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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
23
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pubmed:dateCreated |
2010-11-16
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pubmed:abstractText |
CD91 plays an important role in the scavenging of apoptotic material, possibly through binding to soluble pattern-recognition molecules. In this study, we investigated the interaction of CD91 with mannan-binding lectin (MBL), ficolins and lung surfactant proteins. Both MBL and L-ficolin were found to bind CD91. The MBL-CD91 interaction was time- and concentration-dependent and could be inhibited by known ligands of CD91. MBL-associated serine protease 3 (MASP-3) also inhibited binding between MBL and CD91, suggesting that the site of interaction is located at or near the MASP-MBL interaction site. This was confirmed by using MBL mutants deficient for MASP binding that were unable to interact with CD91. These findings demonstrate that MBL and L-ficolin interact with CD91, strongly suggesting that they have the potential to function as soluble recognition molecules for scavenging microbial and apoptotic material by CD91.
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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, CD,
http://linkedlifedata.com/resource/pubmed/chemical/Calcium,
http://linkedlifedata.com/resource/pubmed/chemical/LRP1 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Lectins,
http://linkedlifedata.com/resource/pubmed/chemical/Ligands,
http://linkedlifedata.com/resource/pubmed/chemical/Low Density Lipoprotein...,
http://linkedlifedata.com/resource/pubmed/chemical/MASP1 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/MBL2 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Mannose-Binding Lectin,
http://linkedlifedata.com/resource/pubmed/chemical/Mannose-Binding Protein-Associated...,
http://linkedlifedata.com/resource/pubmed/chemical/Mutant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/ficolin
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pubmed:status |
MEDLINE
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pubmed:month |
Dec
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pubmed:issn |
1742-4658
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pubmed:author |
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pubmed:copyrightInfo |
© 2010 The Authors Journal compilation © 2010 FEBS.
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pubmed:issnType |
Electronic
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pubmed:volume |
277
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
4956-64
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pubmed:dateRevised |
2011-11-17
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pubmed:meshHeading |
pubmed-meshheading:21054788-Amino Acid Substitution,
pubmed-meshheading:21054788-Antigens, CD,
pubmed-meshheading:21054788-Binding Sites,
pubmed-meshheading:21054788-Calcium,
pubmed-meshheading:21054788-Humans,
pubmed-meshheading:21054788-Kinetics,
pubmed-meshheading:21054788-Lectins,
pubmed-meshheading:21054788-Ligands,
pubmed-meshheading:21054788-Low Density Lipoprotein Receptor-Related Protein-1,
pubmed-meshheading:21054788-Mannose-Binding Lectin,
pubmed-meshheading:21054788-Mannose-Binding Protein-Associated Serine Proteases,
pubmed-meshheading:21054788-Mutagenesis, Site-Directed,
pubmed-meshheading:21054788-Mutant Proteins,
pubmed-meshheading:21054788-Protein Binding,
pubmed-meshheading:21054788-Recombinant Proteins,
pubmed-meshheading:21054788-Surface Plasmon Resonance
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pubmed:year |
2010
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pubmed:articleTitle |
CD91 interacts with mannan-binding lectin (MBL) through the MBL-associated serine protease-binding site.
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pubmed:affiliation |
Department of Clinical Biochemistry and Immunology, Statens Serum Institut, Artillerivej 5, Copenhagen, Denmark. kds@ssi.dk
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pubmed:publicationType |
Journal Article,
In Vitro
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