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PMID: 1371383 Published · ppublish English Journal Article

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

The Biochemical journal ·Vol. 281 ( Pt 3) ·1992-02-01 ·Pages 597-600

Uings IJ, Thompson NT, Randall RW, Spacey GD, Bonser RW, Hudson AT, Garland LG

Abstract

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.

MeSH Terms
Enzyme Activation Humans Indoles N-Formylmethionine Leucyl-Phenylalanine/pharmacology Neutrophils/drug effects,enzymology Phorbol 12,13-Dibutyrate/pharmacology Phosphatidylinositol Diacylglycerol-Lyase Phospholipase D/metabolism Phosphoric Diester Hydrolases/metabolism Phosphorylation Phosphotyrosine Protein Kinase C/antagonists & inhibitors,pharmacology Protein-Tyrosine Kinases/metabolism Receptors, Cell Surface/physiology Type C Phospholipases/metabolism Tyrosine/analogs & derivatives,metabolism
Chemicals
Indoles Receptors, Cell Surface Phosphotyrosine Phorbol 12,13-Dibutyrate Tyrosine N-Formylmethionine Leucyl-Phenylalanine Protein-Tyrosine Kinases Protein Kinase C Phosphoric Diester Hydrolases Type C Phospholipases Phospholipase D Phosphatidylinositol Diacylglycerol-Lyase Ro 31-8220
Authors & Affiliations
7 authors, click to expand affiliations / ORCID
Uings I J
Cell Signalling Group, Biochemical Sciences, Wellcome Research Laboratories, Kent, U.K.
Thompson N T
Randall R W
Spacey G D
Bonser R W
Hudson A T
Garland L G
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Article Info
Journal
The Biochemical journal
Abbr.
Biochem J
ISSN
0264-6021
DOI
10.1042/bj2810597
Published
1992-02-01
Pages
597-600
Language
English
Region
England
NLM ID
2984726R
PMCID
PMC1130730
Subset
IM
Corrections
ErratumIn
-
External Links
PubMed source DOI: 10.1042/bj2810597 PMC Full Text View journal details
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