| pubmed-article:2982660 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:2982660 | lifeskim:mentions | umls-concept:C0027950 | lld:lifeskim |
| pubmed-article:2982660 | lifeskim:mentions | umls-concept:C0071655 | lld:lifeskim |
| pubmed-article:2982660 | lifeskim:mentions | umls-concept:C0220781 | lld:lifeskim |
| pubmed-article:2982660 | lifeskim:mentions | umls-concept:C0699900 | lld:lifeskim |
| pubmed-article:2982660 | lifeskim:mentions | umls-concept:C1883254 | lld:lifeskim |
| pubmed-article:2982660 | pubmed:issue | 2 | lld:pubmed |
| pubmed-article:2982660 | pubmed:dateCreated | 1985-4-15 | lld:pubmed |
| pubmed-article:2982660 | pubmed:abstractText | The interconversions of the inositol-containing lipids (PI, PI-P and PI-P2) and their products (DG, inositol phosphates and PA) in human and rabbit neutrophils stimulated with fMetLeuPhe and PMA have been examined. PMA causes only the phosphorylation of PI to PI-P whereas fMetLeuPhe causes phosphorylation of both PI and PI-P yielding PI-P2 and the hydrolysis of all three lipids. While the predominant reaction is breakdown of PI to PA catalysed by phospholipase D, approx. 2% of PI is converted to polyphosphoinositides and then broken down by the phospholipase C route yielding inositol phosphates and DG. The latter reaction occurs without detectable lag and is a function of receptor occupancy. The amount of inositol trisphosphate thus formed would be sufficient to release Ca2+ from intracellular stores. | lld:pubmed |
| pubmed-article:2982660 | pubmed:language | eng | lld:pubmed |
| pubmed-article:2982660 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2982660 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:2982660 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:2982660 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:2982660 | pubmed:month | Feb | lld:pubmed |
| pubmed-article:2982660 | pubmed:issn | 0014-5793 | lld:pubmed |
| pubmed-article:2982660 | pubmed:author | pubmed-author:CockcroftSS | lld:pubmed |
| pubmed-article:2982660 | pubmed:author | pubmed-author:GompertsB DBD | lld:pubmed |
| pubmed-article:2982660 | pubmed:author | pubmed-author:BarrowmanM... | lld:pubmed |
| pubmed-article:2982660 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:2982660 | pubmed:day | 25 | lld:pubmed |
| pubmed-article:2982660 | pubmed:volume | 181 | lld:pubmed |
| pubmed-article:2982660 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:2982660 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:2982660 | pubmed:pagination | 259-63 | lld:pubmed |
| pubmed-article:2982660 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
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| pubmed-article:2982660 | pubmed:year | 1985 | lld:pubmed |
| pubmed-article:2982660 | pubmed:articleTitle | Breakdown and synthesis of polyphosphoinositides in fMetLeuPhe-stimulated neutrophils. | lld:pubmed |
| pubmed-article:2982660 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:2982660 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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