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  1. Article: Collectins: players of the innate immune system.

    van de Wetering, J Koenraad / van Golde, Lambert M G / Batenburg, Joseph J

    European journal of biochemistry

    2004  Volume 271, Issue 7, Page(s) 1229–1249

    Abstract: Collectins are a family of collagenous calcium-dependent defense lectins in animals. Their polypeptide chains consist of four regions: a cysteine-rich N-terminal domain, a collagen-like region, an alpha-helical coiled-coil neck domain and a C-terminal ... ...

    Abstract Collectins are a family of collagenous calcium-dependent defense lectins in animals. Their polypeptide chains consist of four regions: a cysteine-rich N-terminal domain, a collagen-like region, an alpha-helical coiled-coil neck domain and a C-terminal lectin or carbohydrate-recognition domain. These polypeptide chains form trimers that may assemble into larger oligomers. The best studied family members are the mannan-binding lectin, which is secreted into the blood by the liver, and the surfactant proteins A and D, which are secreted into the pulmonary alveolar and airway lining fluid. The collectins represent an important group of pattern recognition molecules, which bind to oligosaccharide structures and/or lipid moities on the surface of microorganisms. They bind preferentially to monosaccharide units of the mannose type, which present two vicinal hydroxyl groups in an equatorial position. High-affinity interactions between collectins and microorganisms depend, on the one hand, on the high density of the carbohydrate ligands on the microbial surface, and on the other, on the degree of oligomerization of the collectin. Apart from binding to microorganisms, the collectins can interact with receptors on host cells. Binding of collectins to microorganisms may facilitate microbial clearance through aggregation, complement activation, opsonization and activation of phagocytosis, and inhibition of microbial growth. In addition, the collectins can modulate inflammatory and allergic responses, affect apoptotic cell clearance and modulate the adaptive immune system.
    MeSH term(s) Animals ; Bacterial Proteins/chemistry ; Carbohydrates/chemistry ; Collectins/chemistry ; Collectins/physiology ; Epitopes/chemistry ; Fungal Proteins/chemistry ; Humans ; Immune System/physiology ; Inflammation ; Lipids/chemistry ; Models, Biological ; Monosaccharides/chemistry ; Polysaccharides/chemistry ; Protein Binding ; Protein Structure, Tertiary ; Viral Proteins/chemistry
    Chemical Substances Bacterial Proteins ; Carbohydrates ; Collectins ; Epitopes ; Fungal Proteins ; Lipids ; Monosaccharides ; Polysaccharides ; Viral Proteins
    Language English
    Publishing date 2004-04
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Review
    ZDB-ID 3032-6
    ISSN 1432-1033 ; 0014-2956
    ISSN (online) 1432-1033
    ISSN 0014-2956
    DOI 10.1111/j.1432-1033.2004.04040.x
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 260: 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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  2. Article: Surfactant protein D binding to terminal alpha1-3-linked fucose residues and to Schistosoma mansoni.

    van de Wetering, J Koenraad / van Remoortere, Alexandra / Vaandrager, Arie B / Batenburg, Joseph J / van Golde, Lambert M G / Hokke, Cornelis H / van Hellemond, Jaap J

    American journal of respiratory cell and molecular biology

    2004  Volume 31, Issue 5, Page(s) 565–572

    Abstract: Pulmonary surfactant protein (SP)-D is an important component of the innate immune system of the lung, which is thought to function by binding to specific carbohydrates on the surface of viruses and unicellular pathogens. SP-D has been shown to have a ... ...

    Abstract Pulmonary surfactant protein (SP)-D is an important component of the innate immune system of the lung, which is thought to function by binding to specific carbohydrates on the surface of viruses and unicellular pathogens. SP-D has been shown to have a relatively high affinity for the monosaccharides mannose, glucose, and fucose. However, there is limited information on SP-D binding to complex carbohydrate structures, and binding of SP-D to fucose in the context of an oligosaccharide has not yet been investigated. In this study, we used surface plasmon resonance spectroscopy to examine the potential of SP-D to bind to various synthetic fucosylated oligosaccharides, and identified Fucalpha1-3GalNAc and Fucalpha1-3GlcNAc elements as strong ligands. These types of fucosylated glycoconjugates are presented at the surface of Schistosoma mansoni, a parasitic worm that, during development, transiently resides in the lung. In line with the findings by surface plasmon resonance, we found that SP-D can bind to larval stages of S. mansoni, demonstrating for the first time that SP-D interacts with multicellular lung pathogens.
    MeSH term(s) Animals ; Carbohydrates/chemistry ; Concanavalin A/chemistry ; Electrophoresis, Polyacrylamide Gel ; Fucose/chemistry ; Glycoproteins/chemistry ; Humans ; Leukocytes/metabolism ; Ligands ; Lung/cytology ; Microscopy, Confocal ; Models, Chemical ; Protein Binding ; Pulmonary Surfactant-Associated Protein D/chemistry ; Pulmonary Surfactant-Associated Protein D/metabolism ; Schistosoma mansoni/metabolism ; Surface Plasmon Resonance ; Time Factors
    Chemical Substances Carbohydrates ; Glycoproteins ; Ligands ; Pulmonary Surfactant-Associated Protein D ; Concanavalin A (11028-71-0) ; Fucose (28RYY2IV3F)
    Language English
    Publishing date 2004-11
    Publishing country United States
    Document type Journal Article
    ZDB-ID 1025960-0
    ISSN 1535-4989 ; 1044-1549
    ISSN (online) 1535-4989
    ISSN 1044-1549
    DOI 10.1165/rcmb.2004-0105OC
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 2851: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
    Jg. 1995 - 2021: Lesesall (2.OG)
    ab Jg. 2022: Lesesaal (EG)

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    This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

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