| pubmed-article:18332220 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:18332220 | lifeskim:mentions | umls-concept:C0086418 | lld:lifeskim |
| pubmed-article:18332220 | lifeskim:mentions | umls-concept:C0007634 | lld:lifeskim |
| pubmed-article:18332220 | lifeskim:mentions | umls-concept:C0039062 | lld:lifeskim |
| pubmed-article:18332220 | lifeskim:mentions | umls-concept:C0027103 | lld:lifeskim |
| pubmed-article:18332220 | lifeskim:mentions | umls-concept:C0021467 | lld:lifeskim |
| pubmed-article:18332220 | lifeskim:mentions | umls-concept:C0021469 | lld:lifeskim |
| pubmed-article:18332220 | lifeskim:mentions | umls-concept:C0036588 | lld:lifeskim |
| pubmed-article:18332220 | pubmed:issue | 5 | lld:pubmed |
| pubmed-article:18332220 | pubmed:dateCreated | 2008-3-11 | lld:pubmed |
| pubmed-article:18332220 | pubmed:abstractText | Phagocytosis of foreign cells or particles by macrophages is a rapid process that is inefficient when faced with "self" cells that display CD47-although signaling mechanisms in self-recognition have remained largely unknown. With human macrophages, we show the phagocytic synapse at cell contacts involves a basal level of actin-driven phagocytosis that, in the absence of species-specific CD47 signaling, is made more efficient by phospho-activated myosin. We use "foreign" sheep red blood cells (RBCs) together with CD47-blocked, antibody-opsonized human RBCs in order to visualize synaptic accumulation of phosphotyrosine, paxillin, F-actin, and the major motor isoform, nonmuscle myosin-IIA. When CD47 is functional, the macrophage counter-receptor and phosphatase-activator SIRPalpha localizes to the synapse, suppressing accumulation of phosphotyrosine and myosin without affecting F-actin. On both RBCs and microbeads, human CD47 potently inhibits phagocytosis as does direct inhibition of myosin. CD47-SIRPalpha interaction initiates a dephosphorylation cascade directed in part at phosphotyrosine in myosin. A point mutation turns off this motor's contribution to phagocytosis, suggesting that self-recognition inhibits contractile engulfment. | lld:pubmed |
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| pubmed-article:18332220 | pubmed:language | eng | lld:pubmed |
| pubmed-article:18332220 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18332220 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:18332220 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:18332220 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:18332220 | pubmed:month | Mar | lld:pubmed |
| pubmed-article:18332220 | pubmed:issn | 1540-8140 | lld:pubmed |
| pubmed-article:18332220 | pubmed:author | pubmed-author:DischerDennis... | lld:pubmed |
| pubmed-article:18332220 | pubmed:author | pubmed-author:TsaiRichard... | lld:pubmed |
| pubmed-article:18332220 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:18332220 | pubmed:day | 10 | lld:pubmed |
