Measurement of Lectin-Induced Superoxide Release from Human Neutrophils

1993 ◽  
pp. 365-368
Author(s):  
A. V. Timoshenko ◽  
H.-J. Gabius
Keyword(s):  
Human Neutrophils ◽  
Superoxide Release

Calcium Is Required for PMA Induced Superoxide Release From Human Neutrophils

1990 ◽  
Vol 48 (1) ◽  
pp. 89-96 ◽  
Author(s):  
Y. Ishihara ◽  
D.L. Rosolia ◽  
P.J. McKenna ◽  
S.P. Peters ◽  
K.H. Albertine ◽  
...  
Keyword(s):  
Human Neutrophils ◽  
Superoxide Release

Measurement of superoxide release in the phagovacuoles of immune complex-stimulated human neutrophils

1990 ◽  
Vol 130 (2) ◽  
pp. 223-233 ◽  
Author(s):  
Thomas C. Ryan ◽  
Gary J. Weil ◽  
Peter E. Newburger ◽  
Richard Haugland ◽  
Elizabeth R. Simons
Keyword(s):  
Immune Complex ◽  
Human Neutrophils ◽  
Superoxide Release

Phospholipases and the Activation and Priming of Neutrophils by Peritoneal Dialysis Effluent

1997 ◽  
Vol 17 (5) ◽  
pp. 471-479 ◽  
Author(s):  
Mark A. Lindsay ◽  
Ian Daniels ◽  
John Fletcher
Keyword(s):  
Peritoneal Dialysis ◽  
Nadph Oxidase ◽  
Nicotinamide Adenine Dinucleotide Phosphate ◽  
Human Neutrophils ◽  
Induced Response ◽  
Pla2 Activity ◽  
Nonsignificant Increase ◽  
Dependent Inhibition ◽  
Peritoneal Dialysis Effluent ◽  
Superoxide Release

Objective To investigate the role of phospholipases during the activation and priming of neutrophil nicotinamide adenine dinucleotide phosphate (NADPH) oxidase by peritoneal dialysis effluent (PDE). Design Examine the action of 4-hour dwell PDE upon phospholipase activation in the circulating neutrophils obtained from healthy individuals. Results We have previously reported that PDE stimulated superoxide release by the NADPH oxidase of human neutrophils and primed the response to the bacterial peptide, fMLP (fMetLeuPhe). To elucidate the biochemical mechanisms underlying these observations, we have examined the roles of phospholipases (PL) C, D, and A2, whose activation causes the release of a range of intracellular secondary messengers. Following fMLP stimulation, we observed a rapid activation of both PLC and PLD as well as a small but nonsignificant increase in PLA2 activity. Peritoneal dialysis effluent alone failed to stimulate either PLC or PLD, while pre-incubation with PDE had no affect upon fMLP-induced PLC and PLD activation. However, PDE caused a small but nonsignificant increase in PLA2 activity (which was comparable to that observed with fMLP) and primed the fMLP-induced response. In common with a role for PLA2 and the subsequent release of arachidonic acid (AA), we have demonstrated dose-dependent inhibition of PDE-induced superoxide release by the PLA2 inhibitor mepacrine, as well as activation and priming of the fMLP-induced superoxide generation by AA. Conclusions These results imply that PDE-induced NADPH-oxidase activation and priming in human neutrophils is mediated via a PLA2-dependent but PLC and PLD-independent mechanism.

scholarly journals Studies on the mechanism of superoxide release from human neutrophils stimulated with arachidonate.

1984 ◽  
Vol 259 (19) ◽  
pp. 11851-11857
Author(s):  
J T Curnutte ◽  
J A Badwey ◽  
J M Robinson ◽  
M J Karnovsky ◽  
M L Karnovsky
Keyword(s):  
Human Neutrophils ◽  
Superoxide Release

scholarly journals Farnesyl-L-cysteine analogs can inhibit or initiate superoxide release by human neutrophils

1994 ◽  
Vol 269 (24) ◽  
pp. 16837-16844
Author(s):  
J. Ding ◽  
D.J. Lu ◽  
D. Pérez-Sala ◽  
Y.T. Ma ◽  
J.F. Maddox ◽  
...  
Keyword(s):  
Human Neutrophils ◽  
Superoxide Release

scholarly journals Chemotactic factor enhancement of superoxide release from fluoride and phorbol myristate acetate stimulated neutrophils

Blood ◽  
1981 ◽  
Vol 58 (1) ◽  
pp. 129-134 ◽  
Author(s):  
D English ◽  
JS Roloff ◽  
JN Lukens
Keyword(s):  
Phorbol Myristate Acetate ◽  
Normal Serum ◽  
Human Neutrophils ◽  
Chemotactic Peptide ◽  
Myristate Acetate ◽  
Chemotactic Peptides ◽  
Extracellular Glucose ◽  
Increased Activity ◽  
Generating System ◽  
Superoxide Release

Abstract Human neutrophils exposed to chemotactic concentrations of zymosan- activated serum (ZAS) and a formylated chemotactic peptide (FMLP, 10(- 7)--10(-9) M) were markedly enhanced in their ability to generate superoxide (O2-) upon stimulation with either sodium fluoride or phorbol myristate acetate (PMA). For both fluoride and PMA, enhancement was characterized by a decrease in the lag from stimulation to initiation of superoxide release and by an increase in the rate of superoxide generation--representing faster activation and increased activity of O2- generating enzyme, respectively. Chemotactic concentrations of casein, normal serum, and casein-treated serum enhanced the activity, but not the rate of activation, of the fluoride- stimulated superoxide generating system. This effect on activity was not so impressive as that obtained with FMLP or ZAS. The mechanisms by which FMLP enhanced responsiveness to fluoride and PMA were found to be different. Optimal enhancement for fluoride-stimulated responses required extracellular Ca++. Extracellular glucose, but not extracellular Ca++, was required for enhancement of FMLP of PMA- stimulated responses. A similar glucose requirement could not be demonstrated for chemotactic peptide enhancement of the superoxide- generating system stimulated by fluoride. Fluoride and PMA apparently activate the neutrophil O2- generating enzyme by pathways that are not identical. However, responsiveness of the enzyme to both agents is susceptible to modulation by cellular responses to chemotactic peptides.

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