Cited 137 times in
Functional comparison of the mouse DC‐SIGN, SIGNR1, SIGNR3 and Langerin, C‐type lectins
DC Field | Value | Language |
---|---|---|
dc.contributor.author | 박채규 | - |
dc.date.accessioned | 2015-07-14T17:30:08Z | - |
dc.date.available | 2015-07-14T17:30:08Z | - |
dc.date.issued | 2004 | - |
dc.identifier.issn | 0953-8178 | - |
dc.identifier.uri | https://ir.ymlib.yonsei.ac.kr/handle/22282913/113011 | - |
dc.description.abstract | 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. | - |
dc.description.statementOfResponsibility | open | - |
dc.format.extent | 819~829 | - |
dc.relation.isPartOf | INTERNATIONAL IMMUNOLOGY | - |
dc.rights | CC BY-NC-ND 2.0 KR | - |
dc.rights.uri | https://creativecommons.org/licenses/by-nc-nd/2.0/kr/ | - |
dc.subject.MESH | Animals | - |
dc.subject.MESH | Antigens, CD/physiology* | - |
dc.subject.MESH | Antigens, Surface/genetics | - |
dc.subject.MESH | Antigens, Surface/physiology* | - |
dc.subject.MESH | Candida albicans/cytology | - |
dc.subject.MESH | Cell Adhesion Molecules/genetics | - |
dc.subject.MESH | Cell Adhesion Molecules/physiology* | - |
dc.subject.MESH | Cell Line | - |
dc.subject.MESH | Cricetinae | - |
dc.subject.MESH | Dextrans/analysis | - |
dc.subject.MESH | Escherichia coli/cytology | - |
dc.subject.MESH | Fluorescein-5-isothiocyanate/analogs & derivatives* | - |
dc.subject.MESH | Fluorescein-5-isothiocyanate/analysis | - |
dc.subject.MESH | Humans | - |
dc.subject.MESH | Lectins, C-Type/genetics | - |
dc.subject.MESH | Lectins, C-Type/physiology* | - |
dc.subject.MESH | Mannose-Binding Lectins/genetics | - |
dc.subject.MESH | Mannose-Binding Lectins/physiology* | - |
dc.subject.MESH | Mice | - |
dc.subject.MESH | Phagocytosis/physiology | - |
dc.subject.MESH | Receptors, Cell Surface/genetics | - |
dc.subject.MESH | Receptors, Cell Surface/physiology* | - |
dc.subject.MESH | Salmonella typhimurium/cytology | - |
dc.subject.MESH | Transfection | - |
dc.subject.MESH | Zymosan/analysis | - |
dc.title | Functional comparison of the mouse DC‐SIGN, SIGNR1, SIGNR3 and Langerin, C‐type lectins | - |
dc.type | Article | - |
dc.contributor.college | College of Medicine (의과대학) | - |
dc.contributor.department | Dept. of Life Science (의생명과학부) | - |
dc.contributor.googleauthor | Kazuhiko Takahara | - |
dc.contributor.googleauthor | Yusuke Yashima | - |
dc.contributor.googleauthor | Kayo Inaba | - |
dc.contributor.googleauthor | Chae Gyu Park | - |
dc.contributor.googleauthor | Ralph M. Steinman | - |
dc.contributor.googleauthor | Young‐Sun Kang | - |
dc.contributor.googleauthor | Yukino Kimura | - |
dc.contributor.googleauthor | Hideo Yoshida | - |
dc.contributor.googleauthor | Yoshiki Omatsu | - |
dc.identifier.doi | 10.1093/intimm/dxh084 | - |
dc.admin.author | false | - |
dc.admin.mapping | false | - |
dc.contributor.localId | A01718 | - |
dc.relation.journalcode | J01080 | - |
dc.identifier.eissn | 1460-2377 | - |
dc.identifier.pmid | 15096474 | - |
dc.subject.keyword | dendritic cells | - |
dc.subject.keyword | macrophage | - |
dc.subject.keyword | Gram‐negative bacteria | - |
dc.subject.keyword | phagocytosis | - |
dc.contributor.alternativeName | Park, Chae Gyu | - |
dc.contributor.affiliatedAuthor | Park, Chae Gyu | - |
dc.rights.accessRights | free | - |
dc.citation.volume | 16 | - |
dc.citation.number | 6 | - |
dc.citation.startPage | 819 | - |
dc.citation.endPage | 829 | - |
dc.identifier.bibliographicCitation | INTERNATIONAL IMMUNOLOGY, Vol.16(6) : 819-829, 2004 | - |
dc.identifier.rimsid | 36854 | - |
dc.type.rims | ART | - |
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