pubmed-article:1371383 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:1371383 | lifeskim:mentions | umls-concept:C0086418 | lld:lifeskim |
pubmed-article:1371383 | lifeskim:mentions | umls-concept:C0027950 | lld:lifeskim |
pubmed-article:1371383 | lifeskim:mentions | umls-concept:C0031670 | lld:lifeskim |
pubmed-article:1371383 | lifeskim:mentions | umls-concept:C1519726 | lld:lifeskim |
pubmed-article:1371383 | lifeskim:mentions | umls-concept:C0031669 | lld:lifeskim |
pubmed-article:1371383 | lifeskim:mentions | umls-concept:C0597359 | lld:lifeskim |
pubmed-article:1371383 | lifeskim:mentions | umls-concept:C1314939 | lld:lifeskim |
pubmed-article:1371383 | pubmed:dateCreated | 1992-3-24 | lld:pubmed |
pubmed-article:1371383 | pubmed:abstractText | The tyrosine kinase inhibitors ST271, ST638 and erbstatin inhibited phospholipase D (PLD) activity in human neutrophils stimulated by fMet-Leu-Phe, platelet-activating factor and leukotriene B4. These compounds did not inhibit phorbol ester-stimulated PLD, indicating that they do not inhibit PLD per se, but probably act at a site between the receptor and the phospholipase. In contrast, the protein kinase C inhibitor Ro-31-8220 inhibited phorbol 12,13-dibutyrate- but not fMet-Leu-Phe-stimulated PLD activity, arguing against the involvement of protein kinase C in the receptor-mediated activation of PLD. ST271 did not inhibit Ins(1,4,5)P3 generation, but did inhibit protein tyrosine phosphorylation stimulated by fMet-Leu-Phe. The phosphotyrosine phosphatase inhibitor pervanadate increased tyrosine phosphorylation and stimulated PLD. These results suggest that tyrosine kinase activity is involved in receptor coupling to PLD but not to PtdIns(4,5)P2-specific phospholipase C in the human neutrophil. | lld:pubmed |
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pubmed-article:1371383 | pubmed:language | eng | lld:pubmed |
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pubmed-article:1371383 | pubmed:citationSubset | IM | lld:pubmed |
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pubmed-article:1371383 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:1371383 | pubmed:month | Feb | lld:pubmed |
pubmed-article:1371383 | pubmed:issn | 0264-6021 | lld:pubmed |
pubmed-article:1371383 | pubmed:author | pubmed-author:ThompsonN TNT | lld:pubmed |
pubmed-article:1371383 | pubmed:author | pubmed-author:GarlandL GLG | lld:pubmed |
pubmed-article:1371383 | pubmed:author | pubmed-author:RandallR WRW | lld:pubmed |
pubmed-article:1371383 | pubmed:author | pubmed-author:SpaceyG DGD | lld:pubmed |
pubmed-article:1371383 | pubmed:author | pubmed-author:BonserR WRW | lld:pubmed |
pubmed-article:1371383 | pubmed:author | pubmed-author:HudsonA TAT | lld:pubmed |
pubmed-article:1371383 | pubmed:author | pubmed-author:UingsI JIJ | lld:pubmed |
pubmed-article:1371383 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:1371383 | pubmed:day | 1 | lld:pubmed |
pubmed-article:1371383 | pubmed:volume | 281 ( Pt 3) | lld:pubmed |
pubmed-article:1371383 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:1371383 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:1371383 | pubmed:pagination | 597-600 | lld:pubmed |
pubmed-article:1371383 | pubmed:dateRevised | 2010-9-7 | lld:pubmed |
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pubmed-article:1371383 | pubmed:year | 1992 | lld:pubmed |
pubmed-article:1371383 | pubmed:articleTitle | Tyrosine phosphorylation is involved in receptor coupling to phospholipase D but not phospholipase C in the human neutrophil. | lld:pubmed |
pubmed-article:1371383 | pubmed:affiliation | Cell Signalling Group, Biochemical Sciences, Wellcome Research Laboratories, Kent, U.K. | lld:pubmed |
pubmed-article:1371383 | pubmed:publicationType | Journal Article | lld:pubmed |
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