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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
49
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pubmed:dateCreated |
2000-2-3
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pubmed:abstractText |
We previously reported that CR-Fc, an Fc chimeric protein containing the cysteine-rich (CR) domain of the mannose receptor, binds to marginal zone metallophilic macrophages (Mo) and B cell areas in the spleen and to subcapsular sinus Mo in lymph nodes of naive mice (CR-Fc(+) cells). Several CR-Fc ligands were found in spleen and lymph node tissue lysates using ligand blots. In this paper we report the identification of two of these ligands as sialoadhesin (Sn), an Mo-specific membrane molecule, and the leukocyte common antigen, CD45. CR-Fc bound selectively to Sn purified from spleen and lymph nodes and to two low molecular weight isoforms of CD45 in a sugar-dependent manner. CR-Fc binding and non-binding forms of Sn, probably derived from CR-Fc(+) and CR-Fc(-) cells respectively, were selected from spleen lysates. Analysis of the glycan pool associated with the CR-Fc-binding form revealed the presence of charged structures resistant to sialidase, absent in the non-binding form, that could correspond to sulfated structures. These results confirm the identification of the CR region of the mannose receptor as a lectin. We also demonstrate that the same glycoprotein expressed in different cells of the same organ can display distinct sugar epitopes that determine its binding properties.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, CD45,
http://linkedlifedata.com/resource/pubmed/chemical/Cysteine,
http://linkedlifedata.com/resource/pubmed/chemical/Glycoside Hydrolases,
http://linkedlifedata.com/resource/pubmed/chemical/Immunoglobulin Fragments,
http://linkedlifedata.com/resource/pubmed/chemical/Lectins, C-Type,
http://linkedlifedata.com/resource/pubmed/chemical/Mannose-Binding Lectins,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Glycoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Isoforms,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Cell Surface,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Immunologic,
http://linkedlifedata.com/resource/pubmed/chemical/Sulfates,
http://linkedlifedata.com/resource/pubmed/chemical/erythrocyte receptor,
http://linkedlifedata.com/resource/pubmed/chemical/mannose receptor
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pubmed:status |
MEDLINE
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pubmed:month |
Dec
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pubmed:issn |
0021-9258
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
3
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pubmed:volume |
274
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
35211-8
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pubmed:dateRevised |
2007-11-15
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pubmed:meshHeading |
pubmed-meshheading:10575006-Animals,
pubmed-meshheading:10575006-Antigens, CD45,
pubmed-meshheading:10575006-Blotting, Western,
pubmed-meshheading:10575006-Cell Line,
pubmed-meshheading:10575006-Chromatography, Affinity,
pubmed-meshheading:10575006-Chromatography, High Pressure Liquid,
pubmed-meshheading:10575006-Cysteine,
pubmed-meshheading:10575006-Glycoside Hydrolases,
pubmed-meshheading:10575006-Immunoglobulin Fragments,
pubmed-meshheading:10575006-Lectins, C-Type,
pubmed-meshheading:10575006-Mannose-Binding Lectins,
pubmed-meshheading:10575006-Membrane Glycoproteins,
pubmed-meshheading:10575006-Mice,
pubmed-meshheading:10575006-Mice, Inbred BALB C,
pubmed-meshheading:10575006-Precipitin Tests,
pubmed-meshheading:10575006-Protein Binding,
pubmed-meshheading:10575006-Protein Isoforms,
pubmed-meshheading:10575006-Protein Processing, Post-Translational,
pubmed-meshheading:10575006-Receptors, Cell Surface,
pubmed-meshheading:10575006-Receptors, Immunologic,
pubmed-meshheading:10575006-Spleen,
pubmed-meshheading:10575006-Sulfates,
pubmed-meshheading:10575006-Time Factors
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pubmed:year |
1999
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pubmed:articleTitle |
Cell-specific glycoforms of sialoadhesin and CD45 are counter-receptors for the cysteine-rich domain of the mannose receptor.
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pubmed:affiliation |
Sir William Dunn School of Pathology, Oxford University, Oxford OX1 3RE, Scotland. pomares@worf.molbiol.ox.ac.uk
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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