Tyrosine phosphorylation is involved in receptor coupling to phospholipase D but not phospholipase C in the human neutrophil

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...

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Veröffentlicht in:	Biochemical journal 1992-02, Vol.281 ( Pt 3) (3), p.597-600
Hauptverfasser:	Uings, I J, Thompson, N T, Randall, R W, Spacey, G D, Bonser, R W, Hudson, A T, Garland, L G
Format:	Artikel
Sprache:	eng
Schlagworte:	Enzyme Activation Humans Indoles N-Formylmethionine Leucyl-Phenylalanine - pharmacology Neutrophils - drug effects Neutrophils - enzymology Phorbol 12,13-Dibutyrate - pharmacology Phosphatidylinositol Diacylglycerol-Lyase Phospholipase D - metabolism Phosphoric Diester Hydrolases - metabolism Phosphorylation Phosphotyrosine Protein Kinase C - antagonists & inhibitors Protein Kinase C - pharmacology Protein-Tyrosine Kinases - metabolism Receptors, Cell Surface - physiology Type C Phospholipases - metabolism Tyrosine - analogs & derivatives Tyrosine - metabolism
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