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RD Nelson, JM Gracyk, VD Fiegel, MJ Herron and DE Chenoweth
The antiinflammatory drug, phenylbutazone (PBZ), has been studied in terms
of its influence on chemotactic deactivation of human neutrophils. When PBZ
was present during the time of preincubation of cells with
N-formyl-methionyl-phenylalanine (F-Met-Phe), loss of subsequent
spontaneous mobility and chemotactic responsivity to F-Met- Phe did not
occur. The action of PBZ to protect neutrophils from peptide-mediated
chemotactic deactivation was found to involve in part its inhibitory
influence on hexose monophosphate shunt activity and in part its
antagonistic effect on interaction of peptide receptors with N- formyl
peptide. Phenylbutazone interfered with binding of N-formyl-
methionyl-leucyl-[3H]phenylalanine but not [125I]C5a to the neutrophil,
displaced labeled tripeptide bound in the absence of PBZ, increased the
dissociation constant (KD) for labeled tripeptide, and limited down
regulation of peptide receptor function. These results provide an example
of drug-mediated modulation of the interaction of neutrophils with N-formyl
peptide and strongly support the possibility that PBZ interacts directly
and specifically with the human neutrophil peptide receptor as a
competitive antagonist. They also provide an additional example of a
compound outside of th N-formyl peptide series that interacts with the
peptide receptor.
This article has been cited by other articles:
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| Copyright © 1981 by American Society of Hematology Online ISSN: 1528-0020 | |||||||||
