Source:http://linkedlifedata.com/resource/pubmed/id/16697668
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rdf:type | |
lifeskim:mentions |
umls-concept:C0009085,
umls-concept:C0025914,
umls-concept:C0026809,
umls-concept:C0037083,
umls-concept:C0086418,
umls-concept:C0205164,
umls-concept:C0220248,
umls-concept:C0425245,
umls-concept:C0596901,
umls-concept:C0600253,
umls-concept:C1332713,
umls-concept:C1415831,
umls-concept:C1705241,
umls-concept:C1705242,
umls-concept:C1710082,
umls-concept:C2239666
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pubmed:issue |
3
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pubmed:dateCreated |
2006-5-31
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pubmed:abstractText |
Integrin Associated Protein (IAP, CD47) is a ubiquitous integral membrane protein implicated in processes (in mice) that range from inhibiting clearance by phagocytes [Oldenborg et al., Science 2000; Gardai et al., Cell 2005] to neutrophil motility [Lindberg et al., Science 1996]. SIRPalpha is CD47's main receptor on phagocytes plus a number of other cell types, and SIRPalpha-CD47 interactions in clusters are believed to mediate signaling. However, considerable species differences in CD47 sequence as well as differences in CD47 extractability from mouse cells versus man motivate a characterization of mobility, clusterability, and kinetics under force of CD47-SIRPalpha. Despite similar levels of CD47 on red cells from mouse and man, we find an effective avidity of SIRPalpha-CD47 for mouse appears higher than for human. Both mouse and human CD47 show clustering by multivalent SIRPalpha complexes, but only mouse cells aggregate with CD47 concentrating at cell-cell contacts. This proves consistent with fluorescence imaged micro-deformation, which indicates near-complete mobility of CD47 on mouse cells compared to only about 30-40% mobility on normal human cells. To qualify the method, we also show that disrupting cellular F-actin dramatically increases the mobility of integral membrane proteins. Furthermore, atomic force microscopy probing of cell membranes with human SIRPalpha confirms the species-specific interactions and provides evidence of clustering and adhesion on short time scales, but it also shows surprisingly strong forces in detachment for a signaling complex. The results thus highlight major species differences in CD47-SIRPalpha interactions and CD47 integration, suggesting that signaling by CD47 in man may be qualitatively different from mouse.
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pubmed:commentsCorrections | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:issn |
1079-9796
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
36
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
364-72
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pubmed:dateRevised |
2007-2-6
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pubmed:meshHeading |
pubmed-meshheading:16697668-Animals,
pubmed-meshheading:16697668-Antigens, CD47,
pubmed-meshheading:16697668-COS Cells,
pubmed-meshheading:16697668-Cercopithecus aethiops,
pubmed-meshheading:16697668-Humans,
pubmed-meshheading:16697668-Mice,
pubmed-meshheading:16697668-Protein Binding,
pubmed-meshheading:16697668-Rats,
pubmed-meshheading:16697668-Receptor Aggregation,
pubmed-meshheading:16697668-Receptors, Immunologic,
pubmed-meshheading:16697668-Signal Transduction,
pubmed-meshheading:16697668-Species Specificity
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pubmed:articleTitle |
Membrane mobility and clustering of Integrin Associated Protein (IAP, CD47)--major differences between mouse and man and implications for signaling.
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pubmed:affiliation |
Institute for Medicine and Engineering, University of Pennsylvania, Philadelphia, PA 19104, USA.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't,
Research Support, N.I.H., Extramural
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