| pubmed-article:17475884 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:17475884 | lifeskim:mentions | umls-concept:C0027950 | lld:lifeskim |
| pubmed-article:17475884 | lifeskim:mentions | umls-concept:C0886515 | lld:lifeskim |
| pubmed-article:17475884 | lifeskim:mentions | umls-concept:C0037083 | lld:lifeskim |
| pubmed-article:17475884 | lifeskim:mentions | umls-concept:C0024367 | lld:lifeskim |
| pubmed-article:17475884 | lifeskim:mentions | umls-concept:C1424979 | lld:lifeskim |
| pubmed-article:17475884 | lifeskim:mentions | umls-concept:C1710082 | lld:lifeskim |
| pubmed-article:17475884 | lifeskim:mentions | umls-concept:C0456387 | lld:lifeskim |
| pubmed-article:17475884 | lifeskim:mentions | umls-concept:C0205263 | lld:lifeskim |
| pubmed-article:17475884 | lifeskim:mentions | umls-concept:C1313915 | lld:lifeskim |
| pubmed-article:17475884 | lifeskim:mentions | umls-concept:C0425087 | lld:lifeskim |
| pubmed-article:17475884 | pubmed:issue | 10 | lld:pubmed |
| pubmed-article:17475884 | pubmed:dateCreated | 2007-5-3 | lld:pubmed |
| pubmed-article:17475884 | pubmed:abstractText | Lysophosphatidylcholine has been shown to enhance neutrophil functions through a mechanism involving the G protein-coupled receptor G2A. Recent data support an indirect effect of lysophosphatidylcholine on G2A rather than direct ligand binding. These observations prompted the hypothesis that other lysophospholipids (lyso-PLs) may also signal for human neutrophil activation through G2A. To this end, 1-oleoyl-2-hydroxy-sn-glycero-3-[phospho-L-choline], but also C18:1/OH lyso-PLs bearing the phosphoserine and phosphoethanolamine head groups, presented on albumin, were shown to signal for calcium flux in a self- and cross-desensitizing manner, implicating a single receptor. Blocking Abs to G2A inhibited calcium signaling by all three lyso-PLs. Furthermore, inhibition by both pertussis toxin and U-73122 established signaling via the Galphai/phospholipase C pathway for calcium mobilization. Altered plasma membrane localization of G2A has been hypothesized to facilitate signaling. Accordingly, an increase in detectable G2A was demonstrated by 1 min after lyso-PL stimulation and was followed by visible patching of the receptor. Western blotting showed that G2A resides in the plasma membrane/secretory vesicle fraction and not in neutrophil primary, secondary, or tertiary granules. Enhanced detection of G2A induced by lyso-PLs was paralleled by enhanced detection of CD45, confirming mobilization of the labile secretory vesicle pool. Together, these data show that lyso-PLs bearing various head groups redundantly mobilize G2A latent within secretory vesicles and result in G2A receptor/Galphai/phospholipase C signaling for calcium flux in neutrophils. | lld:pubmed |
| pubmed-article:17475884 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:17475884 | pubmed:language | eng | lld:pubmed |
| pubmed-article:17475884 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17475884 | pubmed:citationSubset | AIM | lld:pubmed |
| pubmed-article:17475884 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:17475884 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17475884 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:17475884 | pubmed:month | May | lld:pubmed |
| pubmed-article:17475884 | pubmed:issn | 0022-1767 | lld:pubmed |
| pubmed-article:17475884 | pubmed:author | pubmed-author:BorregaardNie... | lld:pubmed |
| pubmed-article:17475884 | pubmed:author | pubmed-author:HensonPeter... | lld:pubmed |
| pubmed-article:17475884 | pubmed:author | pubmed-author:MurphyRobert... | lld:pubmed |
| pubmed-article:17475884 | pubmed:author | pubmed-author:BrattonDonna... | lld:pubmed |
| pubmed-article:17475884 | pubmed:author | pubmed-author:FraschS... | lld:pubmed |
| pubmed-article:17475884 | pubmed:author | pubmed-author:Zemski-BerryK... | lld:pubmed |
| pubmed-article:17475884 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:17475884 | pubmed:day | 15 | lld:pubmed |
| pubmed-article:17475884 | pubmed:volume | 178 | lld:pubmed |
| pubmed-article:17475884 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:17475884 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:17475884 | pubmed:pagination | 6540-8 | lld:pubmed |
| pubmed-article:17475884 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
| pubmed-article:17475884 | pubmed:meshHeading | pubmed-meshheading:17475884... | lld:pubmed |
| pubmed-article:17475884 | pubmed:meshHeading | pubmed-meshheading:17475884... | lld:pubmed |
| pubmed-article:17475884 | pubmed:meshHeading | pubmed-meshheading:17475884... | lld:pubmed |
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| pubmed-article:17475884 | pubmed:meshHeading | pubmed-meshheading:17475884... | lld:pubmed |
| pubmed-article:17475884 | pubmed:meshHeading | pubmed-meshheading:17475884... | lld:pubmed |
| pubmed-article:17475884 | pubmed:meshHeading | pubmed-meshheading:17475884... | lld:pubmed |
| pubmed-article:17475884 | pubmed:meshHeading | pubmed-meshheading:17475884... | lld:pubmed |
| pubmed-article:17475884 | pubmed:meshHeading | pubmed-meshheading:17475884... | lld:pubmed |
| pubmed-article:17475884 | pubmed:meshHeading | pubmed-meshheading:17475884... | lld:pubmed |
| pubmed-article:17475884 | pubmed:meshHeading | pubmed-meshheading:17475884... | lld:pubmed |
| pubmed-article:17475884 | pubmed:year | 2007 | lld:pubmed |
| pubmed-article:17475884 | pubmed:articleTitle | Lysophospholipids of different classes mobilize neutrophil secretory vesicles and induce redundant signaling through G2A. | lld:pubmed |
| pubmed-article:17475884 | pubmed:affiliation | Department of Pediatrics, Division of Cell Biology, National Jewish Medical and Research Center, Denver, CO 80206, USA. | lld:pubmed |
| pubmed-article:17475884 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:17475884 | pubmed:publicationType | Research Support, N.I.H., Extramural | lld:pubmed |
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