  • Collectins and their role in lung immunity
    Journal of Leukocyte Biology, 2004
    Co-Authors: Timothy P Hickling, Rajneesh Malhotra, Howard Clark
    Abstract:

    The Collectins are a small family of secreted glycoproteins that contain C-type lectin domains and collagenous regions. They have an important function in innate immunity, recognizing and binding to microorganisms via sugar arrays on the microbial surface. Their function is to enhance adhesion and phagocytosis of microorganisms by agglutination and opsonization. In the lung, two members of the Collectin family, surfactant proteins A and D, are major protein constituents of surfactant. Another Collectin, mannan-binding lectin, is also present in the upper airways and buccal cavity and may protect against respiratory infections. Recent work has shown that Collectins have roles in resistance to allergy and in the control of apoptosis and clearance of apoptotic macrophage in the lung.

  • interaction of c1q and the Collectins with the potential receptors calreticulin cclqr Collectin receptor and megalin
    Immunobiology, 1998
    Co-Authors: Søren Kragh Moestrup, G.r. Stuart, Nicholas J. Lynch, Jinhua Lu, Wilhelm J Schwaeble, Rajneesh Malhotra
    Abstract:

    Abstract Several proteins have been identified as candidate cell-surface receptors for the complement protein C1q. Some of these also interact with the structurally-related Collectin proteins. Previous descriptions of C1q-binding properties of cells, and information on the cellular distribution of candidate receptors suggest that there is more than one physiologically relevant receptor for C 1 q. Two such candidate receptors, cell-surface calreticulin (also referred to as cC1qR or Collectin receptor) and megalin are discussed in this review.

Katsuki Ohtani - One of the best experts on this subject based on the ideXlab platform.

  • the Collectins cl l1 cl k1 and cl p1 and their roles in complement and innate immunity
    Immunobiology, 2016
    Co-Authors: Soren Hansen, Katsuki Ohtani, Nobutaka Wakamiya
    Abstract:

    Both the complement system and Collectins play important roles in our innate immune system. The Collectins, which are characterized by their inclusion of a collagen-like region and a calcium-dependent carbohydrate recognition domain, are pattern recognition molecules and include the well characterized proteins mannan-binding lectin (MBL) and the surfactant proteins SP-A/-D. Collectin liver 1 (CL-L1), Collectin kidney 1 (CL-K1) and Collectin placenta 1 (CL-P1) are the most recently discovered Collectins. Although their function is still under investigation, accumulating information suggests that CL-L1, CL-K1 and CL-P1 play important roles in host defense by recognizing a variety of microorganisms and interacting with effector proteins, including complement components. The recent establishment of the existence of CL-K1 in the circulation in form of heteromeric complexes with CL-L1 (known as CL-LK) and its activation of the lectin pathway via MASPs, drew new attention in the complement biology, which was further strengthened by the observed interactions between CL-P1 and CRP-C1q-factor H or properdin. Deficiency of either CL-K1 or MASP-3 has been demonstrated in 3MC syndrome patients with developmental abnormalities, showing that lectin pathway components, regulation and/or activation are essential during the embryonic development; another feature that they most likely share CL-P1. Herein, we discuss the recent characteristics and roles of the Collectins CL-L1, CL-K1 and CL-P1 in the complement system, in innate immunity and their possible association with disease development and pathogenesis.

  • biological functions of the novel Collectins cl l1 cl k1 and cl p1
    BioMed Research International, 2012
    Co-Authors: Katsuki Ohtani, Yasuhiko Suzuki, Nobutaka Wakamiya
    Abstract:

    Collectins are characterized by a collagen-like sequence and a carbohydrate recognition domain and are members of the vertebrate C-type lectin superfamily. Recently, “novel Collectins”, different from “classical Collectins” consisting of mannan-binding lectin (MBL) and surfactant proteins A and D (SP-A and SP-D), have been found by reverse genetics. These “novel Collectins” consist of Collectin liver 1 (CL-L1), Collectin kidney 1 (CL-K1), and Collectin placenta 1 (CL-P1) and are encoded by three separate genes. Experimental findings on human and animal Collectins have shown that both novel Collectins and classical Collectins play an important role in innate immunity. Based on our recent results and those of others, in this paper, we summarize the new biological functions of these novel Collectins in embryonic morphogenesis and development.