Tyrosine phosphorylation is involved in the respiratory burst of electropermeabilized human neutrophils at a step before diacylglycerol formation by phospholipase C

We studied a step where tyrosine phosphorylation is involved in a signaling pathway for the activation of the superoxide (O − 2)-generating NADPH oxidase using electropermeabilized human neutrophils. The permeabilized cells produced O − 2 by the addition of a protein tyrosine phosphatase inhibitor,...

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Bibliographic Details
Published in:FEBS letters 1993-05, Vol.322 (3), p.280-284
Main Authors: Mitsuyama, Takashi, Takeshige, Koichiro, Minakami, Shigeki
Format: Article
Language:English
Subjects:
1,2-diacylglycerol
Biological and medical sciences
Cell Membrane Permeability
Cell physiology
Cinnamates - pharmacology
DAG
Diglycerides - metabolism
Electropermeabilization
Ethanol - pharmacology
Fundamental and applied biological sciences. Psychology
Human neutrophil
Humans
In Vitro Techniques
l-α-phosphatidylinositol 4,5-bisphosphate
MAP kinase
mitogen-activated protein kinase
Molecular and cellular biology
Naphthalenes
Neomycin - pharmacology
Neutrophils - drug effects
Neutrophils - metabolism
Oxygen - metabolism
Phospholipase C
phospholipase D
Phosphorylation
PIP2
PKC
PLC
PLD
Polycyclic Compounds - pharmacology
protein kinase C
Protein Kinase C - antagonists & inhibitors
Protein-Tyrosine Kinases - antagonists & inhibitors
Respiratory Burst
Signal transduction
Sulfides - pharmacology
Type C Phospholipases - metabolism
Tyrosine - metabolism
Tyrosine phosphorylation
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Summary:We studied a step where tyrosine phosphorylation is involved in a signaling pathway for the activation of the superoxide (O − 2)-generating NADPH oxidase using electropermeabilized human neutrophils. The permeabilized cells produced O − 2 by the addition of a protein tyrosine phosphatase inhibitor, vanadate, as well as N-formyl-methionyl-leucyl-phenylalanine (fMLP) and protein kinase C (PKC) activators such as phorbol myristate acetate (PMA) and l-α- 1 -oleoyl-2-acetoyl- sn-3-glycerol (OAG). The O − 2 production by the stimulants was completely inhibited by PKC inhibitors such as calphostin C and staurosporine and was not affected by 1 % ethanol, a metabolic modulator of phospholipase D (PLD). Furthermore, the O − 2 production by vanadate and fMLP, but not by OAG and PMA, was inhibited by both an inhibitor of phospholipase C (PLC), neomycin, and an inhibitor of tyrosine kinase, ST-638. These findings suggest that tyrosine phosphorylation is involved in the activation of the oxidase at a step before diacylglycerol formation by PLC, and that PLD may not be involved in the signaling pathway in permeabilized cells.
ISSN:0014-5793
1873-3468
DOI:10.1016/0014-5793(93)81586-O