Neutrophil activation by surface bound IgG is via a pertussis toxin insensitive G protein

Pre-treatment of neutrophils with either pertussis or cholera toxins does not inhibit neutrophil activation by surface bound IgG. In contrast, pretreatment with the phorbol ester, phorbol myristate acetate, results in a dose dependent inhibition of degranulation by surface bound IgG. This inhibition...

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Veröffentlicht in:Biochemical and biophysical research communications 1989-11, Vol.164 (3), p.983-989
Hauptverfasser: Blackburn, Warren D., Heck, Louis W.
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Heck, Louis W.
description Pre-treatment of neutrophils with either pertussis or cholera toxins does not inhibit neutrophil activation by surface bound IgG. In contrast, pretreatment with the phorbol ester, phorbol myristate acetate, results in a dose dependent inhibition of degranulation by surface bound IgG. This inhibition is similar to that seen with soluble ligands where it is thought to be due to interference with the interaction of an activated guanine nucleotide binding protein with phospholipase C (J. Biol. Chem., 262 , 6121, 1987). More directly, GTP binding and GTPase activity are enhanced when human neutrophil membranes are incubated in wells containing surface bound IgG. Neither of these G protein functions were inhibited when membranes were prepared in the presence of pertussis toxin, suggesting that neutrophil activation by surface bound IgG proceeds by a mechanism that involves a pertussis toxin insensitive G protein.
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subjects Adult
Cell Membrane - immunology
Cell Membrane - metabolism
Cholera Toxin - pharmacology
GTP Phosphohydrolases - blood
GTP-Binding Proteins - blood
Humans
Immunoglobulin G - physiology
In Vitro Techniques
Kinetics
Lactoferrin - blood
Neutrophils - immunology
Neutrophils - physiology
Pertussis Toxin
Receptors, Antigen, B-Cell - physiology
Superoxides - blood
Tetradecanoylphorbol Acetate - pharmacology
Virulence Factors, Bordetella - pharmacology
title Neutrophil activation by surface bound IgG is via a pertussis toxin insensitive G protein
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