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Functional comparison of the mouse DC‐SIGN, SIGNR1, SIGNR3 and Langerin, C‐type lectins

 Kazuhiko Takahara  ;  Yusuke Yashima  ;  Kayo Inaba  ;  Chae Gyu Park  ;  Ralph M. Steinman  ;  Young‐Sun Kang  ;  Yukino Kimura  ;  Hideo Yoshida  ;  Yoshiki Omatsu 
 INTERNATIONAL IMMUNOLOGY, Vol.16(6) : 819-829, 2004 
Journal Title
Issue Date
Animals ; Antigens, CD/physiology* ; Antigens, Surface/genetics ; Antigens, Surface/physiology* ; Candida albicans/cytology ; Cell Adhesion Molecules/genetics ; Cell Adhesion Molecules/physiology* ; Cell Line ; Cricetinae ; Dextrans/analysis ; Escherichia coli/cytology ; Fluorescein-5-isothiocyanate/analogs & derivatives* ; Fluorescein-5-isothiocyanate/analysis ; Humans ; Lectins, C-Type/genetics ; Lectins, C-Type/physiology* ; Mannose-Binding Lectins/genetics ; Mannose-Binding Lectins/physiology* ; Mice ; Phagocytosis/physiology ; Receptors, Cell Surface/genetics ; Receptors, Cell Surface/physiology* ; Salmonella typhimurium/cytology ; Transfection ; Zymosan/analysis
dendritic cells ; macrophage ; Gram‐negative bacteria ; phagocytosis
The mouse (m) DC-SIGN family consists of several homologous type II transmembrane proteins located in close proximity on chromosome 8 and having a single carboxyl terminal carbohydrate recognition domain. We first used transfected non-macrophage cell lines to compare the polysaccharide and microbial uptake capacities of three of these lectins--DC-SIGN, SIGNR1 and SIGNR3--to another homologue mLangerin. Each molecule shares a potential mannose-recognition EPN-motif in its carbohydrate recognition domain. Using an anti-Tag antibody to follow Tag-labeled transfectants, we found that each molecule could be internalized, although the rates differed. However, mDC-SIGN was unable to take up FITC-dextran, FITC-ovalbumin, zymosan or heat-killed Candida albicans. The other three lectins showed distinct carbohydrate recognition properties, assessed by blocking FITC-dextran uptake at 37 degrees C and by mannan binding activity at 4 degrees C. Furthermore, only SIGNR1 was efficient in mediating the capture by transfected cells of Gram-negative bacteria, such as Escherichia coli and Salmonella typhimurium, while none of the lectins tested were competent to capture Gram-positive bacteria, Staphylococcus aureus. Interestingly, transfectants with SIGNR1 lacking the cytoplasmic domain were capable of binding FITC-zymosan in a manner that was abolished by EDTA or mannan, but not laminarin. In addition, resident peritoneal CD11b+ cells expressing SIGNR1 bound zymosan at 4 degrees C in concert with a laminarin-sensitive receptor. Therefore these homologous C-type lectins have distinct recognition patters for microbes despite similarities in the carbohydrate recognition domains.
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1. College of Medicine (의과대학) > BioMedical Science Institute (의생명과학부) > 1. Journal Papers
Yonsei Authors
Park, Chae Gyu(박채규) ORCID logo https://orcid.org/0000-0003-1906-1308
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