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 (3), p.597-600
Hauptverfasser:	UINGS, IJ, THOMPSON, NT, RANDALL, RW, SPACEY, GD, BONSER, RW, HUDSON, AT, GARLAND, LG
Format:	Artikel
Sprache:	eng
Schlagworte:	Biochemistry & Molecular Biology Enzyme Activation Humans Indoles Life Sciences & Biomedicine 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 Science & Technology Type C Phospholipases - metabolism Tyrosine - analogs & derivatives Tyrosine - metabolism
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