Source:http://linkedlifedata.com/resource/pubmed/id/15096474
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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
6
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| pubmed:dateCreated |
2004-5-20
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| pubmed:abstractText |
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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| pubmed:grant | |
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
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| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, CD,
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, Surface,
http://linkedlifedata.com/resource/pubmed/chemical/CD207 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Cd207 protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Cell Adhesion Molecules,
http://linkedlifedata.com/resource/pubmed/chemical/DC-specific ICAM-3 grabbing...,
http://linkedlifedata.com/resource/pubmed/chemical/Dextrans,
http://linkedlifedata.com/resource/pubmed/chemical/Fluorescein-5-isothiocyanate,
http://linkedlifedata.com/resource/pubmed/chemical/Lectins, C-Type,
http://linkedlifedata.com/resource/pubmed/chemical/Mannose-Binding Lectins,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Cell Surface,
http://linkedlifedata.com/resource/pubmed/chemical/Zymosan,
http://linkedlifedata.com/resource/pubmed/chemical/fluorescein isothiocyanate dextran
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| pubmed:status |
MEDLINE
|
| pubmed:month |
Jun
|
| pubmed:issn |
0953-8178
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| pubmed:author | |
| pubmed:copyrightInfo |
Copyright 2004 The Japanese Society for Immunology
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| pubmed:issnType |
Print
|
| pubmed:volume |
16
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
819-29
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| pubmed:dateRevised |
2007-11-14
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| pubmed:meshHeading |
pubmed-meshheading:15096474-Animals,
pubmed-meshheading:15096474-Antigens, CD,
pubmed-meshheading:15096474-Antigens, Surface,
pubmed-meshheading:15096474-Candida albicans,
pubmed-meshheading:15096474-Cell Adhesion Molecules,
pubmed-meshheading:15096474-Cell Line,
pubmed-meshheading:15096474-Cricetinae,
pubmed-meshheading:15096474-Dextrans,
pubmed-meshheading:15096474-Escherichia coli,
pubmed-meshheading:15096474-Fluorescein-5-isothiocyanate,
pubmed-meshheading:15096474-Humans,
pubmed-meshheading:15096474-Lectins, C-Type,
pubmed-meshheading:15096474-Mannose-Binding Lectins,
pubmed-meshheading:15096474-Mice,
pubmed-meshheading:15096474-Phagocytosis,
pubmed-meshheading:15096474-Receptors, Cell Surface,
pubmed-meshheading:15096474-Salmonella typhimurium,
pubmed-meshheading:15096474-Transfection,
pubmed-meshheading:15096474-Zymosan
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| pubmed:year |
2004
|
| pubmed:articleTitle |
Functional comparison of the mouse DC-SIGN, SIGNR1, SIGNR3 and Langerin, C-type lectins.
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| pubmed:affiliation |
Laboratory of Immunobiology, Department of Animal Development and Physiology, Division of Systemic Life Science, Graduate School of Biostudies, Graduate School of Science, Kyoto University, Kitashirakawa-Oiwake-cho, Sakyo-ku, Kyoto 606-8502, Japan.
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| pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
|