Source:http://linkedlifedata.com/resource/pubmed/id/20826801
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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
49
|
| pubmed:dateCreated |
2010-11-29
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| pubmed:abstractText |
Interaction of SIRP? with its ligand, CD47, regulates leukocyte functions, including transmigration, phagocytosis, oxidative burst, and cytokine secretion. Recent progress has provided significant insights into the structural details of the distal IgV domain (D1) of SIRP?. However, the structural roles of proximal IgC domains (D2 and D3) have been largely unstudied. The high degree of conservation of D2 and D3 among members of the SIRP family as well as the propensity of known IgC domains to assemble in cis has led others to hypothesize that SIRP? forms higher order structures on the cell surface. Here we report that SIRP? forms noncovalently linked cis homodimers. Treatment of SIRP?-expressing cells with a membrane-impermeable cross-linker resulted in the formation of SDS-stable SIRP? dimers and oligomers. Biochemical analyses of soluble recombinant extracellular regions of SIRP?, including domain truncation mutants, revealed that each of the three extracellular immunoglobulin loops of SIRP? formed dimers in solution. Co-immunoprecipitation experiments using cells transfected with different affinity-tagged SIRP? molecules revealed that SIRP? forms cis dimers. Interestingly, in cells treated with tunicamycin, SIRP? dimerization but not CD47 binding was inhibited, suggesting that a SIRP? dimer is probably bivalent. Last, we demonstrate robust dimerization of SIRPa in adherent, stimulated human neutrophils. Collectively, these data are consistent with SIRP? being expressed on the cell surface as a functional cis-linked dimer.
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| pubmed:grant | |
| pubmed:language |
eng
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| pubmed:journal | |
| pubmed:citationSubset |
IM
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| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, CD47,
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, Differentiation,
http://linkedlifedata.com/resource/pubmed/chemical/CD47 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Immunologic,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/SIRPA protein, human
|
| pubmed:status |
MEDLINE
|
| pubmed:month |
Dec
|
| pubmed:issn |
1083-351X
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| pubmed:author | |
| pubmed:issnType |
Electronic
|
| pubmed:day |
3
|
| pubmed:volume |
285
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
37953-63
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| pubmed:dateRevised |
2011-1-6
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| pubmed:meshHeading |
pubmed-meshheading:20826801-Animals,
pubmed-meshheading:20826801-Antigens, CD47,
pubmed-meshheading:20826801-Antigens, Differentiation,
pubmed-meshheading:20826801-CHO Cells,
pubmed-meshheading:20826801-Cell Adhesion,
pubmed-meshheading:20826801-Cricetinae,
pubmed-meshheading:20826801-Cricetulus,
pubmed-meshheading:20826801-HEK293 Cells,
pubmed-meshheading:20826801-HL-60 Cells,
pubmed-meshheading:20826801-Humans,
pubmed-meshheading:20826801-Mutation,
pubmed-meshheading:20826801-Neutrophil Activation,
pubmed-meshheading:20826801-Neutrophils,
pubmed-meshheading:20826801-Protein Binding,
pubmed-meshheading:20826801-Protein Multimerization,
pubmed-meshheading:20826801-Protein Structure, Tertiary,
pubmed-meshheading:20826801-Receptors, Immunologic,
pubmed-meshheading:20826801-Recombinant Proteins
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| pubmed:year |
2010
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| pubmed:articleTitle |
The role of cis dimerization of signal regulatory protein alpha (SIRPalpha) in binding to CD47.
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| pubmed:affiliation |
Epithelial Pathobiology Unit, Department of Pathology and Laboratory Medicine, Emory University School of Medicine, Atlanta, Georgia 30322, USA.
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| pubmed:publicationType |
Journal Article,
Research Support, N.I.H., Extramural
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